Bacterial sulfoquinovose catabolism (sulfoglycolysis and sulfo-SMO)

A reusable bacterial module for breakdown of sulfoquinovose (SQ; 6-deoxy-6-sulfo-D-glucose), the polar head group of the plant and cyanobacterial sulfolipid sulfoquinovosyl diacylglycerol. An optional glycoside hydrolase first releases free SQ from sulfoquinovosyl glycerides. SQ is then consumed by one of several alternative, biochemically characterized routes. Three C-C bond cleavage (sulfoglycolytic) routes split the C6 sulfosugar into a non-sulfonated C3 unit used for growth and the C3 organosulfonate 3-sulfolactaldehyde (SLA), which is then reduced to 2,3-dihydroxypropane-1-sulfonate (DHPS) or oxidized to 3-sulfolactate (SL) for excretion: the sulfo-EMP route (SQ isomerase, sulfofructose kinase, sulfofructose-1-phosphate aldolase), the sulfo-ED route (SQ dehydrogenase, sulfogluconolactonase, sulfogluconate dehydratase, KDSG aldolase), and the sulfo-SFT route (SQ isomerase and sulfofructose transaldolase). In the oxidative sulfo-SMO route a two-component flavin-dependent SQ monooxygenase cleaves the C-S bond, releasing sulfite and 6-dehydroglucose, which is reduced to glucose so that all six carbons are used. Uptake, regulation, and downstream mineralization of DHPS, SL or sulfite by other enzymes or community members are outside the module boundary.

MODULE:bacterial_sulfoquinovose_catabolismCOMPLETECONCRETEMetabolic Pathwaymodules/bacterial_sulfoquinovose_catabolism.yaml
6-sulfoquinovose(1-) catabolic processGO:1902777
PMID:41676062
Advances in microbial sulfoquinovose catabolism.
Trigger review. Summarizes the C-S cleavage (sulfo-ASMO/SMO, sulfo-ASDO) and C-C cleavage (sulfo-EMP, sulfo-ED, sulfo-TAL/SFT, sulfo-TK) routes for SQ degradation and their short-chain sulfonate products; used to set the module boundary and the axis of route variation, with each modeled step grounded in primary literature below.
Microorganisms employ two principal classes of catabolic pathways to degrade SQ: (i) C-S bond cleavage pathways, including the sulfo-ASMO (alkanesulfonate monooxygenase-dependent) and sulfo-ASDO (alkanesulfonate dioxygenase-dependent) pathways, which release glucose and sulfite; and (ii) C-C bond cleavage pathways, including sulfo-EMP
PMID:41676062
Advances in microbial sulfoquinovose catabolism.
SQ degradation pathways are so far known only from bacteria, supporting a Bacteria-scoped module.
Currently, all known SQ degradation pathways are restricted to bacteria and no characterized pathways exist in eukaryotes or archaea

Boundary decision. The routes share one input (SQ, released by an optional sulfoquinovosidase) and one ecological role (use of the sulfosugar as carbon and energy source), but no route-defining enzyme is shared across all of them; SQ isomerase is shared only by sulfo-EMP and sulfo-SFT, and SLA dehydrogenase only by sulfo-ED and sulfo-SFT. They are therefore modeled as alternative implementations in a single route variant_set (selection ONE_OR_MORE, because some bacteria carry more than one route) rather than as four standalone modules, with each variant carrying its own ordered parts and connections. The terminal SLA reduction or oxidation is modeled inside each route with the enzyme documented for that route's exemplar organism; the same SLA-redox alternatives recur across routes (for example, Arthrobacter sulfo-EMP clusters use an SLA dehydrogenase instead of YihU, and anaerobic sulfo-SFT clusters use an SLA reductase instead of SftD/SlaB), as summarized in PMID:41676062 and PMID:32919372. Not modeled: the sulfo-ASDO route (Fe(II)/2-oxoglutarate-dependent SQ dioxygenase SqoD) and the sulfo-TK route (SF transketolase SqwGH), which have fewer characterized reference proteins in UniProtKB; the EMP2-specific kinase and aldolase SqiK and SqiA of the sulfo-EMP2 variant (its isomerase SqvD is shared with sulfo-SFT and is modeled there); the SQ mutarotases YihR/SqvB (EC 5.1.3.43, RHEA:59228), because no UniProtKB entry carries that activity (E. coli YihR, P32139, is still named "Uncharacterized protein YihR") and GO has no term mapped to RHEA:59228, so the alpha-to-beta anomer step is recorded on the top-level connection instead; SQ and sulfoquinovosyl glyceride uptake systems (YihO, SmoEFGH); the transcriptional repressor CsqR; and downstream desulfonation of DHPS, SL, isethionate or 3-sulfopropionate (HpsGH, SuyAB, IseG, HpfG and related enzymes), which is a distinct community-level module. Reaction chaining across the non-CoA sulfosugar intermediates was checked manually against the cited Rhea equations. Ontology gaps noted for GO editors: GO has specific molecular-function terms only for the sulfo-EMP reactions (GO:0061593, GO:0061594, GO:0061595, GO:0061596) and for sulfoquinovosidase (GO:1990929); the sulfo-ED (EC 1.1.1.390, 3.1.1.99, 4.2.1.162, 4.1.2.58), sulfo-SFT (EC 2.2.1.14), SQ monooxygenase (EC 1.14.14.181) and 6-dehydroglucose reductase (EC 1.1.1.432) reactions have Rhea entries but no rhea2go/ec2go mapping, so their annotons use the nearest existing parent GO term with the exact Rhea reaction as evidence. GO:0061722 sulphoglycolysis (is_a GO:1902777) is defined as "The chemical reactions and pathways resulting in the breakdown of 6-sulfoquinovose(1-) resulting in the formation of glycerone phosphate (DHAP) and pyruvate." (OLS, checked 2026-10-10). That covers the DHAP-forming sulfo-EMP route and the pyruvate-forming sulfo-ED route, but not the F6P-forming sulfo-SFT route or the sulfite-releasing sulfo-SMO route; the root concept therefore uses the broader parent GO:1902777. Adjacency. The SmoC/SmoA step is an SQ-specific instance of the two-component reduced-flavin desulfonation motif modeled abstractly in modules/bacterial_alkanesulfonate_uptake_desulfonation.yaml (ssued_desulfonation): SmoA fills the reductase tier (GO:0052874 FMN reductase, NADH) and SmoC the oxygenase tier (GO:0008726), differing from the SsuE/SsuD abstract motif only in the SQ-specific substrate and the NADH versus NADPH reductase cofactor. A formal conforms_to is not declared because this module collapses the two-component system into one reaction node rather than the template's two parts, but that module covers promiscuous SsuD/SsuE alkanesulfonate desulfonation, so there is no overlap in members. Downstream desulfonation of DHPS, SL and sulfite is left to community-level modules as stated above. Family grounding. Every member protein's PANTHER family has a family review under interpro/panther/ (PTHR46959, PTHR15108, PTHR10584, PTHR39340, PTHR22981, PTHR43639, PTHR10907, PTHR43183, PTHR30502, PTHR43353, PTHR36120, PTHR10683, PTHR42991, PTHR42847, PTHR30466, PTHR43364). Where a verified subfamily holds all representative members the annoton names it (PTHR46959:SF2, PTHR10584:SF157, PTHR39340:SF1, PTHR43639:SF1, PTHR43183:SF2, PTHR43353:SF5, PTHR36120:SF1, PTHR10683:SF40, PTHR42991:SF1, PTHR42847:SF4, PTHR30466:SF11, PTHR43364:SF1); the YihS, YihU, lactonase and KDSG aldolase steps keep the family id (PTHR15108, PTHR22981, PTHR10907, PTHR30502) as a membership record. Four family descriptors raise a FAMILY_FUNCTION_UNREVIEWED notice because their family reviews deliberately leave the step's activity UNRESOLVED at family or subfamily level: YihS (PTHR15108 has no subfamily for the enterobacterial YihS clade), YihT (PTHR39340:SF1 also holds Firmicutes LacD tagatose-1,6-bisphosphate aldolases), YihU (PTHR22981:SF7 also holds the 3-hydroxyisobutyrate dehydrogenases) and SmoA (PTHR30466:SF11 members differ in flavin and reductant preference). The verified ids are kept because they record membership; the activity itself rests on the representative members' gene reviews and, for YihS and YihV, on the PAINT nodes PTN001431668 and PTN000061922 cited on those annotons. PAINT nodes considered and not cited: PTN000541321 (PTHR22981 root) and PTN002462421 (PTHR43639 root) assert only generic oxidoreductase parents of the annotons' functions; PTN008681047 (PTHR43353) propagates succinate-semialdehyde dehydrogenase activity, which is only an in vitro activity of the SLA dehydrogenase PpSQ1_00395 and is judged NEEDS_PRUNING in the PTHR43353 family review; PTN002217485 (PTHR39340) and PTN000768559 (PTHR42847) are judged too deep in their family reviews. Representative members were not extended to Escherichia coli YgfF, human ALDH5A1 or Pseudomonas putida KT2440 SsuD, which do not perform the reactions of the steps concerned. Module-level deep research was not generated (the provider client could not run in the curation environment); the module rests on the cited primary literature and on the member gene reviews.

21Nodes
16Parts
1Variant Sets
4Variants
16Annotons
11Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:bacterial_sulfoquinovose_catabolism deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ every leaf node grounds to a representative protein.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Function consistency and core coverage

22 gene-function check(s) reflected in core functions · 0 conflict(s) · 4 evidence or coverage gap(s) (38 comparison(s))

Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.

AnnotonParticipantFunctionAssessment
sulfoquinovosidase YihQ (Escherichia coli K-12)
UniProtKB:P32138
Family Representative
sulfoquinovosidase activity
GO:1990929
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sulfoquinovosidase SmoI (Agrobacterium fabrum C58)
UniProtKB:A9CEZ0
Family Representative
sulfoquinovosidase activity
GO:1990929
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
yihs_sq_isomerase YihS (Escherichia coli K-12)
UniProtKB:P32140
Family Representative
sulfoquinovose isomerase activity
GO:0061593
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
yihv_sf_kinase YihV (Escherichia coli K-12)
UniProtKB:P32143
Family Representative
6-deoxy-6-sulfofructose kinase activity
GO:0061594
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
yiht_sfp_aldolase YihT (Escherichia coli K-12)
UniProtKB:P32141
Family Representative
6-deoxy-6-sulfofructose-1-phosphate aldolase activity
GO:0061595
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
yihu_sla_reductase YihU (Escherichia coli K-12)
UniProtKB:P0A9V8
Family Representative
3-sulfolactaldehyde reductase activity
GO:0061596
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
ed_sq_dehydrogenase PpSQ1_00405 (Pseudomonas putida SQ1 SQ dehydrogenase)
UniProtKB:P0DOV5
Family Representative
sulfoquinovose 1-dehydrogenase (NAD+) activity (EC 1.1.1.390)
GO:0016616
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
ed_sgl_lactonase PpSQ1_00410 (Pseudomonas putida SQ1 SGL lactonase)
UniProtKB:P0DOV6
Family Representative
6-deoxy-6-sulfogluconolactonase activity (EC 3.1.1.99)
GO:0052689
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
ed_sg_dehydratase PpSQ1_00400 (Pseudomonas putida SQ1 SG dehydratase)
UniProtKB:P0DOV7
Family Representative
6-deoxy-6-sulfo-D-gluconate dehydratase activity (EC 4.2.1.162)
GO:0016836
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
ed_kdsg_aldolase PpSQ1_00455 (Pseudomonas putida SQ1 KDSG aldolase)
UniProtKB:P0DOV8
Family Representative
KDSG aldolase activity (EC 4.1.2.58)
GO:0016832
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
ed_sla_dehydrogenase PpSQ1_00395 (Pseudomonas putida SQ1 SLA dehydrogenase)
UniProtKB:P0DOV9
Family Representative
aldehyde dehydrogenase (NAD+) activity
GO:0004029
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sqvd_sq_isomerase SqvD (Bacillus megaterium)
UniProtKB:D5E1S9
Family Representative
sulfoquinovose isomerase activity
GO:0061593
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sqvd_sq_isomerase SftI (Bacillus aryabhattai)
UniProtKB:A0A7W3RDA3
Family Representative
sulfoquinovose isomerase activity
GO:0061593
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sqva_sf_transaldolase SqvA (Bacillus megaterium)
UniProtKB:D5E1T2
Family Representative
6-deoxy-6-sulfo-D-fructose transaldolase activity (EC 2.2.1.14)
GO:0016744
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sqva_sf_transaldolase SftT (Bacillus aryabhattai)
UniProtKB:A0A7W3N5X5
Family Representative
6-deoxy-6-sulfo-D-fructose transaldolase activity (EC 2.2.1.14)
GO:0016744
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sft_sla_dehydrogenase SlaB (Bacillus megaterium)
UniProtKB:D5E1S7
Family Representative
aldehyde dehydrogenase (NAD+) activity
GO:0004029
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sft_sla_dehydrogenase SftD (Bacillus aryabhattai)
UniProtKB:A0A7W3RCJ3
Family Representative
aldehyde dehydrogenase (NAD+) activity
GO:0004029
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
smoc_sq_monooxygenase SmoC (Agrobacterium fabrum C58)
UniProtKB:A9CEY7
Family Representative
sulfoquinovose monooxygenase activity (EC 1.14.14.181)
GO:0008726
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
smoc_sq_monooxygenase SquD (Novosphingobium aromaticivorans)
UniProtKB:Q2G5J4
Family Representative
sulfoquinovose monooxygenase activity (EC 1.14.14.181)
GO:0008726
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
smoa_flavin_reductase SmoA (Agrobacterium fabrum C58)
UniProtKB:Q7CS24
Family Representative
FMN reductase (NADH) activity
GO:0052874
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
smob_dehydroglucose_reductase SmoB (Agrobacterium fabrum C58)
UniProtKB:A9CEY6
Family Representative
6-dehydroglucose reductase activity (EC 1.1.1.432)
GO:0016616
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
smob_dehydroglucose_reductase SquF (Novosphingobium aromaticivorans)
UniProtKB:Q2G5J3
Family Representative
6-dehydroglucose reductase activity (EC 1.1.1.432)
GO:0016616
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
sulfoquinovosidase GH31 sulfoquinovosidases
PANTHER:PTHR46959:SF2
Family
sulfoquinovosidase activity
GO:1990929
Family Supported
Family review supports GO:1990929 FAMILY_WIDE. Both characterized members, the only SwissProt members of the family, are sulfoquinovosidases, and the activity is tied to the sulfonate-binding triad that the family shares. The GO definition names SQDG as substrate, whereas SmoI was assayed on SQGro and PNPSQ; both glycosides are cleaved at the same bond, and a question to broaden the definition is raised in the SmoI gene review.
yihs_sq_isomerase YihS-type sulfoquinovose isomerase
PANTHER:PTHR15108
Family
sulfoquinovose isomerase activity
GO:0061593
Family Function Unreviewed
Family review leaves GO:0061593 UNRESOLVED. The activity belongs to the enterobacterial YihS clade (PAINT node PTN001431668), not to the family. PANTHER defines no subfamily for this clade, so no subfamily can be named, and no curated residue site is recorded here; membership of an uncharacterized protein in the clade must be decided from the PAINT node or from the HAMAP SQ_isomerase rule (MF_00998).
yihv_sf_kinase YihV-type sulfofructose kinase
PANTHER:PTHR10584:SF157
Family
6-deoxy-6-sulfofructose kinase activity
GO:0061594
Family Supported
Family review supports GO:0061594 for PANTHER:PTHR10584:SF157. Holds for the sulfofructose kinase clade (PAINT PTN000061922) and PANTHER subfamily SF157. Every reviewed SF157 member in the local inventory was checked; the only one is YihV, directly assayed. It must not descend family-wide, because the ribokinase, nucleoside kinase, KdgK and KHK clades phosphorylate other substrates.
yiht_sfp_aldolase YihT-type class I SFP aldolase
PANTHER:PTHR39340:SF1
Family
6-deoxy-6-sulfofructose-1-phosphate aldolase activity
GO:0061595
Family Function Unreviewed
Family review leaves GO:0061595 UNRESOLVED. True for the five YihT members, not established for the 42 LacD members, and PANTHER's only subfamily (SF1) contains both groups, so no subfamily scope can be stated. A residue-determined scope based on the YihT sulfonate pocket (Arg253 and the phosphate-binding Ser226/Ser227 of Salmonella YihT, PMID:33791429) is plausible but has not been curated as a residue site here; until then the term should be carried by the YihT clade node or the HAMAP SFP_aldolase rule (MF_01912), not by family or SF1 membership.
yihu_sla_reductase YihU-type NADH-dependent SLA reductase
PANTHER:PTHR22981
Family
3-sulfolactaldehyde reductase activity
GO:0061596
Family Function Unreviewed
Family review leaves GO:0061596 UNRESOLVED. True for the three enterobacterial YihU members (E. coli P0A9V8, Shigella P0A9V9, Salmonella Q9L7S0); not established for the 17 other reviewed members, all of which share subfamily SF7 with YihU. No PANTHER subfamily or PAINT node isolates the YihU clade, so no subfamily scope can be stated; until a YihU-clade node or a curated residue site exists, the term should be carried by the HAMAP SLA_reductase rule (MF_01913) and InterPro IPR030876, not by family or SF7 membership.
ed_sq_dehydrogenase sulfo-ED NAD+-dependent SQ dehydrogenase
PANTHER:PTHR43639:SF1
Family
sulfoquinovose 1-dehydrogenase (NAD+) activity (EC 1.1.1.390)
GO:0016616
Family Supported
Family review supports GO:0016616 for PANTHER:PTHR43639:SF1. Holds for the CH-OH dehydrogenases that dominate SF1: the sugar 1-dehydrogenases, the P. putida sulfoquinovose 1-dehydrogenase (directly assayed), diol and alcohol dehydrogenases and the keto reductases that act on the reverse direction of a CH-OH oxidation. SF1 is mixed, so members whose curated reactions reduce C=N (PTR1) or C=C bonds (FabL, ChcA) are excepted by name. The uncharacterized SF1 members (for example Rv0927c and MexAM1_META1p0182) are neither supported nor excluded and carry no exception entry. SF6 (FolM pterin reductases) is outside the scope.
ed_sgl_lactonase sulfo-ED SGL lactonase
PANTHER:PTHR10907
Family
6-deoxy-6-sulfogluconolactonase activity (EC 3.1.1.99)
GO:0052689
Family Supported
Family review supports GO:0052689 FAMILY_WIDE. Lactone hydrolysis is the activity shared by every characterized member: regucalcin (gluconolactone), XylC (D-xylonolactone), AraB (L-arabinolactone), XacC (pentonolactones) and the P. putida SQ1 enzyme (6-deoxy-6-sulfogluconolactone). The parent ester-hydrolase term is therefore the family-level function; the substrate-specific child must be set per member, which is why the sulfo-ED annoton uses this term and the gluconolactonase term is not transferred to P0DOV6.
ed_sg_dehydratase sulfo-ED SG dehydratase
PANTHER:PTHR43183:SF2
Family
6-deoxy-6-sulfo-D-gluconate dehydratase activity (EC 4.2.1.162)
GO:0016836
Family Supported
Family review supports GO:0016836 FAMILY_WIDE. Every characterized member is a sugar-acid dehydratase (L-arabinonate, D-xylonate or 6-deoxy-6-sulfo-D-gluconate), so the generic hydro-lyase parent holds family-wide. GO has no term for the sulfogluconate reaction (EC 4.2.1.162), so this is also the term used for the sulfo-ED annoton; the substrate-specific pentonate dehydratase terms must not be transferred to SF2.
ed_kdsg_aldolase sulfo-ED KDSG aldolase
PANTHER:PTHR30502
Family
KDSG aldolase activity (EC 4.1.2.58)
GO:0016832
Family Supported
Family review supports GO:0016832 FAMILY_WIDE. The family's characterized members are retro-aldol pyruvate aldolases that release an aldehyde (EC 4.1.2 class), as the root IBD asserts; this is also the term the sulfo-ED KDSG aldolase annoton uses, because GO has no KDSG aldolase term. TasA, whose product is an oxo acid, is excepted.
ed_sla_dehydrogenase NAD(P)+-dependent SLA dehydrogenase
PANTHER:PTHR43353:SF5
Family
aldehyde dehydrogenase (NAD+) activity
GO:0004029
Family Supported
Family review supports GO:0004029 for PANTHER:PTHR43353:SF5. NAD+-dependent oxidation of an aldehyde to its carboxylate is established for most SF5 members, whatever their aldehyde: the SSADHs ALDH5A1, ALDH5F1, UGA2, ssd1, Paenarthrobacter Sad and Acinetobacter TgnE, lactaldehyde dehydrogenase AldA, alpha-ketoglutaric semialdehyde dehydrogenase AraE, 3,6-anhydro-L-galactose dehydrogenase Vejahgd, the 4-formylbenzenesulfonate dehydrogenases TsaD1/TsaD2, the AstD N-succinylglutamate semialdehyde dehydrogenases and the P. putida SQ1 3-sulfolactaldehyde dehydrogenase P0DOV9 (RHEA:47932), for which this term is the rhea2go mapping and the sulfo-ED module's function. Each of the 35 SF5 inventory members was checked against its UniProt catalytic-activity annotation; the ten members for which only an NADP+-linked reaction is curated are excepted by name, because the cofactor is not predicted by membership. SF3 and SF12 were not assessed.
sqvd_sq_isomerase SqvD-type sulfoquinovose isomerase
PANTHER:PTHR36120:SF1
Family
sulfoquinovose isomerase activity
GO:0061593
Family Supported
Family review supports GO:0061593 for PANTHER:PTHR36120:SF1. Directly assayed for SftI (13C6-SQ converted to 13C6-SF by the purified enzyme) and recorded with experimental evidence for SqvD; the remaining SF1 members are the SqvD isomerases of sulfo-TK and sulfo-EMP2 gene clusters. Restricted to SF1 because SF2 has no characterized member.
sqva_sf_transaldolase sulfofructose transaldolase
PANTHER:PTHR10683:SF40
Family
6-deoxy-6-sulfo-D-fructose transaldolase activity (EC 2.2.1.14)
GO:0016744
Family Supported
Family review supports GO:0016744 FAMILY_WIDE. Group transfer of the dihydroxyacetone unit from a ketose donor to an aldose acceptor is shared by the classical transaldolases of SF18, SF36, SF31 and SF16, by the type-3 transaldolases of SF40, and by the SF40 sulfofructose transaldolases SqvA and SftT, for which no specific GO term exists (EC 2.2.1.14); GO:0016744 is the term their gene reviews and the sulfoquinovose catabolism module use. Parsing the member inventory shows that every member outside the fructose-6-phosphate aldolases is named as a transaldolase, so the term is recorded family-wide. The 24 SF40 fructose-6-phosphate aldolases and the 2 probable fructose-6-phosphate aldolases that make up SF28 are acceptor-independent aldolases and are excepted by name. The narrower GO:0004801 transaldolase activity keeps its own SUBFAMILY_ONLY assessment above.
sft_sla_dehydrogenase Firmicutes NAD+-dependent SLA dehydrogenase
PANTHER:PTHR42991:SF1
Family
aldehyde dehydrogenase (NAD+) activity
GO:0004029
Family Supported
Family review supports GO:0004029 for PANTHER:PTHR42991:SF1. The NAD+-specific aldehyde dehydrogenase term is the parent used for the SLA dehydrogenase step, for which GO has no specific term (EC 1.2.1.97). It holds for the NAD+-dependent members of SF1: the SLA dehydrogenases SlaB (RHEA:47932 recorded with experimental evidence) and SftD (assayed with NAD+), and plausibly the lactaldehyde, sulfoacetaldehyde and phosphonoacetaldehyde dehydrogenases. It does not hold for the NADP-dependent GapN enzymes of plants, green algae and streptococci, which are excepted by name. The aspartate-semialdehyde dehydrogenases and the uncharacterized y4uC are left without an exception entry because their cofactor use is not established in the committed data. Because SF1 is substrate-heterogeneous, a module that needs the SLA dehydrogenase step should select members by function or gene-cluster context, not by SF1 membership alone.
smoc_sq_monooxygenase SQ-specific luciferase-like monooxygenase
PANTHER:PTHR42847:SF4
Family
sulfoquinovose monooxygenase activity (EC 1.14.14.181)
GO:0008726
Family Supported
Family review supports GO:0008726 for PANTHER:PTHR42847:SF4. The term holds for the SsuD orthologs of SF4, which are directly assayed in E. coli and genetically grounded in P. putida, and is defensible for MsuD, since methanesulfonate is itself an alkanesulfonate. It also holds for the sulfoquinovose monooxygenases SmoC and SquD: their reaction (RHEA:70775) is the GO:0008726 transformation applied to the primary alkyl sulfonate at C6 of sulfoquinovose, so they are not exceptions, although their substrate range is far narrower than SsuD's and a child term "sulfoquinovose monooxygenase activity" is proposed in their gene reviews. It is not family-wide: SF4 is the only populated subfamily and also contains RutA, whose substrate is uracil, so the scope is recorded here as this subfamily with RutA excepted by name. The uncharacterized actinobacterial and fungal members of the subfamily are neither supported nor excluded; they are left without an exception entry because no evidence places them on either side, and a member-level assertion should not be manufactured from silence.
smoa_flavin_reductase sulfo-SMO cluster flavin reductase
PANTHER:PTHR30466:SF11
Family
FMN reductase (NADH) activity
GO:0052874
Family Function Unreviewed
Family review leaves GO:0052874 UNRESOLVED. NADH-dependent FMN reduction is established for SmoA (SF11) and is the activity named for RutF (SF1), but family members differ in flavin (the inventory also names members such as "NADH-dependent FAD reductase" and "NADH:FAD oxidoreductase") and reductant preference, and most members are unassayed; no subfamily can be shown to be uniform for this specific term.
smob_dehydroglucose_reductase sulfo-SMO 6-dehydroglucose reductase
PANTHER:PTHR43364:SF1
Family
6-dehydroglucose reductase activity (EC 1.1.1.432)
GO:0016616
Family Supported
Family review supports GO:0016616 FAMILY_WIDE. NAD(P)H-dependent interconversion of a carbonyl and an alcohol on the AKR scaffold is the family's shared chemistry; it is the most specific GO term that holds for the characterized SF1 members SmoB and SquF, whose EC 1.1.1.432 activity has no GO term yet.

Gene-review completeness (22/22 grounded genes reviewed)

22 complete review(s) · 0 with deep research · 0 missing review · 22 reviewed but lacking deep research

Gene Review Complete Deep research
PpSQ1_00395 P0DOV9 ✓ ✓ ✗
PpSQ1_00400 P0DOV7 ✓ ✓ ✗
PpSQ1_00405 P0DOV5 ✓ ✓ ✗
PpSQ1_00410 P0DOV6 ✓ ✓ ✗
PpSQ1_00455 P0DOV8 ✓ ✓ ✗
sftD A0A7W3RCJ3 ✓ ✓ ✗
sftI A0A7W3RDA3 ✓ ✓ ✗
sftT A0A7W3N5X5 ✓ ✓ ✗
slaB D5E1S7 ✓ ✓ ✗
smoA Q7CS24 ✓ ✓ ✗
smoB A9CEY6 ✓ ✓ ✗
smoC A9CEY7 ✓ ✓ ✗
smoI A9CEZ0 ✓ ✓ ✗
squD Q2G5J4 ✓ ✓ ✗
squF Q2G5J3 ✓ ✓ ✗
sqvA D5E1T2 ✓ ✓ ✗
sqvD D5E1S9 ✓ ✓ ✗
yihQ P32138 ✓ ✓ ✗
yihS P32140 ✓ ✓ ✗
yihT P32141 ✓ ✓ ✗
yihU P0A9V8 ✓ ✓ ✗
yihV P32143 ✓ ✓ ✗

Details

Context
bacteriaNCBITaxon:2
Bacterial sulfoquinovose catabolismMetabolic Pathwaybacterial_sulfoquinovose_catabolism
6-sulfoquinovose(1-) catabolic processGO:1902777
Context
bacteriaNCBITaxon:2

Connections

Sulfoquinovosidase supplies free SQ to whichever catabolic route the organism carries.
Part 1: optional release of free sulfoquinovose from sulfoquinovosyl glycosides (optional)
Sulfoquinovosidase release of sulfoquinovoseReactionsq_glycoside_hydrolysis

Annotons

Sulfoquinovosidase (YihQ/SmoI type)
sulfoquinovosidase
Participant: Family: GH31 sulfoquinovosidases
Family:
GH31 sulfoquinovosidasesPANTHER:PTHR46959:SF2 Glycoside hydrolase family 31 sulfoquinovosidases with a sulfonate-binding pocket. Other sulfoquinovosidase families (for example GH188) are known but not represented here.
Representative Members: YihQ (Escherichia coli K-12)UniProtKB:P32138 SmoI (Agrobacterium fabrum C58)UniProtKB:A9CEZ0
Required Function:
sulfoquinovosidase activityGO:1990929

Function

sulfoquinovosidase activityGO:1990929
Substrates: sulfoquinovosyl glycerol or sulfoquinovosyl diacylglycerol water
Products: 6-sulfo-alpha-D-quinovose glycerol or 1,2-diacyl-sn-glycerol

Processes

glycoside catabolic processGO:0016139

Hydrolyzes the alpha-glycosidic bond of sulfoquinovosyl glycerides to supply free SQ. Optional because free SQ can also be taken up directly and some sulfo-EMP organisms lack a YihQ ortholog.

PMID:26878550
YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids.
E. coli YihQ is a dedicated sulfoquinovosidase upstream of sulfoglycolysis.
We have identified Escherichia coli YihQ as the first dedicated sulfoquinovosidase and the gateway enzyme to sulfoglycolytic pathways.
PMID:35074914
Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.
In the sulfo-SMO cluster, SmoI hydrolyzes SQGro before C-S cleavage, because SmoC does not act on the glycoside.
As such, the hydrolysis of SQGro by SmoI necessarily precedes oxidative desulfurization by SmoC.
Part 2: route-specific catabolism of free sulfoquinovose
Alternative sulfoquinovose catabolic routesMetabolic Pathwaysq_catabolic_routes
Variant set: Sulfoquinovose catabolic route by bond cleaved and enzyme set (C-C cleavage by aldolase or transaldolase versus oxidative C-S cleavage) (One Or More)
PMID:41676062
Advances in microbial sulfoquinovose catabolism.
C-C cleavage routes yield C3 organosulfonates that must be desulfonated separately, whereas C-S cleavage routes release sulfite directly.
For the C-S bond cleavage pathways, SQ is directly desulfurized to yield glucose, which can be further metabolized via glycolysis or other pathways. In contrast, C-C bond cleavage pathways produce short-chain sulfonated carbohydrates, which require additional desulfurization or further degradation steps.
Sulfo-EMP route (YihS-YihV-YihT-YihU)Metabolic Pathwaysulfo_emp_route

Embden-Meyerhof-like sulfoglycolysis characterized in Escherichia coli K-12: SQ is isomerized to 6-deoxy-6-sulfofructose (SF), phosphorylated to SF 1-phosphate (SFP), and split by an aldolase into DHAP and SLA; SLA is reduced to DHPS for excretion.

sulphoglycolysisGO:0061722
PMID:24463506
Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle.
The four sulfo-EMP reactions were established with purified E. coli enzymes; DHAP supports growth and DHPS is excreted.
SQ is catabolised through four newly discovered reactions that we established using purified, heterologously expressed enzymes: SQ isomerase, 6-deoxy-6-sulphofructose (SF) kinase, 6-deoxy-6-sulphofructose-1-phosphate (SFP) aldolase, and 3-sulpholactaldehyde (SLA) reductase.
PMID:33791429
Molecular Basis of Sulfosugar Selectivity in Sulfoglycolysis.
Structural and kinetic analysis shows the three core sulfo-EMP enzymes are specific for sulfosugar substrates rather than glycolytic analogues.
Our data show that despite the superficial similarity of this pathway to glycolysis, the sulfoglycolytic enzymes are specific for SQ metabolites and are not catalytically active on related metabolites from glycolytic pathways.

Connections

YihS supplies 6-deoxy-6-sulfofructose to YihV.
YihV supplies sulfofructose 1-phosphate to YihT.
YihT supplies (2S)-3-sulfolactaldehyde to YihU.
Part 1: SQ to sulfofructose isomerization
YihS sulfoquinovose isomerizationReactionemp_sq_isomerization

Annotons

Sulfoquinovose isomerase (YihS)
yihs_sq_isomerase
Participant: Family: YihS-type sulfoquinovose isomerase
Family:
YihS-type sulfoquinovose isomerasePANTHER:PTHR15108
Representative Members: YihS (Escherichia coli K-12)UniProtKB:P32140
Required Function:
sulfoquinovose isomerase activityGO:0061593

Function

sulfoquinovose isomerase activityGO:0061593
Substrates: 6-sulfo-beta-D-quinovose
Products: 6-deoxy-6-sulfo-D-fructose

Processes

sulphoglycolysisGO:0061722

Aldose-ketose isomerization that commits SQ to the sulfo-EMP route; acts preferentially on the beta anomer.

Part 2: sulfofructose phosphorylation
YihV sulfofructose phosphorylationReactionemp_sf_phosphorylation

Annotons

6-deoxy-6-sulfofructose kinase (YihV)
yihv_sf_kinase
Participant: Family: YihV-type sulfofructose kinase
Family:
YihV-type sulfofructose kinasePANTHER:PTHR10584:SF157
Representative Members: YihV (Escherichia coli K-12)UniProtKB:P32143
Required Function:
6-deoxy-6-sulfofructose kinase activityGO:0061594

Function

6-deoxy-6-sulfofructose kinase activityGO:0061594
Substrates: 6-deoxy-6-sulfo-D-fructose ATP
Products: 6-deoxy-6-sulfo-D-fructose 1-phosphate ADP

Processes

sulphoglycolysisGO:0061722

ATP-dependent phosphorylation of SF; the allosterically regulated step of the route.

Part 3: sulfofructose-1-phosphate aldol cleavage
YihT sulfofructose-1-phosphate aldol cleavageReactionemp_sfp_aldol_cleavage

Annotons

Sulfofructose-1-phosphate aldolase (YihT)
yiht_sfp_aldolase
Participant: Family: YihT-type class I SFP aldolase
Family:
YihT-type class I SFP aldolasePANTHER:PTHR39340:SF1 PANTHER records membership only: subfamily SF1 also holds Firmicutes LacD tagatose-1,6-bisphosphate aldolases, so SF1 membership does not by itself imply SFP aldolase activity (see the PTHR39340 family review, where PAINT node PTN002217485 is judged too deep).
Representative Members: YihT (Escherichia coli K-12)UniProtKB:P32141
Required Function:
6-deoxy-6-sulfofructose-1-phosphate aldolase activityGO:0061595

Function

6-deoxy-6-sulfofructose-1-phosphate aldolase activityGO:0061595
Substrates: 6-deoxy-6-sulfo-D-fructose 1-phosphate
Products: (2S)-3-sulfolactaldehyde dihydroxyacetone phosphate

Processes

sulphoglycolysisGO:0061722

Splits SFP into DHAP, which enters glycolysis, and the organosulfonate SLA.

Part 4: sulfolactaldehyde reduction
YihU sulfolactaldehyde reduction to DHPSReactionemp_sla_reduction

Annotons

3-sulfolactaldehyde reductase (YihU)
yihu_sla_reductase
Participant: Family: YihU-type NADH-dependent SLA reductase
Family:
YihU-type NADH-dependent SLA reductasePANTHER:PTHR22981 PANTHER records membership only: the family, and its subfamily SF7 that holds YihU, also contain the 3-hydroxyisobutyrate dehydrogenases, so membership does not by itself imply SLA reductase activity. No PAINT node in PTHR22981 asserts GO:0061596; the root node PTN000541321 asserts only the generic parent GO:0016616 and is therefore not cited here.
Representative Members: YihU (Escherichia coli K-12)UniProtKB:P0A9V8
Required Function:
3-sulfolactaldehyde reductase activityGO:0061596

Function

3-sulfolactaldehyde reductase activityGO:0061596
Substrates: (2S)-3-sulfolactaldehyde NADH
Products: (2S)-3-sulfopropanediol (DHPS) NAD+

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Reduces SLA to DHPS, regenerating NAD+; DHPS is excreted. YihU also reduces succinic semialdehyde, a separate non-core activity.

Sulfo-ED route (SQ dehydrogenase to KDSG aldolase)Metabolic Pathwaysulfo_ed_route

Entner-Doudoroff-like sulfoglycolysis characterized in Pseudomonas putida SQ1: SQ is oxidized to 6-deoxy-6-sulfogluconolactone, hydrolyzed to 6-deoxy-6-sulfogluconate, dehydrated to 2-keto-3,6-dideoxy-6-sulfogluconate (KDSG), and split into pyruvate and SLA; SLA is oxidized to SL for excretion.

sulphoglycolysisGO:0061722
PMID:26195800
Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1.
The complete sulfo-ED pathway was reconstituted in vitro from five heterologously produced P. putida SQ1 enzymes.
It involves an NAD(+)-dependent SQ dehydrogenase, 6-deoxy-6-sulfogluconolactone (SGL) lactonase, 6-deoxy-6-sulfogluconate (SG) dehydratase, and 2-keto-3,6-dideoxy-6-sulfogluconate (KDSG) aldolase.

Connections

ed_sq_oxidation -> ed_sgl_hydrolysis Provides Input For
SQ dehydrogenase supplies SGL to the lactonase.
ed_sgl_hydrolysis -> ed_sg_dehydration Provides Input For
The lactonase supplies SG to the dehydratase.
The dehydratase supplies KDSG to the aldolase.
The aldolase supplies (2S)-SLA to SLA dehydrogenase.
Part 1: SQ oxidation
SQ dehydrogenase oxidation to sulfogluconolactoneReactioned_sq_oxidation

Annotons

Sulfoquinovose 1-dehydrogenase
ed_sq_dehydrogenase
Participant: Family: sulfo-ED NAD+-dependent SQ dehydrogenase
Family:
sulfo-ED NAD+-dependent SQ dehydrogenasePANTHER:PTHR43639:SF1
Representative Members: PpSQ1_00405 (Pseudomonas putida SQ1 SQ dehydrogenase)UniProtKB:P0DOV5

Function

sulfoquinovose 1-dehydrogenase (NAD+) activity (EC 1.1.1.390)GO:0016616
Substrates: 6-sulfo-D-quinovose NAD+
Products: 6-deoxy-6-sulfo-D-glucono-1,5-lactone NADH

Processes

sulphoglycolysisGO:0061722

NAD+-dependent oxidation of SQ at C1. No specific GO molecular-function term exists; the parent term is used with the exact Rhea reaction.

Part 2: sulfogluconolactone hydrolysis
Sulfogluconolactonase ring openingReactioned_sgl_hydrolysis

Annotons

6-deoxy-6-sulfogluconolactonase
ed_sgl_lactonase
Participant: Family: sulfo-ED SGL lactonase
Family:
sulfo-ED SGL lactonasePANTHER:PTHR10907
Representative Members: PpSQ1_00410 (Pseudomonas putida SQ1 SGL lactonase)UniProtKB:P0DOV6

Function

6-deoxy-6-sulfogluconolactonase activity (EC 3.1.1.99)GO:0052689
Substrates: 6-deoxy-6-sulfo-D-glucono-1,5-lactone water
Products: 6-deoxy-6-sulfo-D-gluconate

Processes

sulphoglycolysisGO:0061722

Hydrolyzes the lactone to the open-chain sulfogluconate. Its IEA gluconolactonase annotation names a different, non-sulfonated substrate.

Part 3: sulfogluconate dehydration
Sulfogluconate dehydratase formation of KDSGReactioned_sg_dehydration

Annotons

6-deoxy-6-sulfo-D-gluconate dehydratase
ed_sg_dehydratase
Participant: Family: sulfo-ED SG dehydratase
Family:
sulfo-ED SG dehydratasePANTHER:PTHR43183:SF2
Representative Members: PpSQ1_00400 (Pseudomonas putida SQ1 SG dehydratase)UniProtKB:P0DOV7

Function

6-deoxy-6-sulfo-D-gluconate dehydratase activity (EC 4.2.1.162)GO:0016836
Substrates: 6-deoxy-6-sulfo-D-gluconate
Products: 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate (KDSG) water

Processes

sulphoglycolysisGO:0061722

Dehydrates SG to the 2-keto-3-deoxy aldolase substrate KDSG.

Part 4: KDSG aldol cleavage
KDSG aldolase cleavage to pyruvate and SLAReactioned_kdsg_aldol_cleavage

Annotons

2-dehydro-3,6-dideoxy-6-sulfogluconate aldolase
ed_kdsg_aldolase
Participant: Family: sulfo-ED KDSG aldolase
Family:
sulfo-ED KDSG aldolasePANTHER:PTHR30502
Representative Members: PpSQ1_00455 (Pseudomonas putida SQ1 KDSG aldolase)UniProtKB:P0DOV8

Function

KDSG aldolase activity (EC 4.1.2.58)GO:0016832
Substrates: 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate (KDSG)
Products: pyruvate (2S)-3-sulfolactaldehyde

Processes

sulphoglycolysisGO:0061722

Splits KDSG into pyruvate, which supports growth, and the organosulfonate SLA.

Part 5: sulfolactaldehyde oxidation
SLA dehydrogenase oxidation to sulfolactateReactioned_sla_oxidation

Annotons

3-sulfolactaldehyde dehydrogenase
ed_sla_dehydrogenase
Participant: Family: NAD(P)+-dependent SLA dehydrogenase
Family:
NAD(P)+-dependent SLA dehydrogenasePANTHER:PTHR43353:SF5
Representative Members: PpSQ1_00395 (Pseudomonas putida SQ1 SLA dehydrogenase)UniProtKB:P0DOV9

Function

aldehyde dehydrogenase (NAD+) activityGO:0004029
Substrates: (2S)-3-sulfolactaldehyde NAD+
Products: (2S)-3-sulfolactate NADH

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Oxidizes SLA to SL, which is exported; the enzyme also accepts NADP+ (RHEA:47928).

Sulfo-SFT route (SQ isomerase and sulfofructose transaldolase)Metabolic Pathwaysulfo_sft_route

Transaldolase-dependent sulfoglycolysis characterized in Bacillus megaterium and Bacillus aryabhattai: SQ is isomerized to SF, and a sulfofructose transaldolase transfers the dihydroxyacetone unit of SF to glyceraldehyde 3-phosphate, forming fructose 6-phosphate and SLA; in these aerobes SLA is oxidized to SL.

PMID:33036753
A transaldolase-dependent sulfoglycolysis pathway in Bacillus megaterium DSM 1804.
SqvA is a sulfofructose transaldolase that forms F6P and SLA.
in which sulfosugar cleavage is catalyzed by the transaldolase SqvA, which converts 6-deoxy-6-sulfofructose and glyceraldehyde 3-phosphate into fructose -6-phosphate and (S)-sulfolactaldehyde.
PMID:32919372
Environmental and Intestinal Phylum Firmicutes Bacteria Metabolize the Plant Sugar Sulfoquinovose via a 6-Deoxy-6-sulfofructose Transaldolase Pathway.
The route was independently reconstituted with B. aryabhattai SftI, SftT and SftD and is expressed by intestinal Firmicutes.
An isomerase converts SQ to 6-deoxy-6-sulfofructose (SF). A novel transaldolase enzyme cleaves the SF to 3-sulfolactaldehyde (SLA), while the non-sulfonated C3-(glycerone)-moiety is transferred to an acceptor molecule, glyceraldehyde phosphate (GAP), yielding fructose-6-phosphate (F6P).

Connections

The isomerase supplies SF to the transaldolase.
The transaldolase supplies (2S)-SLA to SLA dehydrogenase.
Part 1: SQ to sulfofructose isomerization
SqvD/SftI sulfoquinovose isomerizationReactionsft_sq_isomerization

Annotons

Sulfoquinovose isomerase (SqvD/SftI)
sqvd_sq_isomerase
Participant: Family: SqvD-type sulfoquinovose isomerase
Family:
SqvD-type sulfoquinovose isomerasePANTHER:PTHR36120:SF1 Firmicutes SQ isomerases that are non-orthologous to E. coli YihS.
Representative Members: SqvD (Bacillus megaterium)UniProtKB:D5E1S9 SftI (Bacillus aryabhattai)UniProtKB:A0A7W3RDA3
Required Function:
sulfoquinovose isomerase activityGO:0061593

Function

sulfoquinovose isomerase activityGO:0061593
Substrates: 6-sulfo-beta-D-quinovose
Products: 6-deoxy-6-sulfo-D-fructose

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Isomerizes SQ to SF, the transaldolase donor substrate.

PMID:32919372
Environmental and Intestinal Phylum Firmicutes Bacteria Metabolize the Plant Sugar Sulfoquinovose via a 6-Deoxy-6-sulfofructose Transaldolase Pathway.
Recombinant SftI isomerizes SQ.
Thus, protein SftI is an SQ isomerase.
Part 2: sulfofructose transaldol cleavage
SqvA/SftT sulfofructose transaldolaseReactionsft_transaldol_cleavage

Annotons

6-deoxy-6-sulfo-D-fructose transaldolase (SqvA/SftT)
sqva_sf_transaldolase
Participant: Family: sulfofructose transaldolase
Family:
sulfofructose transaldolasePANTHER:PTHR10683:SF40
Representative Members: SqvA (Bacillus megaterium)UniProtKB:D5E1T2 SftT (Bacillus aryabhattai)UniProtKB:A0A7W3N5X5

Function

6-deoxy-6-sulfo-D-fructose transaldolase activity (EC 2.2.1.14)GO:0016744
Substrates: 6-deoxy-6-sulfo-D-fructose D-glyceraldehyde 3-phosphate
Products: D-fructose 6-phosphate (2S)-3-sulfolactaldehyde

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Schiff-base transaldolase that transfers the C3 glycerone unit of SF to GAP (or erythrose 4-phosphate), releasing SLA. GO:0004801 transaldolase activity is defined by the sedoheptulose 7-phosphate reaction, so the parent term is used here.

PMID:36805128
Structure and mechanism of sulfofructose transaldolase, a key enzyme in sulfoquinovose metabolism.
Cryo-EM structure shows a covalent Schiff-base intermediate with SF.
We demonstrate a covalent "Schiff base" intermediate formed by reaction of SF with Lys89 within a conserved Asp-Lys-Glu catalytic triad
Part 3: sulfolactaldehyde oxidation
SlaB/SftD oxidation of SLA to sulfolactateReactionsft_sla_oxidation

Annotons

3-sulfolactaldehyde dehydrogenase (SlaB/SftD)
sft_sla_dehydrogenase
Participant: Family: Firmicutes NAD+-dependent SLA dehydrogenase
Family:
Firmicutes NAD+-dependent SLA dehydrogenasePANTHER:PTHR42991:SF1
Representative Members: SlaB (Bacillus megaterium)UniProtKB:D5E1S7 SftD (Bacillus aryabhattai)UniProtKB:A0A7W3RCJ3

Function

aldehyde dehydrogenase (NAD+) activityGO:0004029
Substrates: (2S)-3-sulfolactaldehyde NAD+
Products: (2S)-3-sulfolactate NADH

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Oxidizes SLA to SL in aerobic Bacillus strains; anaerobic sulfo-SFT organisms instead reduce SLA to DHPS with a YihU-like reductase.

PMID:32919372
Environmental and Intestinal Phylum Firmicutes Bacteria Metabolize the Plant Sugar Sulfoquinovose via a 6-Deoxy-6-sulfofructose Transaldolase Pathway.
Recombinant SftD oxidizes SLA with NAD+.
Thus, protein SftD is another NAD+-dependent SLA dehydrogenase
Sulfo-SMO route (SQ monooxygenase and 6-dehydroglucose reductase)Metabolic Pathwaysulfo_smo_route

Oxidative desulfurization route characterized in Agrobacterium tumefaciens C58 (also called sulfo-ASMO): the FMNH2-dependent SQ monooxygenase SmoC, supplied with reduced FMN by the NADH-dependent flavin reductase SmoA, cleaves the C-S bond of SQ to release sulfite and 6-dehydroglucose, which the NADPH-dependent reductase SmoB reduces to glucose.

PMID:35074914
Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.
Defines the sulfo-SMO route in A. tumefaciens, in which all six SQ carbons are used and sulfite is released.
A sulfoquinovosidase hydrolyzes the SQ glycoside and the liberated SQ is acted on by a flavin mononucleotide-dependent sulfoquinovose monooxygenase, in concert with an NADH-dependent flavin reductase, to release sulfite and 6-oxo-glucose. An NAD(P)H-dependent oxidoreductase reduces the 6-oxo-glucose to glucose, enabling entry into primary metabolic pathways.

Connections

SmoC supplies 6-dehydroglucose to SmoB.
Part 1: oxidative C-S bond cleavage
SmoC/SmoA two-component SQ monooxygenaseReactionsmo_sq_desulfonation

Annotons

Sulfoquinovose monooxygenase (SmoC/SquD)
smoc_sq_monooxygenase
Participant: Family: SQ-specific luciferase-like monooxygenase
Family:
SQ-specific luciferase-like monooxygenasePANTHER:PTHR42847:SF4 SsuD-related FMNH2-dependent monooxygenases that are specific for SQ.
Representative Members: SmoC (Agrobacterium fabrum C58)UniProtKB:A9CEY7 SquD (Novosphingobium aromaticivorans)UniProtKB:Q2G5J4

Function

sulfoquinovose monooxygenase activity (EC 1.14.14.181)GO:0008726
Substrates: 6-sulfo-D-quinovose FMNH2 O2
Products: 6-dehydro-D-glucose sulfite FMN

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Cleaves the C-S bond of free SQ (not of SQGro), releasing sulfite.

PMID:35074914
Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.
SmoC is specific for SQ, unlike the promiscuous SsuD.
No activity was observed when SQ was replaced with other sulfonates, including SQGro (the precursor to SQ) or HEPES (an unrelated sulfonate) demonstrating that, unlike the promiscuous SsuD, SmoC has high specificity for SQ
PMID:41676062
Advances in microbial sulfoquinovose catabolism.
Sources the second member, Novosphingobium aromaticivorans SquD, as the SQ monooxygenase of the sulfo-ASMO/SMO route.
the degradation of SQ is initiated by the flavin-dependent alkane sulfonate monooxygenase SquD, which converts SQ to 6-dehydro-D-glucose and sulfite by an oxidative C-S bond cleavage
NADH-dependent FMN reductase (SmoA)
smoa_flavin_reductase
Participant: Family: sulfo-SMO cluster flavin reductase
Family:
sulfo-SMO cluster flavin reductasePANTHER:PTHR30466:SF11 The reductase partner differs between implementations: A. tumefaciens uses the cluster-encoded NADH-preferring SmoA, whereas PMID:41676062 describes SquD as partnered by an SsuE-type NAD(P)H flavin reductase. Only SmoA is asserted as a member here.
Representative Members: SmoA (Agrobacterium fabrum C58)UniProtKB:Q7CS24
Required Function:
FMN reductase (NADH) activityGO:0052874

Function

FMN reductase (NADH) activityGO:0052874
Substrates: FMN NADH
Products: FMNH2 NAD+

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Supplies FMNH2 to SmoC as the reductase partner of the two-component monooxygenase.

PMID:35074914
Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.
NADH is the preferred reductant of SmoA.
indicating that NADH is the preferred cofactor for SmoA
Part 2: 6-dehydroglucose reduction
SmoB/SquF reduction of 6-dehydroglucose to glucoseReactionsmo_dehydroglucose_reduction

Annotons

6-dehydroglucose reductase (SmoB/SquF)
smob_dehydroglucose_reductase
Participant: Family: sulfo-SMO 6-dehydroglucose reductase
Family:
sulfo-SMO 6-dehydroglucose reductasePANTHER:PTHR43364:SF1
Representative Members: SmoB (Agrobacterium fabrum C58)UniProtKB:A9CEY6 SquF (Novosphingobium aromaticivorans)UniProtKB:Q2G5J3

Function

6-dehydroglucose reductase activity (EC 1.1.1.432)GO:0016616
Substrates: 6-dehydro-D-glucose NADPH
Products: D-glucose NADP+

Processes

6-sulfoquinovose(1-) catabolic processGO:1902777

Reduces the aldehyde product of SmoC to glucose, which enters central metabolism.

PMID:35074914
Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.
SmoB uses NADP(H), not NAD(H).
Only enzymatic reactions conducted in the presence of NADP+ produced product labeled with 18O at C6: NAD+ failed to produce any product
PMID:41676062
Advances in microbial sulfoquinovose catabolism.
Sources the second member, Novosphingobium aromaticivorans SquF, as the 6-dehydroglucose reductase of the sulfo-ASMO/SMO route.
the NAD(P)H-dependent oxidoreductase SquF reduces 6-dehydro-D-glucose to form glucose