Gene Ontology annotation through association of InterPro records with GO terms

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

GO_REF:0000118

TreeGrafter-generated GO annotations

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:PSEPK/moaA/moaA-uniprot.txt

UniProtKB reviewed entry for moaA

The reviewed HAMAP record identifies Q88E69 as the two-cluster radical-SAM GTP 3',8'-cyclase EC 4.1.99.22.

"CC -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- CC dihydroguanosine 5'-triphosphate. {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + AH2 + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8- CC dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + CC A + H(+); Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:17499, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:131766; CC EC=4.1.99.22; Evidence={ECO:0000255|HAMAP-Rule:MF_01225}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01225}; CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 CC [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived CC substrate. {ECO:0000255|HAMAP-Rule:MF_01225};"

file:PSEPK/moaA/moaA-goa.tsv

QuickGO GOA annotations for moaA

The fetched table contains the exact GTP cyclase annotation accepted here.

"UniProtKB Q88E69 moaA enables GO:0061798 GTP 3',8'-cyclase activity molecular_function ECO:0000501 IEA GO_REF:0000120 RHEA:49576|EC:4.1.99.22|PANTHER:PTN002344120|UniRule:UR000101305 160488 Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) UniProt GTP 3',8-cyclase 20260706"

file:PSEPK/moaA/moaA-deep-research-openscientist.md

OpenScientist gene research for moaA

The report gives the canonical MoaA reaction assignment, independently supported by reviewed Q88E69 UniProt.

"MoaA is a **radical S-adenosyl-L-methionine (SAM) metalloenzyme, GTP 3',8-cyclase**, that catalyzes the **first and committed step of molybdenum cofactor (Moco) biosynthesis**."
The report correctly distinguishes MoaA cyclization from the cyclic-phosphate-forming MoaC reaction.

"MoaA is **not** the enzyme that forms the cyclic phosphate or releases pyrophosphate (that is MoaC)"
The report presents target-specific residue analysis that was not saved as a reproducible local artifact.

"**N-terminal radical-SAM cluster:** the canonical **CX₃CX₂C** motif at **Cys27–Cys31–Cys34** (…C27-D-F-R-C31-V-Y-C34…), matching the SAM-cleaving [4Fe-4S] cluster fingerprint (IPR000385)."
The report explicitly acknowledges that its mechanistic and structural evidence is transferred from orthologs.

"All mechanistic/structural data derive from **orthologs**, not the *P. putida* KT2440 protein directly; however, MoaA family conservation (HAMAP MF_01225) makes transfer of annotation robust."
The report overstates Q88E69 as rate-defining despite unresolved KT2440 MoaA-family paralogs.

"Because MoaA sits at the pathway's entry point, its activity is **rate-defining for the supply of all Moco-dependent enzymes**"

file:PSEPK/moaA/moaA-bioinformatics/RESULTS.md

Reproducible sequence comparison of KT2440 MoaA-family and MobA-like proteins

Q88E69 alone carries the MoaA-specific InterPro records among the three KT2440 MoaA-family candidates examined.

"- The reviewed MoaA sequence Q88E69 is the only one of the three with the MoaA-specific InterPro entries IPR013483 and IPR000385 in its UniProt record. All three share broader MoaA-like/radical-SAM entries and PTHR22960."