Auto-converted DRAFT module for Histidine biosynthesis, mined from the GapMind amino-acid pathway definition 'his.steps' and grounded against ModelSEED. Generated by a feasibility-spike importer; GO molecular-function term assignments and biological prose are intentionally left for human/deep-research review and must not be treated as curated.
MINED DRAFT -- not curated. Source: GapMind .steps (PaperBLAST, Price/Arkin LBL). Steps map to annotons; GapMind OR-rules map to EXACTLY_ONE variant_sets; EC numbers grounded to ModelSEED/KEGG/MetaCyc. 'ignore'/'term' GapMind tokens were dropped.
All recommended fields populated.
✗ none found
No MODULE:gapmind_his_biosynthesis deep-research report alongside the module YAML.
9 leaf node(s) with no concrete protein grounding:
✓ every declared conforms_to bundle matches its template motif.
No concrete UniProt-grounded genes in this module.
CH_123581 and uniprot:A1BPP9 probably do all three: hisD, hisE, and hisI.
uniprot:A1BPP9 is annotated as hisD but is likely multifunctional, so similarity to it is ignored.
Subunits are not always annotated consistently, so are added manually, and uniprot:Q9SZ30 is a fusion protein of the two subunits
Subunits are not always annotated consistently, so are added manually, and uniprot:Q9SZ30 is a fusion protein of the two subunits
Fitness data showed that BPHYT_RS17700 (B2SZ63) from Burkholderia phytofirmans is required for histidine biosynthesis. PA5143 (Q9HU41) from Pseudomonas aeruginosa is required for histidine biosynthesis (PMC7028973).
In Bacillus subtilis, the histidinol-phosphate aminotransferase activity is provided by a gene that is in a cluster of genes for tyrosine and phenylalanine biosynthesis (PMID:4431). Homology suggests that this activity is provided by "HisH" (BSU22620), which indeed is just upstream of tyrA (PMID:6092865). This protein is now usually referred to as "HisC" (uniprot:HIS8_BACSU). AAFF19_12795 from Acidovorax sp. FHTAMBA (nearly identical to uniprot:A0A2R7PAQ8) can complement a hisC- strain of E. coli (Bradley Biggs) and is in a histidine synthesis gene cluster. AAGF34_01100 from Rhodoferax sp. GW822-FHT02A01 (similar to uniprot:A0A975E8Y9) can complement a hisC- strain of E. coli (Bradley Biggs) and is in a histidine synthesis gene cluster. Fitness data for BPHYT_RS14905 from Burkholderia phytofirmans suggests that it is an aromatic amino acid transaminase, but it is 55% identical to TK06_RS12685, which can complement a hisC- mutant of E.coli (Bradley Biggs), so any similarity to it is ignored. Fitness data confirms that BBR_RS17050 (uniprot:A0AAW7LC73) from Bifidobacterium breve is hisC.
In Bacillus subtilis and some related bacteria, histidinol-phosphate phosphatase is known as HisJ and has been confirmed by biochemical assays of purified proteins (PMC3570733). The identifiers given (see their Table 3) are MCCL_0344 BBR47_00270 BCE_1533 BcerKBAB4_1335 BcerKBAB4_1335 BSU29620 BH3206 GK2799 SMU_1486c (uniprot:B9E9Z0_MACCJ uniprot:C0ZH63_BREBN uniprot:Q73B87_BACC1 uniprot:A9VLI0_BACMK uniprot:HIS9_BACHD uniprot:Q5KW52_GEOKA uniprot:Q8DT80_STRMU uniprot:HIS9_BACSU). In Bifidobacterium breve, the phosphatase activity is provided by Bbr_0982 (uniprot:A0A0L7BRC5, URL:https://doi.org/10.1101/2023.08.29.555234). uniprot:S5FT07 and uniprot:S5FU55 are misannotated as this in BRENDA. E. coli phoA (ecocyc:ALKAPHOSPHA-MONOMER) has this activity but is ignored because it is periplasmic. HVO_0431 (uniprot:D4GRX2) from Haloferax has auxotrophic phenotypes and must be the missing hisN (PMC4300041; PMC8305020). uniprot:A0A1I1YPH6 ("Beta1") and Nmar_1556 (uniprot:A9A5X4) were shown biochemically to be hisN (PMC10804674); Beta1 is similar to BPHYT_RS03625, which has auxotrophic phenotypes; Nmar_1556 lies in a histidine synthesis operon and must be the missing hisN.