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Entry: A0A6M0QA86_9BACI
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ID   A0A6M0QA86_9BACI        Unreviewed;        84 AA.
AC   A0A6M0QA86;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   18-JUN-2025, entry version 16.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurS {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_01926};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_01926};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit III {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAR amidotransferase III {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAR-AT III {ECO:0000256|HAMAP-Rule:MF_01926};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit III {ECO:0000256|HAMAP-Rule:MF_01926};
GN   Name=purS {ECO:0000256|HAMAP-Rule:MF_01926,
GN   ECO:0000313|EMBL:NEY73167.1};
GN   ORFNames=G4D63_15645 {ECO:0000313|EMBL:NEY73167.1};
OS   Bacillus mesophilus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1808955 {ECO:0000313|EMBL:NEY73167.1, ECO:0000313|Proteomes:UP000481043};
RN   [1] {ECO:0000313|EMBL:NEY73167.1, ECO:0000313|Proteomes:UP000481043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA4 {ECO:0000313|EMBL:NEY73167.1,
RC   ECO:0000313|Proteomes:UP000481043};
RA   Xie J.;
RT   "Bacillus aquiflavi sp. nov., isolated from yellow water of strong flavor
RT   Chinese baijiu in Yibin region of China.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes the
CC       ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC       glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC       glutamate. The FGAM synthase complex is composed of three subunits.
CC       PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC       PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC       dependent manner. PurS interacts with PurQ and PurL and is thought to
CC       assist in the transfer of the ammonia molecule from PurQ to PurL.
CC       {ECO:0000256|HAMAP-Rule:MF_01926}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-
CC         glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC         ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+);
CC         Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01926};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01926}.
CC   -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ
CC       and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_01926}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01926}.
CC   -!- SIMILARITY: Belongs to the PurS family. {ECO:0000256|HAMAP-
CC       Rule:MF_01926}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NEY73167.1}.
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DR   EMBL; JAAIWM010000006; NEY73167.1; -; Genomic_DNA.
DR   RefSeq; WP_163180647.1; NZ_JAAIWM010000006.1.
DR   AlphaFoldDB; A0A6M0QA86; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000481043; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1280.10; Phosphoribosylformylglycinamidine synthase subunit PurS; 1.
DR   HAMAP; MF_01926; PurS; 1.
DR   InterPro; IPR003850; PurS.
DR   InterPro; IPR036604; PurS-like_sf.
DR   NCBIfam; TIGR00302; phosphoribosylformylglycinamidine synthase subunit PurS; 1.
DR   NCBIfam; NF004630; PRK05974.1; 1.
DR   PANTHER; PTHR34696; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURS; 1.
DR   PANTHER; PTHR34696:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURS; 1.
DR   Pfam; PF02700; PurS; 1.
DR   SUPFAM; SSF82697; PurS-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01926};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01926};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01926};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01926};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01926}; Reference proteome {ECO:0000313|Proteomes:UP000481043}.
SQ   SEQUENCE   84 AA;  9638 MW;  9352EF30D6AFF4D5 CRC64;
     MYKVKVFVTL RESVLDPQGT AVKGSLHSLS YTEVQDVRIG KFLELTIEKS DHSIDELVKE
     MCERLLTNTV IEDYTYEVEE VVAK
//
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