ID A0A972H1A0_9BACL Unreviewed; 80 AA.
AC A0A972H1A0;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
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:NOU98384.1};
GN ORFNames=GC093_34960 {ECO:0000313|EMBL:NOU98384.1};
OS Paenibacillus foliorum.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=2654974 {ECO:0000313|EMBL:NOU98384.1, ECO:0000313|Proteomes:UP000641588};
RN [1] {ECO:0000313|EMBL:NOU98384.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMG 31456 {ECO:0000313|EMBL:NOU98384.1};
RA Carlier A., Qi S.;
RT "Description of Paenibacillus glebae sp. nov.";
RL Submitted (OCT-2019) 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:NOU98384.1}.
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DR EMBL; WHOD01000135; NOU98384.1; -; Genomic_DNA.
DR Proteomes; UP000641588; 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:UP000641588}.
SQ SEQUENCE 80 AA; 8903 MW; AB5A07100B5835A1 CRC64;
MLKATVYVTI KQSVLDPQGV AVQGALHSMG FDEVGKVRVG KYLELELGTS DRAEAEQRVK
AMCEKLLANT VIEDYRYELV
//
