ID A0A917LJI9_9BACI Unreviewed; 79 AA.
AC A0A917LJI9;
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:GGG32458.1};
GN ORFNames=GCM10007425_28880 {ECO:0000313|EMBL:GGG32458.1};
OS Lysinibacillus alkalisoli.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Lysinibacillus.
OX NCBI_TaxID=1911548 {ECO:0000313|EMBL:GGG32458.1, ECO:0000313|Proteomes:UP000616608};
RN [1] {ECO:0000313|EMBL:GGG32458.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15760 {ECO:0000313|EMBL:GGG32458.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:GGG32458.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15760 {ECO:0000313|EMBL:GGG32458.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-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:GGG32458.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BMJT01000013; GGG32458.1; -; Genomic_DNA.
DR RefSeq; WP_188615780.1; NZ_BMJT01000013.1.
DR Proteomes; UP000616608; 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:UP000616608}.
SQ SEQUENCE 79 AA; 8875 MW; E9B572A0007F504A CRC64;
MTKVNVYVTL RESVVDPQGI AAKEALHSMG HDAVKNVRIG KLIELEVESN TVEADVTKMC
DELLINKVIE DYRFEIEGE
//
