GenomeNet

Database: UniProt
Entry: A0A926RV35_9BACL
LinkDB: A0A926RV35_9BACL
Original site: A0A926RV35_9BACL 
ID   A0A926RV35_9BACL        Unreviewed;        83 AA.
AC   A0A926RV35;
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:MBD1373352.1};
GN   ORFNames=IC620_13440 {ECO:0000313|EMBL:MBD1373352.1};
OS   Polycladospora coralii.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC   Thermoactinomycetaceae; Polycladospora.
OX   NCBI_TaxID=2771432 {ECO:0000313|EMBL:MBD1373352.1, ECO:0000313|Proteomes:UP000661691};
RN   [1] {ECO:0000313|EMBL:MBD1373352.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IB182357 {ECO:0000313|EMBL:MBD1373352.1};
RA   Huang H., Mo K., Hu Y.;
RT   "A novel bacterium of genus Hazenella, isolated from South China Sea.";
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:MBD1373352.1}.
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; JACXAH010000023; MBD1373352.1; -; Genomic_DNA.
DR   RefSeq; WP_191142468.1; NZ_JACXAH010000023.1.
DR   Proteomes; UP000661691; 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:UP000661691}.
SQ   SEQUENCE   83 AA;  9225 MW;  03C80D1AB7ABD17C CRC64;
     MYKAIIDVTL KQSVLDPQGV AVKGSLHSLG YESVSDVRIG KRMEVLLESV TLAEAERDIE
     EICKKVLSNP VIEDFSYQLE EVA
//
DBGET integrated database retrieval system