ID A5D2D2_PELTS Unreviewed; 260 AA.
AC A5D2D2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00421};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00421};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
DE Short=FGAR amidotransferase I {ECO:0000256|HAMAP-Rule:MF_00421};
DE Short=FGAR-AT I {ECO:0000256|HAMAP-Rule:MF_00421};
DE AltName: Full=Glutaminase PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
DE EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00421};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
GN Name=PurL {ECO:0000313|EMBL:BAF59611.1};
GN Synonyms=purQ {ECO:0000256|HAMAP-Rule:MF_00421};
GN OrderedLocusNames=PTH_1430 {ECO:0000313|EMBL:BAF59611.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59611.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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_00421}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
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_00421};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00421};
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_00421}.
CC -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ
CC and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00421}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421}.
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DR EMBL; AP009389; BAF59611.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D2D2; -.
DR STRING; 370438.PTH_1430; -.
DR KEGG; pth:PTH_1430; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_0_9; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000006556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00421; PurQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR NCBIfam; TIGR01737; FGAM_synth_I; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF13507; GATase_5; 1.
DR PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00421};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421};
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00421,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00421};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00421};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00421};
KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00421};
KW Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW Transferase {ECO:0000313|EMBL:BAF59611.1}.
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 260 AA; 28973 MW; E2D7A9212AAB2114 CRC64;
MKKPRVCIMK TDGINCDEET YYAFVKAGAE CRIVHVNQLR KGEEKLASYQ ILALPGGFSY
GDDVHSGKIL AVELTSFLKD QLKEFVNAGK LIIGICNGFQ VLVRTGLLPE QNLDCIKTTL
MVNDSGHFEC RWVNLLVEHN HCVFTKGLEG TVISVQVAHG EGKFYTDPAT LQEIENRGQV
VFRYAGTDGR PTVLYPYNPN GSLNAIAGIC DSTGRIMGMM PHPERYVEKT QHPNWRRLPG
NTLPHGMAIF KNAVEYALQL
//
