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PURQ_CARHZ
ID   PURQ_CARHZ              Reviewed;         234 AA.
AC   Q3AD65;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000255|HAMAP-Rule:MF_00421};
DE            Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00421};
DE            EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00421};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000255|HAMAP-Rule:MF_00421};
DE            Short=FGAR amidotransferase I {ECO:0000255|HAMAP-Rule:MF_00421};
DE            Short=FGAR-AT I {ECO:0000255|HAMAP-Rule:MF_00421};
DE   AltName: Full=Glutaminase PurQ {ECO:0000255|HAMAP-Rule:MF_00421};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00421};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000255|HAMAP-Rule:MF_00421};
GN   Name=purQ {ECO:0000255|HAMAP-Rule:MF_00421}; OrderedLocusNames=CHY_1073;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00421}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00421}.
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DR   EMBL; CP000141; ABB14844.1; -; Genomic_DNA.
DR   RefSeq; WP_011343995.1; NC_007503.1.
DR   AlphaFoldDB; Q3AD65; -.
DR   SMR; Q3AD65; -.
DR   STRING; 246194.CHY_1073; -.
DR   PRIDE; Q3AD65; -.
DR   EnsemblBacteria; ABB14844; ABB14844; CHY_1073.
DR   KEGG; chy:CHY_1073; -.
DR   eggNOG; COG0047; Bacteria.
DR   HOGENOM; CLU_001031_3_1_9; -.
DR   OMA; LHFVCRD; -.
DR   OrthoDB; 1527083at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000002706; 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:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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   PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01737; FGAM_synth_I; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glutamine amidotransferase; Hydrolase; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..234
FT                   /note="Phosphoribosylformylglycinamidine synthase subunit
FT                   PurQ"
FT                   /id="PRO_0000252701"
FT   DOMAIN          3..233
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
SQ   SEQUENCE   234 AA;  25793 MW;  AE76C171A543D119 CRC64;
     MKFGVVVFPG SNCDADCFHV LKNVFGRETV YIWHKEDNFD VDCIVLPGGF SYGDYLRAGA
     IARFSPVMKK VVEFANAGGL VIGICNGFQI LLEAGLLPGA MLRNKSINFR CHDVYLRVEN
     NNTPFTSKAH EGQVLKIPIA HGEGNYYCEP DTLKKLIANG QVVFRYCNSR GEVTEDANPN
     GSLYNIAGII NEKGNVLGMM PHPERCSENI LGGEDGRVIW ESIIAYLERG ANRG
 
 
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