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Database: UniProt
Entry: PURQ_SALRD
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ID   PURQ_SALRD              Reviewed;         235 AA.
AC   Q2S567;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=SRU_0521;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(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; CP000159; ABC43823.1; -; Genomic_DNA.
DR   RefSeq; WP_011403297.1; NC_007677.1.
DR   RefSeq; YP_444664.1; NC_007677.1.
DR   AlphaFoldDB; Q2S567; -.
DR   SMR; Q2S567; -.
DR   STRING; 309807.SRU_0521; -.
DR   EnsemblBacteria; ABC43823; ABC43823; SRU_0521.
DR   KEGG; sru:SRU_0521; -.
DR   PATRIC; fig|309807.25.peg.543; -.
DR   eggNOG; COG0047; Bacteria.
DR   HOGENOM; CLU_001031_3_1_10; -.
DR   OrthoDB; 9804441at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000008674; 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   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; PTHR47552; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1.
DR   PANTHER; PTHR47552:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 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; Cytoplasm; Glutamine amidotransferase; Hydrolase; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..235
FT                   /note="Phosphoribosylformylglycinamidine synthase subunit
FT                   PurQ"
FT                   /id="PRO_0000252729"
FT   DOMAIN          5..235
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
SQ   SEQUENCE   235 AA;  25198 MW;  D385CC7DDCB51A30 CRC64;
     MSARFGVVVF PGSNCDHDAY HAAHDVFDQE ARFIWHEEAS LGDVDVVIVP GGFSYGDYLR
     SGAVARFSPI MQDVVRFAED GGLVFGICNG FQVLCEAGLL PGTLMRNESL RFVCKDTPLR
     VENAGTPFTN ALTEGQVITI PVSHGEGRYY ADEDVLARIE ANDQVLLRYS TADGAVTDEA
     NPNGSVHGIA GLVNEAGNVC GLMPHPERCV ESLLGGDDGR LIFESLLNHV SIVAA
//
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