PURQ_EXISA
ID PURQ_EXISA Reviewed; 226 AA.
AC C4L298;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=EAT1b_2228;
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium;
OC unclassified Exiguobacterium.
OX NCBI_TaxID=360911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b;
RX PubMed=21460088; DOI=10.1128/jb.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ71150.1; -; Genomic_DNA.
DR RefSeq; WP_015880709.1; NC_012673.1.
DR AlphaFoldDB; C4L298; -.
DR SMR; C4L298; -.
DR STRING; 360911.EAT1b_2228; -.
DR EnsemblBacteria; ACQ71150; ACQ71150; EAT1b_2228.
DR KEGG; eat:EAT1b_2228; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_1_9; -.
DR OMA; LHFVCRD; -.
DR OrthoDB; 1527083at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000716; 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..226
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurQ"
FT /id="PRO_1000206052"
FT DOMAIN 3..225
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 194
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 196
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
SQ SEQUENCE 226 AA; 24702 MW; 95ED368A1FC38D67 CRC64;
MKFAVIVFPG SNCDLDMYHA VKDVLGEEAE YVFHTETSLE GFDGVLLPGG FSYGDYLRCG
SIAQFSPIMA EVKRFAEEGR PVLGVCNGFQ VLVEAGLLPG VLMRNRDLKF MCKTVDLVVE
NNETMFTSEY AAQETIRVPI AHGEGNYYCD DATLAALKAN GQIAFTYKEN PNGSVENIAG
ITNEAGNVLG MMPHPERAVE ALLGGEDGKR LFTSIVKWGA RHVTYN
