PURQ_EXIS2
ID PURQ_EXIS2 Reviewed; 227 AA.
AC B1YJ04;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=Exig_0452;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) 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: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; CP001022; ACB59934.1; -; Genomic_DNA.
DR RefSeq; WP_012369358.1; NC_010556.1.
DR AlphaFoldDB; B1YJ04; -.
DR SMR; B1YJ04; -.
DR STRING; 262543.Exig_0452; -.
DR EnsemblBacteria; ACB59934; ACB59934; Exig_0452.
DR KEGG; esi:Exig_0452; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_1_9; -.
DR OMA; LHFVCRD; -.
DR OrthoDB; 1527083at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001681; 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..227
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurQ"
FT /id="PRO_1000124118"
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 227 AA; 24742 MW; 1D66F6670177FF3F CRC64;
MKFAVIVFPG SNCDLDMYHA VKDALGEEVE YVFHTETSLE GYDGVLLPGG FSYGDYLRCG
AIAQFSPIME EVKRFAAEGK TVLGVCNGFQ ILVEAGLLPG VLHRNTGLKF MCRTVELKVE
NNETRFTSDY AAQETITIPI AHGEGNYYCD DATYAMLQTN RQIAFTYTDN PNGSRGDIAG
ITNKAGNVLG MMPHPERAVE LLTGGTDGLK LFTSLVKQGA HHVKTTV
