PURQ_SYNJA
ID PURQ_SYNJA Reviewed; 225 AA.
AC Q2JWK2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, 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=CYA_0646;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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; CP000239; ABC98861.1; -; Genomic_DNA.
DR RefSeq; WP_011429544.1; NC_007775.1.
DR AlphaFoldDB; Q2JWK2; -.
DR SMR; Q2JWK2; -.
DR STRING; 321327.CYA_0646; -.
DR EnsemblBacteria; ABC98861; ABC98861; CYA_0646.
DR KEGG; cya:CYA_0646; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_1_3; -.
DR OMA; LHFVCRD; -.
DR OrthoDB; 1527083at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000008818; 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.
FT CHAIN 1..225
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurQ"
FT /id="PRO_0000252740"
FT DOMAIN 5..225
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 89
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 198
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 200
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
SQ SEQUENCE 225 AA; 24108 MW; 4C5F40D28DC246F4 CRC64;
MAKVRFGIVV FPGSNCDRDV AWVTRGLLGC PTRLIWHRET DLSGLDVVVL PGGFSYGDYL
RAGALARFAP VMGSLAEHGA RGGYVLGICN GFQILTEAGL LPGALVRNAN LHFICDRVGI
RVERQDLPWT SAYPCGATLT LPIAHGEGRY VCDADTLKQL QDRGQIVFRY APVAPNGSVD
NIAGICDPSG RILGLMPHPE RAADPDLPGQ DGIPFWQSIV QSLAG
