PURQ_ZYMMO
ID PURQ_ZYMMO Reviewed; 221 AA.
AC Q5NMA4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=ZMO1532;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(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; AE008692; AAV90156.1; -; Genomic_DNA.
DR RefSeq; WP_011241302.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NMA4; -.
DR SMR; Q5NMA4; -.
DR STRING; 264203.ZMO1532; -.
DR EnsemblBacteria; AAV90156; AAV90156; ZMO1532.
DR GeneID; 58027258; -.
DR KEGG; zmo:ZMO1532; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_1_5; -.
DR OMA; LHFVCRD; -.
DR OrthoDB; 1527083at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001173; 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..221
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurQ"
FT /id="PRO_0000100604"
FT DOMAIN 3..221
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 195
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 197
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
SQ SEQUENCE 221 AA; 23952 MW; 68CEC688EC270603 CRC64;
MKAAVLVFPG SNCDRDLAVA IEKICGTKPL MVWHQESELP DDLDLIAVPG GFSYGDYLRS
GAMAARSAVM PAVIKQAERG VPVLGICNGF QILTEAGLLP GALMRNAGLS FICRNVGLEI
QNTTSPFLRL YKKNQKIHLP VAHHDGNYTA DEATLDQLED EDRVALRYTE SVNGSARNIA
GVLNKKGNVL GLMPHPERMI EDAHGGKDGY NMFASLMQVM A
