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PURQ_ANOFW
ID   PURQ_ANOFW              Reviewed;         228 AA.
AC   B7GFT7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Aflv_0233;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ32617.1; -; Genomic_DNA.
DR   RefSeq; WP_012573956.1; NC_011567.1.
DR   AlphaFoldDB; B7GFT7; -.
DR   SMR; B7GFT7; -.
DR   STRING; 491915.Aflv_0233; -.
DR   EnsemblBacteria; ACJ32617; ACJ32617; Aflv_0233.
DR   KEGG; afl:Aflv_0233; -.
DR   PATRIC; fig|491915.6.peg.239; -.
DR   eggNOG; COG0047; Bacteria.
DR   HOGENOM; CLU_001031_3_1_9; -.
DR   OMA; LHFVCRD; -.
DR   OrthoDB; 1527083at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000000742; 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..228
FT                   /note="Phosphoribosylformylglycinamidine synthase subunit
FT                   PurQ"
FT                   /id="PRO_1000194842"
FT   DOMAIN          3..226
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        195
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
SQ   SEQUENCE   228 AA;  25325 MW;  7F5632CDCC1A9D38 CRC64;
     MKFAVVVFPG SNCDVDMYHA ISDELGEEVE YVWHDVDCLD DFDAILLPGG FSYGDYLRSG
     AIARFSNVMK AIKKAADEGK PILGVCNGFQ ILLEAGLLPG AMRRNNTLTF ICRPIKLRVE
     NNETMFTSQY EQGEVITIPI AHGEGNYYCD EQTLQQLIAN NQIVFRYEGE NPNGSLFNIA
     GIVNEKGNVL GMMPHPERAV HELLGGADGL KLFQSIVTYW RDAHVVTT
 
 
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