ID   GUAAA_PYRFU             Reviewed;         188 AA.
AC   Q8U0R9;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000255|HAMAP-Rule:MF_01510};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_01510};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_01510};
GN   Name=guaAA {ECO:0000255|HAMAP-Rule:MF_01510}; OrderedLocusNames=PF1515;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_01510}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC         H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01510};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01510}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP-Rule:MF_01510}.
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DR   EMBL; AE009950; AAL81639.1; -; Genomic_DNA.
DR   RefSeq; WP_011012662.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0R9; -.
DR   SMR; Q8U0R9; -.
DR   STRING; 186497.PF1515; -.
DR   MEROPS; C26.A31; -.
DR   EnsemblBacteria; AAL81639; AAL81639; PF1515.
DR   GeneID; 41713334; -.
DR   KEGG; pfu:PF1515; -.
DR   PATRIC; fig|186497.12.peg.1578; -.
DR   eggNOG; arCOG00087; Archaea.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   OMA; GPDMDRI; -.
DR   OrthoDB; 79931at2157; -.
DR   PhylomeDB; Q8U0R9; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01510; GMP_synthase_A; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR023686; GMP_synthase_A.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..188
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT                   /id="PRO_0000140229"
FT   DOMAIN          1..188
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
SQ   SEQUENCE   188 AA;  21306 MW;  B9E5ADC7CF832EBF CRC64;
     MIIIMDNGGQ YVHRIWRTLR YLGVEAKIIP NTTPLDEIKA MKPKGIIFSG GPSLENTGNC
     EKILEHYEEF NVPILGICLG HQLIAKFFGG EVGRGEKAEY SLVEIEIIDE NDIFKGLPRK
     VRVWESHMDE VKKLPPKFKL LARSDTCPVE AMKHEELPIY GVQFHPEVAH TEHGADILRN
     FAKICGEL