ID   GUAAA_METM7             Reviewed;         189 AA.
AC   A6VH31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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};
GN   OrderedLocusNames=MmarC7_0690;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR65757.1; -; Genomic_DNA.
DR   RefSeq; WP_011977078.1; NC_009637.1.
DR   AlphaFoldDB; A6VH31; -.
DR   SMR; A6VH31; -.
DR   STRING; 426368.MmarC7_0690; -.
DR   EnsemblBacteria; ABR65757; ABR65757; MmarC7_0690.
DR   GeneID; 5328155; -.
DR   KEGG; mmz:MmarC7_0690; -.
DR   eggNOG; arCOG00087; Archaea.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   OMA; GPDMDRI; -.
DR   OrthoDB; 79931at2157; -.
DR   UniPathway; UPA00189; UER00296.
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.
FT   CHAIN           1..189
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT                   /id="PRO_0000316095"
FT   DOMAIN          1..189
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        76
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01510"
SQ   SEQUENCE   189 AA;  20993 MW;  278EFD7A2E2A9B45 CRC64;
     MIVILNNGGQ YVHRIQRSLK YLGVPAKIVP NSTTLEEITV NPEIKGIILS GGPDITKATN
     CENIALNSEI PVLGICLGHQ LISKAYGGHV SRADSEEYAS IKIYVKEEND LFKGVPSEFT
     AWASHMDEVK VTPECFEILA YSDICGVESI KHKEKSLYGV QFHPEVSHTE YGDVLLKNFC
     KKCGFEFEE