ID   GUAAA_METST             Reviewed;         186 AA.
AC   Q2NER5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   02-SEP-2026, entry version 98.
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=Msp_1311;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_01510}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP +
CC         diphosphate + 2 H(+); 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; CP000102; ABC57688.1; -; Genomic_DNA.
DR   RefSeq; WP_011406887.1; NC_007681.1.
DR   AlphaFoldDB; Q2NER5; -.
DR   SMR; Q2NER5; -.
DR   STRING; 339860.Msp_1311; -.
DR   MEROPS; C26.A31; -.
DR   GeneID; 3855939; -.
DR   KEGG; mst:Msp_1311; -.
DR   eggNOG; arCOG00087; Archaea.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   OrthoDB; 10772at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001931; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003921; F:GMP synthase activity; IEA:TreeGrafter.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   FunFam; 3.40.50.880:FF:000047; GMP synthase [glutamine-hydrolyzing] subunit A; 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   NCBIfam; TIGR00888; guaA_Nterm; 1.
DR   NCBIfam; NF001975; PRK00758.1; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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..186
FT                   /note="GMP synthase [glutamine-hydrolyzing] subunit A"
FT                   /id="PRO_0000292197"
FT   DOMAIN          2..186
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   186 AA;  20948 MW;  608D3625C5D10B41 CRC64;
     MSIVIINNFG QYNHRISRTL KYLNIENSLI PNTTSFEEIE QMNPKGIILG GGPSIERIGN
     CKEIILNMDI PILGICLGHQ IIADVFGGET KSAEIESYAQ IELNILKENG LFKGIGDSLK
     VWASHKDEVV TLPENFEILA NSDKCDIEAM KHEDKNIYGI QFHPEVQHTP RGGEIFENFN
     KICENY
//