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Database: UniProt
Entry: F2KSS2_ARCVS
LinkDB: F2KSS2_ARCVS
Original site: F2KSS2_ARCVS 
ID   F2KSS2_ARCVS            Unreviewed;       184 AA.
AC   F2KSS2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000256|HAMAP-Rule:MF_01510};
DE            EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_01510};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01510};
GN   Name=guaAA {ECO:0000256|HAMAP-Rule:MF_01510};
GN   OrderedLocusNames=Arcve_0956 {ECO:0000313|EMBL:AEA46967.1};
OS   Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA46967.1, ECO:0000313|Proteomes:UP000008136};
RN   [1] {ECO:0000313|EMBL:AEA46967.1, ECO:0000313|Proteomes:UP000008136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SNP6;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Archaeoglobus veneficus SNP6.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01510};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_01510}.
CC   -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC       (A) and a GMP-binding subunit (B). {ECO:0000256|HAMAP-Rule:MF_01510}.
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DR   EMBL; CP002588; AEA46967.1; -; Genomic_DNA.
DR   RefSeq; WP_013683631.1; NC_015320.1.
DR   AlphaFoldDB; F2KSS2; -.
DR   STRING; 693661.Arcve_0956; -.
DR   MEROPS; C26.A31; -.
DR   GeneID; 10394066; -.
DR   KEGG; ave:Arcve_0956; -.
DR   eggNOG; arCOG00087; Archaea.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   OMA; GPDMDRI; -.
DR   OrthoDB; 10772at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000008136; 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-UniRule.
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   NCBIfam; TIGR00888; guaA_Nterm; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01510};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_01510};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW   Rule:MF_01510};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01510};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01510};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01510}; Reference proteome {ECO:0000313|Proteomes:UP000008136}.
FT   DOMAIN          6..179
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   184 AA;  20923 MW;  1A0F13FC64F2AEDD CRC64;
     MVKIYVVYNY GQYNHLIHRT LRDLGVESKL IENTTPVEQI KDADGIVLGG GPSLERTGNC
     ELYVKELDVP ILGICLGHQL LAKVFGGEVG KGQVGGYAEV NVRIVEEDEI FEGLPKELKA
     WASHADEVKK MPEDFKHLAE SDVCKIEAMR HKEKPIYGVQ WHPEVYHTER GVDFYRNFIK
     ICKR
//
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