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Database: UniProt
Entry: F4G2C6_METCR
LinkDB: F4G2C6_METCR
Original site: F4G2C6_METCR 
ID   F4G2C6_METCR            Unreviewed;       188 AA.
AC   F4G2C6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=Mcup_0869 {ECO:0000313|EMBL:AEB94974.1};
OS   Metallosphaera cuprina (strain Ar-4).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=1006006 {ECO:0000313|EMBL:AEB94974.1, ECO:0000313|Proteomes:UP000007812};
RN   [1] {ECO:0000313|EMBL:AEB94974.1, ECO:0000313|Proteomes:UP000007812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar-4 {ECO:0000313|EMBL:AEB94974.1,
RC   ECO:0000313|Proteomes:UP000007812};
RX   PubMed=21551305; DOI=10.1128/JB.05038-11;
RA   Liu L.J., You X.Y., Zheng H., Wang S., Jiang C.Y., Liu S.J.;
RT   "Complete genome sequence of Metallosphaera cuprina, a metal sulfide-
RT   oxidizing archaeon from a hot spring.";
RL   J. Bacteriol. 193:3387-3388(2011).
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; CP002656; AEB94974.1; -; Genomic_DNA.
DR   RefSeq; WP_013737472.1; NC_015435.1.
DR   AlphaFoldDB; F4G2C6; -.
DR   STRING; 1006006.Mcup_0869; -.
DR   MEROPS; C26.A31; -.
DR   GeneID; 10493060; -.
DR   KEGG; mcn:Mcup_0869; -.
DR   PATRIC; fig|1006006.8.peg.867; -.
DR   eggNOG; arCOG00087; Archaea.
DR   HOGENOM; CLU_014340_1_4_2; -.
DR   OMA; GPDMDRI; -.
DR   OrthoDB; 33844at2157; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000007812; 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; PR00099; CPSGATASE.
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}.
FT   DOMAIN          5..183
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01510,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   188 AA;  20884 MW;  F374CFF028FE804F CRC64;
     MKVGLIYFGG QYNHLILKNV KYLGVDIEVV DPSLPVEKLN AYDCLIFSGG PQSVKEEINS
     IGNSVNYVRE LSSPKLGICL GHQLIAYALG GVVDKASNPE FGLVKVTIHD HDTILKDMPS
     VFNAWESHND EVKAPPLGFR VLASSETTKI QSMVNKDNTI FTVQFHPEVK HTQQGLLVFK
     NFLEVCKR
//
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