(data stored in SCRATCH zone)

SWISSPROT: C4KKS7_SULIK

ID   C4KKS7_SULIK            Unreviewed;       188 AA.
AC   C4KKS7;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
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=M164_0258 {ECO:0000313|EMBL:ACR40892.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40892.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40892.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000256|HAMAP-Rule:MF_01510}.
CC   -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP +
CC       diphosphate + GMP + L-glutamate. {ECO:0000256|HAMAP-
CC       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
CC       subunit (A) and a GMP-binding subunit (B). {ECO:0000256|HAMAP-
CC       Rule:MF_01510}.
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DR   EMBL; CP001402; ACR40892.1; -; Genomic_DNA.
DR   RefSeq; WP_012710416.1; NC_012726.1.
DR   ProteinModelPortal; C4KKS7; -.
DR   MEROPS; C26.A31; -.
DR   EnsemblBacteria; ACR40892; ACR40892; M164_0258.
DR   GeneID; 7813366; -.
DR   KEGG; sid:M164_0258; -.
DR   HOGENOM; HOG000025031; -.
DR   KO; K01951; -.
DR   OMA; GQYVHRI; -.
DR   OrthoDB; POG093Z0A6E; -.
DR   BioCyc; SISL426118:GI01-260-MONOMER; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP.
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;
DR   PRODOM; C4KKS7.
DR   SWISS-2DPAGE; C4KKS7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01510};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01510};
KW   GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01510};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01510};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01510};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01510}.
FT   DOMAIN        2    188       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   ACT_SITE     79     79       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01510}.
FT   ACT_SITE    166    166       {ECO:0000256|HAMAP-Rule:MF_01510}.
FT   ACT_SITE    168    168       {ECO:0000256|HAMAP-Rule:MF_01510}.
SQ   SEQUENCE   188 AA;  21023 MW;  7DDBCA3E13AB164E CRC64;
     MKVGLVYYGG QYNHLILKNV KYLGADIEVT PPHKPVEELK KFDCVIFSGG PYSVSEEIQK
     MGNSPLYIKE LKVPMLGICL GHQLIAYVLG GVVRRALNPE YGLTRINIFD EDTILKGFSQ
     QLNVWESHND EVVEPPSGFR VLASSANARV QAMANSSNSI FGVQFHPEVK HTERGIEIFK
     NFLGVCRK
//

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