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Database: UniProt/TrEMBL
Entry: G8STS6_BRUCA
LinkDB: G8STS6_BRUCA
Original site: G8STS6_BRUCA 
ID   G8STS6_BRUCA            Unreviewed;       520 AA.
AC   G8STS6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   11-JUN-2014, entry version 20.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; ORFNames=BCA52141_II0686;
OS   Brucella canis HSK A52141.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=1104321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A52141;
RA   Kim J.-S., Jeong W., Kim H., Baek J.-H., Vinuselvi P., Lee S.K.,
RA   Kim J.W., Kim J.-Y., Jung S.C., Her M., An D.-J.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A52141;
RX   PubMed=22933762; DOI=10.1128/JB.01125-12;
RA   Kim J.S., Jeong W., Jeoung H.Y., Song J.Y., Kim H., Beak J.H.,
RA   Parisutham V., Lee S.K., Kim J.W., Kim J.Y., Jung S.C., Her M.,
RA   An D.J.;
RT   "Complete Genome Sequence of Brucella canis Strain HSK A52141,
RT   Isolated from the Blood of an Infected Dog.";
RL   J. Bacteriol. 194:5134-5134(2012).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP +
CC       diphosphate + GMP + L-glutamate.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase)
CC       domain.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- SIMILARITY: Contains GMPS ATP-PPase (ATP pyrophosphatase) domain.
CC   -!- SIMILARITY: Contains glutamine amidotransferase type-1 domain.
CC   -!- SIMILARITY: Contains glutamine amidotransferase type-domain.
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DR   EMBL; CP003175; AEW15603.1; -; Genomic_DNA.
DR   RefSeq; YP_005152996.1; NC_016796.1.
DR   ProteinModelPortal; G8STS6; -.
DR   SMR; G8STS6; 7-520.
DR   EnsemblBacteria; AEW15603; AEW15603; BCA52141_II0686.
DR   GeneID; 11726591; -.
DR   KEGG; bsk:BCA52141_II0686; -.
DR   KO; K01951; -.
DR   BioCyc; BCAN1104321:GJV1-2617-MONOMER; -.
DR   UniPathway; UPA00189; UER00296.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00344; GMP_synthase; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_N.
DR   InterPro; IPR022955; GMP_synthase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutamine amidotransferase;
KW   GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   DOMAIN        9    202       Glutamine amidotransferase type-1 (By
FT                                similarity).
FT   DOMAIN      203    395       GMPS ATP-PPase (By similarity).
FT   NP_BIND     230    236       ATP (By similarity){EA2}.
FT   ACT_SITE     86     86       Nucleophile (By similarity){EA2}.
FT   ACT_SITE    176    176       By similarity{EA2}.
FT   ACT_SITE    178    178       By similarity{EA2}.
SQ   SEQUENCE   520 AA;  57069 MW;  1EC07D39D0731EC2 CRC64;
     MSTTAYPDTI LIIDFGSQVT QLIARRVREA NVYCEIVPFQ SADEAFKRLQ PKGVILSGSP
     HSTTDIGSPR APQAIFDAGI PVLGICYGEQ TMCAQLGGNV ESGHDREFGR AFLDVQEDSP
     LFAGIWAKGT RHQVWMSHGD RVTSLPDGFT IIGTSPNAPY AVIADEKRKY YGVQFHPEVV
     HTPDGAKLLQ NFVHRIVGVK PGWTMGAYRE QAVEAIRKQV GSGKVICALS GGVDSSVAAL
     LAHEAVGDQL TCILVDHGLM RKDEAQQVVE MFREHYNLPL ILVDASDRFI GALEGESDPE
     KKRKTIGRLF IEVFEEEARK LGGADFLVQG TLYPDVIESV SFTGGPSVTI KSHHNVGGLP
     ERMKMQLVEP LRELFKDEVR LLGKELGLPD SFIGRHPFPG PGLAIRCPGG VTRGKLEILR
     EADAIYLDEI RKAGLYDAIW QAFAVLLPVQ TVGVMGDGRT YEFVCALRAV TSVDGMTADF
     YHYDMNFLGN AATRIINEVR GINRVVYDVT SKPPGTIEWE
//
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