ID G8STS6_BRUCA Unreviewed; 520 AA.
AC G8STS6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-APR-2013, entry version 12.
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 + xanthosine 5'-phosphate + L-glutamine +
CC H(2)O = AMP + 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.
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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 UniPathway; UPA00189; UER00296.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:HAMAP.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00344; GMP_synthase; 1; -.
DR InterPro; IPR017926; GATASE_1.
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 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; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW 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).
FT ACT_SITE 86 86 Nucleophile (By similarity).
FT ACT_SITE 176 176 By similarity.
FT ACT_SITE 178 178 By similarity.
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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