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Database: UniProt/TrEMBL
Entry: F4EFD7_STRSU
LinkDB: F4EFD7_STRSU
Original site: F4EFD7_STRSU 
ID   F4EFD7_STRSU            Unreviewed;       516 AA.
AC   F4EFD7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   19-FEB-2014, entry version 24.
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=SSUST3_0996;
OS   Streptococcus suis ST3.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1007064;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ST3;
RX   PubMed=21572001; DOI=10.1128/JB.05018-11;
RA   Hu P., Yang M., Zhang A., Wu J., Chen B., Hua Y., Yu J., Chen H.,
RA   Xiao J., Jin M.;
RT   "Complete Genome Sequence of Streptococcus suis Serotype 3 Strain
RT   ST3.";
RL   J. Bacteriol. 193:3428-3429(2011).
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; CP002633; AEB81429.1; -; Genomic_DNA.
DR   RefSeq; YP_004401615.1; NC_015433.1.
DR   EnsemblBacteria; AEB81429; AEB81429; SSUST3_0996.
DR   GeneID; 10491165; -.
DR   KEGG; sst:SSUST3_0996; -.
DR   PATRIC; 54543114; VBIStrSui186933_0975.
DR   KO; K01951; -.
DR   BioCyc; SSUI1007064:GHXD-1022-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   HAMAP; MF_00344; GMP_synthase; 1.
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   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        8    201       Glutamine amidotransferase type-1 (By
FT                                similarity).
FT   DOMAIN      202    391       GMPS ATP-PPase (By similarity).
FT   NP_BIND     229    235       ATP (By similarity).
FT   ACT_SITE     85     85       Nucleophile (By similarity).
FT   ACT_SITE    175    175       By similarity.
FT   ACT_SITE    177    177       By similarity.
SQ   SEQUENCE   516 AA;  57136 MW;  223A0ED2834EB263 CRC64;
     MTKQDVQKII VLDYGSQYNQ LISRRIREFG VFSELKNHKI TAEEVRAINP IGIVLSGGPN
     SVYAENAFDI DPEIFELGIP ILGICYGMQL ITHKLVGKVV PAGEAGNREY GQSNLQLKTE
     SALFAGTPEE QLVLMSHGDA VTEIPADFHL VGLSADCPYA AIENTERRIY GIQFHPEVRH
     SVYGNDILKN FAFGICGAKG DWTMENFIET EIEKIRQTVG DKKVLLGLSG GVDSSVVGVL
     LQRAIGDQLT CIFVDHGLLR KNEGDQVMEM LGGKFGLNII RVDAAKRFLD LLAGVSDPEK
     KRKIIGNEFV YVFDDEASKL TDVEFLAQGT LYTDIIESGT DTAETIKSHH NVGGLPEDMQ
     FKLIEPLNTL FKDEVRALGT ALGMPDEVVW RQPFPGPGLA IRVMGEITEE KLQTVRESDA
     ILREEIAKAG LDRDVWQYFT VNTGVRSVGV MGDGRTYDYT IAIRAITSVD GMTADFAKLP
     WDVLQKISVR IVNEVDHVNR IVYDITSKPP ATVEWE
//
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