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Database: UniProt/SWISS-PROT
Entry: GUAA_STRPD
LinkDB: GUAA_STRPD
Original site: GUAA_STRPD 
ID   GUAA_STRPD              Reviewed;         520 AA.
AC   Q1JGP6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   26-NOV-2014, entry version 77.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344};
GN   OrderedLocusNames=MGAS10270_Spy1033;
OS   Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10270;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F.,
RA   DeLeo F.R., Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in
RT   the human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP +
CC       diphosphate + GMP + L-glutamate. {ECO:0000255|HAMAP-
CC       Rule:MF_00344}.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase)
CC       domain. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR   EMBL; CP000260; ABF34098.1; -; Genomic_DNA.
DR   RefSeq; YP_598642.1; NC_008022.1.
DR   ProteinModelPortal; Q1JGP6; -.
DR   STRING; 370552.MGAS10270_Spy1033; -.
DR   EnsemblBacteria; ABF34098; ABF34098; MGAS10270_Spy1033.
DR   GeneID; 4063277; -.
DR   KEGG; sph:MGAS10270_Spy1033; -.
DR   PATRIC; 19719988; VBIStrPyo120482_1051.
DR   eggNOG; COG0519; -.
DR   HOGENOM; HOG000223964; -.
DR   KO; K01951; -.
DR   OMA; KIYGLQF; -.
DR   OrthoDB; EOG6JHRJV; -.
DR   BioCyc; SPYO370552:GHYF-1088-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   CHAIN         1    520       GMP synthase [glutamine-hydrolyzing].
FT                                /FTId=PRO_1000120432.
FT   DOMAIN       12    205       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00344}.
FT   DOMAIN      206    395       GMPS ATP-PPase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00344}.
FT   NP_BIND     233    239       ATP. {ECO:0000255|HAMAP-Rule:MF_00344}.
FT   ACT_SITE     89     89       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00344}.
FT   ACT_SITE    179    179       {ECO:0000255|HAMAP-Rule:MF_00344}.
FT   ACT_SITE    181    181       {ECO:0000255|HAMAP-Rule:MF_00344}.
SQ   SEQUENCE   520 AA;  57479 MW;  68FD2F7DBAB42C7D CRC64;
     MTEISILNDV QKIIVLDYGS QYNQLIARRI REFGVLSELK SHKITAQELH EINPIGIVLS
     GGPNSVYADN AFGIDPEIFE LGIPILGICY GMQLITHKLG GKVVPAGQAG NREYGQSTLH
     LRETSKLFSG TPQEQLVLMS HGDAVTEIPE GFHLVGDSND CPYAAIENTE KNLYGIQFHP
     EVRHSVYGND ILKNFAISIC GARGDWSMDN FIDMEITKIR ETVGDRKVLL GLSGGVDSSV
     VGVLLQKAIG DQLTCIFVDH GLLRKDEGDQ VMGMLGGKFG LNIIRVDASK RFLDLLADVE
     DPEKKRKIIG NEFVYVFDDE ASKLKGVDFL AQGTLYTDII ESGTETAQTI KSHHNVGGLP
     EDMQFELIEP LNTLFKDEVR ALGIALGMPE EIVWRQPFPG PGLAIRVMGA ITEEKLETVR
     ESDAILREEI AKAGLDRDVW QYFTVNTGVR SVGVMGDGRT YDYTIAIRAI TSIDGMTADF
     AQLPWDVLKK ISTRIVNEVD HVNRIVYDIT SKPPATVEWE
//
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