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 01-MAY-2013, entry version 66.
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; 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 (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 glutamine amidotransferase type-1 domain.
CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase)
CC domain.
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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; TCMFIDH; -.
DR ProtClustDB; PRK00074; -.
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; 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 DOMAIN 206 395 GMPS ATP-PPase.
FT NP_BIND 233 239 ATP (By similarity).
FT ACT_SITE 89 89 Nucleophile (By similarity).
FT ACT_SITE 179 179 By similarity.
FT ACT_SITE 181 181 By similarity.
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
//
