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Database: UniProt
Entry: Q92SN3
LinkDB: Q92SN3
Original site: Q92SN3 
ID   GSHB_RHIME              Reviewed;         315 AA.
AC   Q92SN3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-FEB-2019, entry version 93.
DE   RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162};
DE   AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00162};
DE   AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00162};
GN   Name=gshB {ECO:0000255|HAMAP-Rule:MF_00162}; OrderedLocusNames=R00338;
GN   ORFNames=SMc00419;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.,
RA   Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA   Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont
RT   Sinorhizobium meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F.,
RA   Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M.,
RA   Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D.,
RA   Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V.,
RA   Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B.,
RA   Ramsperger U., Surzycki R., Thebault P., Vandenbol M.,
RA   Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP +
CC         glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00162};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00162}.
CC   -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00162}.
DR   EMBL; AL591688; CAC41775.1; -; Genomic_DNA.
DR   RefSeq; NP_384444.1; NC_003047.1.
DR   RefSeq; WP_003529770.1; NC_003047.1.
DR   ProteinModelPortal; Q92SN3; -.
DR   SMR; Q92SN3; -.
DR   STRING; 266834.SMc00419; -.
DR   EnsemblBacteria; CAC41775; CAC41775; SMc00419.
DR   GeneID; 1231972; -.
DR   KEGG; sme:SMc00419; -.
DR   PATRIC; fig|266834.11.peg.1709; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OMA; WMRKDPP; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00162; GSH_S; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006284; Glut_synth_pro.
DR   InterPro; IPR004218; GSHS_ATP-bd.
DR   InterPro; IPR004215; GSHS_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR21621:SF4; PTHR21621:SF4; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01380; glut_syn; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    315       Glutathione synthetase.
FT                                /FTId=PRO_0000197481.
FT   DOMAIN      127    311       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00162}.
FT   NP_BIND     153    209       ATP. {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       282    282       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       284    284       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
SQ   SEQUENCE   315 AA;  35317 MW;  32666BD118EB4087 CRC64;
     MAGIVNVGVQ MDHVSGITIA GDSTFAMSLE AQARGYRLFH YTPDKLSLRD GRVYATAQQM
     QLRDVRGDHF TLGEDERIDL STMDVILLRQ DPPFDMAYIT STHLLERLHP KTLVVNDPAW
     VRNSPEKIFV TEFPDLMPKT LITRDPDEIA RFRQEMGDII LKPLYGNGGA GVFHSARDDR
     NFSSLLEMFA QMFREPYIAQ EYLPAVRKGD KRILLVDGEP VGAINRVPAE HDSRSNMHVG
     GRAEATDLTA REREICTRIG PALKERGFLF VGIDVIGDYL TEINVTSPTG IREVKKFGGA
     DVASLLWDAI EKKRA
//
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