ID   GSH1_PSE14              Reviewed;         535 AA.
AC   Q48PX1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Glutamate--cysteine ligase;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-glutamylcysteine synthetase;
DE   AltName: Full=Gamma-ECS;
DE            Short=GCS;
GN   Name=gshA; OrderedLocusNames=PSPPH_0243;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP +
CC       phosphate + gamma-L-glutamyl-L-cysteine.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1
CC       family. Type 1 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000058; AAZ34309.1; -; Genomic_DNA.
DR   RefSeq; YP_272548.1; -.
DR   GeneID; 3556857; -.
DR   GenomeReviews; CP000058_GR; PSPPH_0243.
DR   KEGG; psp:PSPPH_0243; -.
DR   NMPDR; fig|264730.3.peg.732; -.
DR   HOGENOM; Q48PX1; -.
DR   OMA; Q48PX1; DTLYLPY.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:HAMAP.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00578; -; 1.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    535       Glutamate--cysteine ligase.
FT                                /FTId=PRO_1000025176.
SQ   SEQUENCE   535 AA;  60081 MW;  191AAA74067CC62A CRC64;
     MKDYTLSELL NRRLALLGER NNLSLLEQCL HGIERECLRV TATAELAQTP HPQALGAALT
     NGQVTTDYSE SLLEFITPAL KNPAETIDSL DKIHRFAYSK LGDELLWSPS MPCPLPDEEH
     TPIAYYGTSN IGKLKYVYRK GLALRYGKTM QCIAGIHYNF SLPEDAWALL KQTEDFAGDA
     RDYQSHSYIA LIRNFRRYSW LLMYLFGASP ALDAGFLRGR KHQLEQHFDA DTLYLPYATS
     LRMSDLGYQS DAQADLTPCY NDLVSYTDSL RKAVATPYKP YVDVGTHDQN GEWVQLNTNV
     LQIENEYYSN IRPKRATYSG ERPIQALVAR GVQYVEVRCL DINPFLPTGI SLEQSRFIDA
     FVLYCALEES QQLASHECSN ASSNFLAVVK EGRRPGLSLQ RNNSPVDLKT WATELLEKIT
     PIARLLDQAQ GIDEHIKSIA VQQAKIDDAS LTPSAQVLAS MKAHNEGFTA FSLRQSQAHA
     EYFRTHPLSA QEQADFEAQA KTSIEEQAEL EATEEVVDFD TFVGSYQASI LSISN
//