ID   GSH1_PSEF5              Reviewed;         532 AA.
AC   Q4KK14;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=PFL_0273;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(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.
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DR   EMBL; CP000076; AAY95684.1; -; Genomic_DNA.
DR   RefSeq; YP_257419.1; -.
DR   GeneID; 3480866; -.
DR   GenomeReviews; CP000076_GR; PFL_0273.
DR   KEGG; pfl:PFL_0273; -.
DR   NMPDR; fig|220664.3.peg.1759; -.
DR   HOGENOM; Q4KK14; -.
DR   OMA; Q4KK14; DTLYLPY.
DR   BioCyc; PFLU220664:PFL_0273-MON; -.
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    532       Glutamate--cysteine ligase.
FT                                /FTId=PRO_1000025180.
SQ   SEQUENCE   532 AA;  59803 MW;  3E9B99EFDAF10151 CRC64;
     MKESNLSELL NRRLALLGER ANLSLLEQCL HGIERECLRV TGEGRLAQTP HPEELGSALT
     NEQITTDYSE SLLEFITPAL KDPADTLASL DKIHRFAYSK LGNEYLWSPS MPCPLPAEED
     IPIAYYGTSN IGQLKYVYRK GLALRYGKTM QCIAGIHYNF SLPEQLWPLL KQAEGFVGTD
     RDYQSSAYIA LIRNFRRYSW LLMYLFGASP ALDAGFLRGR SHQLEQLDAE TLYLPYATSL
     RMSDLGYQSK AQAGLTPCYN DLNSYTDSLR KAVATPYAPY VEVGTHKDGE WVQLNTNILQ
     IENEYYSNIR PKRVTYTGER PIQALMARGI QYVEVRCLDI NPFLPLGIDI QEARFLDAFL
     LYCALNDSPL FENNECGNAT SNFLAVVKEG RRPGLQLQRQ GQPVEMKEWA AQLLEQIAPL
     AALLDQSHGS DVHSKALDAQ LAKVKDSSLT PSAQVLAAMS EHKESFTQFS LRQSQAHAEY
     FRSQTLSKEE QAAFEEAARK SLEQQTELEQ NEVGDFDVFV GAYQASILAI SN
//