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GSH1_KLEP7
ID   GSH1_KLEP7              Reviewed;         518 AA.
AC   A6TCV4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE            Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN   Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578};
GN   OrderedLocusNames=KPN78578_29640; ORFNames=KPN_03019;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00578};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00578}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC       Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
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DR   EMBL; CP000647; ABR78425.1; -; Genomic_DNA.
DR   RefSeq; WP_002914353.1; NC_009648.1.
DR   AlphaFoldDB; A6TCV4; -.
DR   SMR; A6TCV4; -.
DR   STRING; 272620.KPN_03019; -.
DR   EnsemblBacteria; ABR78425; ABR78425; KPN_03019.
DR   KEGG; kpn:KPN_03019; -.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000265; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00578; Glu_cys_ligase; 1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   PANTHER; PTHR38761; PTHR38761; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..518
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000025175"
SQ   SEQUENCE   518 AA;  58101 MW;  80276982F050682D CRC64;
     MIPDVSQALA WLEKHPQALQ GIQRGLERET LRVNADGTLA TTGHPPALGS ALTHKWITTD
     FAEALLEFIT PVDGDIEHML TFMRDVHRYT ARQLGDERMW PLSMPCYIAP GQDIELAQYG
     TSNVGRLKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGVEDAE SGKEAISAGY
     FRSIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTTLPFEE TGNGMYYLPY ATSLRLSDLG
     YTNKSQSNLG ITFNDLHEYV AGLKRAIKTP SEEYAKIGLQ KDGKYLQINS NILQIENELY
     APIRPKRVTR RGETPSDALL RGGIEYIEVR SLDINPFSPI GVDAQQVRFL DLFMVWCALA
     DAPEMSSDEL LCTRTNWNRV ILEGRKPGLT LGIGCESAQF PLAQVGKDLF RDLRRVAQTL
     DSIHGGQAYQ QVCDELLACF DDPELTFSAR ILRSMIEEGI GGTGRALADR YRTQLREEPL
     EILSEDDFIA ERDASVARQK KVEAEDSEPF EALLARHA
 
 
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