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GSH1_WIGBR
ID   GSH1_WIGBR              Reviewed;         505 AA.
AC   Q8D2V5;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
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}; OrderedLocusNames=WIGBR2470;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24393.1; -; Genomic_DNA.
DR   RefSeq; WP_011070051.1; NC_004344.2.
DR   AlphaFoldDB; Q8D2V5; -.
DR   SMR; Q8D2V5; -.
DR   STRING; 36870.25166202; -.
DR   EnsemblBacteria; BAC24393; BAC24393; BAC24393.
DR   KEGG; wbr:gshA; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000562; 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..505
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192546"
SQ   SEQUENCE   505 AA;  59745 MW;  065BE526813EDF2B CRC64;
     MIPKVSKIIP WIKDNKKFLK KTYKGIERES LRIDIDGNIS KKPHPIIFGS PLTHNWITTD
     FSESLLELIT PVSNSKKYTI NFLNDLHIFI IKNLINENLW PMSMPCKINN DSSIIIAQYG
     NSKLGRTKTI YRNGLKNRYG AKMQIISGVH YNFSFHKDFW KKYNNFYKIQ DKFSSIGYFN
     LIRNYYRFGW IIPYFFGASP IAHSSFFKGL NTDLIFKKNK FGDIYLPFST SLRLSEIGYI
     NKVQKKIKLK FNNIEEYVDI VKKAMKTPYL NYKKIELKNN EKNLQINVNL LQKENELYSH
     VRPKRSLNKN KYKLEDLIYK GIEYIEIRSL DVNPFSPIGI KINQIYFLDI FLIWCILIES
     PKINDEELRS INENWNRVIL YGRNPKIKLI NFFKKKEKKL SEILKFILND LQILVESLAF
     KKNNKIYQKI FFDLHKMTDN PNKTLSGKLL EESIEYGVER LGLDMSKSHK INIENKKLKV
     INYQSLIKEA EKSIKEQIVL EKNET
 
 
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