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GSH1_PSET1
ID   GSH1_PSET1              Reviewed;         525 AA.
AC   Q3IEB7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=PSHAa0937;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI86016.1; -; Genomic_DNA.
DR   RefSeq; WP_011327627.1; NC_007481.1.
DR   AlphaFoldDB; Q3IEB7; -.
DR   SMR; Q3IEB7; -.
DR   STRING; 326442.PSHAa0937; -.
DR   PRIDE; Q3IEB7; -.
DR   EnsemblBacteria; CAI86016; CAI86016; PSHAa0937.
DR   KEGG; pha:PSHAa0937; -.
DR   PATRIC; fig|326442.8.peg.898; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; REAMHEP; -.
DR   OrthoDB; 967793at2; -.
DR   BioCyc; PHAL326442:PSHA_RS04575-MON; -.
DR   BRENDA; 6.3.2.2; 5081.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000006843; Chromosome I.
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..525
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000146879"
SQ   SEQUENCE   525 AA;  59188 MW;  E380BE638BAC3ACC CRC64;
     MATHDLTNAL DALSVTQHKH AINGIKRGIE RESLRIKSDG VISAQKHPEG VGSALTNGQI
     TTDFSESLLE FITPVSESST QTLQQLKDLQ KFTLEKMGDE LLWPISMPCF IEHQDDIVIA
     QFGSSNVGQM KTLYREGLKN RYGSMMQAIA GVHFNISFPD SLWQSLHTLK NSDLSLEDFI
     SDGYLALIRN FKRELWLISY LFGASPALCS SFLQGRKTDL PFKKLGKGTL YLEVGTALRL
     GNLGYTNSAQ SSLRVMYNSL DEYVAGLKKS INTPSDIYGN LDDYTSENPK QLNKNILQIE
     NEFYSPIRPK RNAKNGETPT DALLRAGIEY VEIRALDVNP FSEVGIDIEQ FHFLDVFLTY
     CLLKSSPAMD WEEQTRSTEN LDTVVNKGRE KGLELNYFNQ PRTLQSWGED IFSQLSEVAK
     YMDTAYGVSY YSSTIERMAT WINNPGLTYS GRYVAELEAS GLDNGHYALA IAEKYKQSHQ
     AADYQVFSKQ WLEEQVTRSN DAQRAIEQSD SVSFTAFLNA YFDPK
 
 
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