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MAAI_CAEEL
ID   MAAI_CAEEL              Reviewed;         214 AA.
AC   Q18938;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Probable maleylacetoacetate isomerase;
DE            Short=MAAI;
DE            EC=5.2.1.2;
DE   AltName: Full=Glutathione S-transferase gst-42;
GN   Name=gst-42; ORFNames=D1053.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-maleylacetoacetate = 4-fumarylacetoacetate;
CC         Xref=Rhea:RHEA:14817, ChEBI:CHEBI:17105, ChEBI:CHEBI:18034;
CC         EC=5.2.1.2;
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 5/6.
CC   -!- INTERACTION:
CC       Q18938; Q18938: gst-42; NbExp=3; IntAct=EBI-318532, EBI-318532;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR   EMBL; Z66560; CAA91449.1; -; Genomic_DNA.
DR   PIR; T20294; T20294.
DR   RefSeq; NP_509962.1; NM_077561.6.
DR   AlphaFoldDB; Q18938; -.
DR   SMR; Q18938; -.
DR   BioGRID; 48718; 19.
DR   DIP; DIP-24905N; -.
DR   IntAct; Q18938; 3.
DR   STRING; 6239.D1053.1; -.
DR   EPD; Q18938; -.
DR   PaxDb; Q18938; -.
DR   PeptideAtlas; Q18938; -.
DR   EnsemblMetazoa; D1053.1.1; D1053.1.1; WBGene00001790.
DR   GeneID; 183911; -.
DR   KEGG; cel:CELE_D1053.1; -.
DR   UCSC; D1053.1; c. elegans.
DR   CTD; 183911; -.
DR   WormBase; D1053.1; CE03099; WBGene00001790; gst-42.
DR   eggNOG; KOG0868; Eukaryota.
DR   GeneTree; ENSGT00390000006580; -.
DR   HOGENOM; CLU_011226_20_1_1; -.
DR   InParanoid; Q18938; -.
DR   OMA; CCQRIII; -.
DR   OrthoDB; 1283865at2759; -.
DR   PhylomeDB; Q18938; -.
DR   Reactome; R-CEL-156590; Glutathione conjugation.
DR   Reactome; R-CEL-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-CEL-8963684; Tyrosine catabolism.
DR   UniPathway; UPA00139; UER00340.
DR   PRO; PR:Q18938; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00001790; Expressed in larva and 4 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016034; F:maleylacetoacetate isomerase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03191; GST_C_Zeta; 1.
DR   CDD; cd03042; GST_N_Zeta; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR005955; GST_Zeta.
DR   InterPro; IPR034330; GST_Zeta_C.
DR   InterPro; IPR034333; GST_Zeta_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01262; maiA; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isomerase; Phenylalanine catabolism; Reference proteome;
KW   Tyrosine catabolism.
FT   CHAIN           1..214
FT                   /note="Probable maleylacetoacetate isomerase"
FT                   /id="PRO_0000186025"
FT   DOMAIN          4..84
FT                   /note="GST N-terminal"
FT   DOMAIN          89..212
FT                   /note="GST C-terminal"
FT   BINDING         14..19
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..69
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         112..114
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  23656 MW;  EF1CB1EE62EF41EB CRC64;
     MSNQKPVLYS YWRSSCSWRV RIALALKNVD YEYKTVDLLS EEAKSKLKEI NPAAKVPTFV
     VDGQVITESL AIIEYLEETH PDVPLLPKDP IKRAHARAIS LLVASGIQPL HNLKVLQLLN
     KKEAGFGGQF AKQFVVEGLT ALEILLKQHS GKYAVGDDVT IADLSIPPLI YSANRFNLDL
     SPYPTVNRIN ETLADIPAFI AAHPDNQPDT GLNA
 
 
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