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