ID MAAI_RAT Reviewed; 216 AA.
AC P57113; B0BNI1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 24-JAN-2024, entry version 133.
DE RecName: Full=Maleylacetoacetate isomerase;
DE Short=MAAI;
DE EC=5.2.1.2;
DE AltName: Full=GSTZ1-1;
DE AltName: Full=Glutathione S-transferase zeta 1;
DE EC=2.5.1.18;
GN Name=Gstz1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Li G., Xie P.;
RT "Microcystin-induced variations in transcription of GSTs in Wistar rat.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 131-158, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND BLOCKAGE OF
RP N-TERMINUS.
RC STRAIN=Fischer 344; TISSUE=Liver;
RX PubMed=9531472; DOI=10.1042/bj3310371;
RA Tong Z., Board P.G., Anders M.W.;
RT "Glutathione transferase zeta catalyses the oxygenation of the carcinogen
RT dichloroacetic acid to glyoxylic acid.";
RL Biochem. J. 331:371-374(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probable bifunctional enzyme showing minimal glutathione-
CC conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-
CC oxa-1, 3-diazole and maleylacetoacetate isomerase activity. Has also
CC low glutathione peroxidase activity with t-butyl and cumene
CC hydroperoxides (By similarity). Is able to catalyze the glutathione
CC dependent oxygenation of dichloroacetic acid to glyoxylic acid.
CC {ECO:0000250, ECO:0000269|PubMed:9531472}.
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; Evidence={ECO:0000269|PubMed:9531472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:9531472};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
CC Note=Glutathione is required for the MAAI activity. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=71.4 uM for dichloroacetic acid {ECO:0000269|PubMed:9531472};
CC KM=59.0 uM for glutathione {ECO:0000269|PubMed:9531472};
CC Vmax=1334 nmol/min/mg enzyme {ECO:0000269|PubMed:9531472};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 5/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9531472}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR EMBL; FJ179410; ACI32127.1; -; mRNA.
DR EMBL; CH473982; EDL81627.1; -; Genomic_DNA.
DR EMBL; BC158833; AAI58834.1; -; mRNA.
DR RefSeq; NP_001102915.1; NM_001109445.1.
DR AlphaFoldDB; P57113; -.
DR SMR; P57113; -.
DR IntAct; P57113; 1.
DR STRING; 10116.ENSRNOP00000065390; -.
DR ChEMBL; CHEMBL4630822; -.
DR iPTMnet; P57113; -.
DR PhosphoSitePlus; P57113; -.
DR SwissPalm; P57113; -.
DR jPOST; P57113; -.
DR PaxDb; 10116-ENSRNOP00000065390; -.
DR GeneID; 681913; -.
DR KEGG; rno:681913; -.
DR AGR; RGD:1589363; -.
DR CTD; 2954; -.
DR RGD; 1589363; Gstz1.
DR VEuPathDB; HostDB:ENSRNOG00000047708; -.
DR eggNOG; KOG0868; Eukaryota.
DR InParanoid; P57113; -.
DR OrthoDB; 986565at2759; -.
DR PhylomeDB; P57113; -.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR Reactome; R-RNO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-RNO-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00340.
DR PRO; PR:P57113; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000047708; Expressed in liver and 20 other cell types or tissues.
DR ExpressionAtlas; P57113; baseline and differential.
DR Genevisible; P57113; RN.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
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 Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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 NCBIfam; TIGR01262; maiA; 1.
DR PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isomerase;
KW Multifunctional enzyme; Phenylalanine catabolism; Phosphoprotein;
KW Reference proteome; Transferase; Tyrosine catabolism.
FT CHAIN 1..216
FT /note="Maleylacetoacetate isomerase"
FT /id="PRO_0000186024"
FT DOMAIN 4..87
FT /note="GST N-terminal"
FT DOMAIN 92..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 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 71..72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 115..117
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43708"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL0"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL0"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 177
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL0"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 216 AA; 23961 MW; 3E02041A8E3749A3 CRC64;
MQAGKPVLYS YFRSSCSWRV RIALALKGID YEIVPINLIK DGGQQFSEEF QTLNPMKQVP
ALKIDGITIG QSLAILEYLE ETRPIPRLLP QDPQKRAIVR MISDLIASGI QPLQNLSVLK
QVGQENQMPW AQKAITSGFN ALEKILQSTA GKYCVGDEVS MADVCLAPQV ANAERFKVDL
SPYPTISHIN KALLALEAFQ VSHPCRQPDT PAELRT
//
