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 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   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.
DR   Genevisible; P57113; RN.
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
//