GenomeNet

Database: UniProt/SWISS-PROT
Entry: MAAI_RAT
LinkDB: MAAI_RAT
Original site: MAAI_RAT 
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   23-MAY-2018, entry version 109.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   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
RT   project: 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
RT   carcinogen 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.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Probable bifunctional enzyme showing minimal
CC       glutathione-conjugating activity with ethacrynic acid and 7-
CC       chloro-4-nitrobenz-2-oxa-1, 3-diazole and maleylacetoacetate
CC       isomerase activity. Has also low glutathione peroxidase activity
CC       with t-butyl and cumene hydroperoxides (By similarity). Is able to
CC       catalyze the glutathione dependent oxygenation of dichloroacetic
CC       acid to glyoxylic acid. {ECO:0000250, ECO:0000269|PubMed:9531472}.
CC   -!- CATALYTIC ACTIVITY: 4-maleylacetoacetate = 4-fumarylacetoacetate.
CC       {ECO:0000269|PubMed:9531472}.
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC       {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.
CC       {ECO:0000305}.
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   UniGene; Rn.216913; -.
DR   ProteinModelPortal; P57113; -.
DR   SMR; P57113; -.
DR   STRING; 10116.ENSRNOP00000065390; -.
DR   iPTMnet; P57113; -.
DR   PhosphoSitePlus; P57113; -.
DR   PaxDb; P57113; -.
DR   PRIDE; P57113; -.
DR   Ensembl; ENSRNOT00000072215; ENSRNOP00000065390; ENSRNOG00000047708.
DR   GeneID; 681913; -.
DR   KEGG; rno:681913; -.
DR   CTD; 2954; -.
DR   RGD; 1589363; Gstz1.
DR   eggNOG; KOG0868; Eukaryota.
DR   eggNOG; COG0625; LUCA.
DR   GeneTree; ENSGT00390000006580; -.
DR   HOVERGEN; HBG001501; -.
DR   InParanoid; P57113; -.
DR   KO; K01800; -.
DR   OMA; CRQPDTP; -.
DR   OrthoDB; EOG091G0QFQ; -.
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-71182; Phenylalanine and tyrosine catabolism.
DR   UniPathway; UPA00139; UER00340.
DR   PRO; PR:P57113; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000047708; -.
DR   ExpressionAtlas; P57113; baseline and differential.
DR   Genevisible; P57113; RN.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016034; F:maleylacetoacetate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
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; 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   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   Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Isomerase; Multifunctional enzyme; Phenylalanine catabolism;
KW   Phosphoprotein; Reference proteome; Transferase; Tyrosine catabolism.
FT   CHAIN         1    216       Maleylacetoacetate isomerase.
FT                                /FTId=PRO_0000186024.
FT   DOMAIN        4     87       GST N-terminal.
FT   DOMAIN       92    212       GST C-terminal.
FT   REGION       14     19       Glutathione binding. {ECO:0000250}.
FT   REGION       71     72       Glutathione binding. {ECO:0000250}.
FT   REGION      115    117       Glutathione binding. {ECO:0000250}.
FT   BINDING      45     45       Glutathione. {ECO:0000250}.
FT   BINDING      59     59       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000250}.
FT   BINDING     111    111       Glutathione. {ECO:0000250}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:O43708}.
FT   MOD_RES      57     57       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9WVL0}.
FT   MOD_RES     136    136       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9WVL0}.
FT   MOD_RES     137    137       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     177    177       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9WVL0}.
FT   MOD_RES     181    181       Phosphoserine.
FT                                {ECO:0000244|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
//
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