ID   MAAI_MOUSE              Reviewed;         216 AA.
AC   Q9WVL0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 184.
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; Synonyms=Maai;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10373324; DOI=10.1006/geno.1999.5832;
RA   Fernandez-Canon J.M., Hejna J., Reifsteck C., Olson S., Grompe M.;
RT   "Gene structure, chromosomal location, and expression pattern of
RT   maleylacetoacetate isomerase.";
RL   Genomics 58:263-269(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136 AND SER-181, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57 AND LYS-177, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP   SUBUNIT.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate
RT   isomerase) from Mus musculus (form-1 crystal).";
RL   Submitted (FEB-2009) to the PDB data bank.
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. Is able to catalyze the glutathione dependent
CC       oxygenation of dichloroacetic acid to glyoxylic acid (By similarity).
CC       {ECO:0000250}.
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   -!- 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   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
CC       Note=Glutathione is required for the MAAI activity. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 5/6.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney, seminal glands and
CC       breast.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR   EMBL; AF093418; AAD43846.1; -; mRNA.
DR   EMBL; AK002398; BAB22070.1; -; mRNA.
DR   EMBL; AK075927; BAC36059.1; -; mRNA.
DR   EMBL; BC031777; AAH31777.1; -; mRNA.
DR   CCDS; CCDS26071.1; -.
DR   RefSeq; NP_001239484.1; NM_001252555.1.
DR   RefSeq; NP_001239485.1; NM_001252556.1.
DR   RefSeq; NP_034493.1; NM_010363.4.
DR   PDB; 2CZ2; X-ray; 1.40 A; A=1-216.
DR   PDB; 2CZ3; X-ray; 2.30 A; A/B=1-216.
DR   PDBsum; 2CZ2; -.
DR   PDBsum; 2CZ3; -.
DR   AlphaFoldDB; Q9WVL0; -.
DR   SMR; Q9WVL0; -.
DR   BioGRID; 200105; 3.
DR   STRING; 10090.ENSMUSP00000053540; -.
DR   iPTMnet; Q9WVL0; -.
DR   PhosphoSitePlus; Q9WVL0; -.
DR   SwissPalm; Q9WVL0; -.
DR   EPD; Q9WVL0; -.
DR   jPOST; Q9WVL0; -.
DR   MaxQB; Q9WVL0; -.
DR   PaxDb; 10090-ENSMUSP00000053540; -.
DR   PeptideAtlas; Q9WVL0; -.
DR   ProteomicsDB; 252709; -.
DR   Pumba; Q9WVL0; -.
DR   TopDownProteomics; Q9WVL0; -.
DR   Antibodypedia; 188; 277 antibodies from 29 providers.
DR   DNASU; 14874; -.
DR   Ensembl; ENSMUST00000063117.10; ENSMUSP00000053540.9; ENSMUSG00000021033.12.
DR   GeneID; 14874; -.
DR   KEGG; mmu:14874; -.
DR   UCSC; uc007oil.1; mouse.
DR   AGR; MGI:1341859; -.
DR   CTD; 2954; -.
DR   MGI; MGI:1341859; Gstz1.
DR   VEuPathDB; HostDB:ENSMUSG00000021033; -.
DR   eggNOG; KOG0868; Eukaryota.
DR   GeneTree; ENSGT00390000006580; -.
DR   HOGENOM; CLU_011226_20_1_1; -.
DR   InParanoid; Q9WVL0; -.
DR   OMA; VYNAHRF; -.
DR   OrthoDB; 986565at2759; -.
DR   PhylomeDB; Q9WVL0; -.
DR   TreeFam; TF105324; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-MMU-8963684; Tyrosine catabolism.
DR   UniPathway; UPA00139; UER00340.
DR   BioGRID-ORCS; 14874; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Gstz1; mouse.
DR   EvolutionaryTrace; Q9WVL0; -.
DR   PRO; PR:Q9WVL0; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9WVL0; Protein.
DR   Bgee; ENSMUSG00000021033; Expressed in gonadal fat pad and 267 other cell types or tissues.
DR   ExpressionAtlas; Q9WVL0; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0016034; F:maleylacetoacetate isomerase activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR   GO; GO:0006572; P:tyrosine catabolic process; TAS:MGI.
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; Q9WVL0; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isomerase; Multifunctional enzyme;
KW   Phenylalanine catabolism; Phosphoprotein; Reference proteome; Transferase;
KW   Tyrosine catabolism.
FT   CHAIN           1..216
FT                   /note="Maleylacetoacetate isomerase"
FT                   /id="PRO_0000186023"
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   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|Ref.7"
FT   BINDING         59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|Ref.7"
FT   BINDING         71..72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT   BINDING         111
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|Ref.7"
FT   BINDING         115..117
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
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:0007744|PubMed:23806337"
FT   MOD_RES         136
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         177
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           48..53
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           72..82
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           93..109
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           111..114
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           116..122
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           127..149
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   STRAND          150..156
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           161..175
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           184..194
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:2CZ2"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:2CZ2"
SQ   SEQUENCE   216 AA;  24275 MW;  BDB1E6C07981E855 CRC64;
     MQAGKPILYS YFRSSCSWRV RIALALKGID YEIVPINLIK DGGQQFTEEF QTLNPMKQVP
     ALKIDGITIV QSLAIMEYLE ETRPIPRLLP QDPQKRAIVR MISDLIASGI QPLQNLSVLK
     QVGQENQMQW AQKVITSGFN ALEKILQSTA GKYCVGDEVS MADVCLVPQV ANAERFKVDL
     SPYPTISHIN KELLALEVFQ VSHPRRQPDT PAELRT
//