ID MAAI_HUMAN Reviewed; 216 AA. AC O43708; A6NED0; A6NNB8; A8MWD7; B2RCK3; O15308; O75430; Q6IB17; Q7Z610; AC Q9BV63; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 3. DT 27-MAR-2024, entry version 226. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND VARIANTS RP GLY-42 AND THR-82. RX PubMed=9417084; DOI=10.1074/jbc.273.1.329; RA Fernandez-Canon J.M., Penalva M.A.; RT "Characterization of a fungal maleylacetoacetate isomerase gene and RT identification of its human homologue."; RL J. Biol. Chem. 273:329-337(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT THR-82, AND RP CHARACTERIZATION. RX PubMed=9396740; DOI=10.1042/bj3280929; RA Board P.G., Baker R.T., Chelvanayagam G., Jermiin L.S.; RT "Zeta, a novel class of glutathione transferases in a range of species from RT plants to humans."; RL Biochem. J. 328:929-935(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS GLU-32; GLY-42 RP AND THR-82. RX PubMed=9925947; DOI=10.1159/000015145; RA Blackburn A.C., Woollatt E., Sutherland G.R., Board P.G.; RT "Characterization and chromosome location of the gene GSTZ1 encoding the RT human zeta class glutathione transferase and maleylacetoacetate RT isomerase."; RL Cytogenet. Cell Genet. 83:109-114(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS GLY-42 AND RP THR-82. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-82. RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-42 AND RP THR-82. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS GLU-32; GLY-42; RP THR-82 AND HIS-133. RG NIEHS SNPs program; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-32 AND RP GLY-42. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-32 AND RP GLY-42. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-32 AND RP GLY-42. RC TISSUE=Placenta; 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 [11] RP CHARACTERIZATION. 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP INVOLVEMENT IN MAAID, VARIANTS MAAID 87-ARG--ALA-216 DEL; MET-99 AND RP VAL-150, AND CHARACTERIZATION OF VARIANTS MAAID MET-99 AND VAL-150. RX PubMed=27876694; DOI=10.1136/jmedgenet-2016-104289; RG Quebec NTBC Study Group; RA Yang H., Al-Hertani W., Cyr D., Laframboise R., Parizeault G., Wang S.P., RA Rossignol F., Berthier M.T., Giguere Y., Waters P.J., Mitchell G.A.; RT "Hypersuccinylacetonaemia and normal liver function in maleylacetoacetate RT isomerase deficiency."; RL J. Med. Genet. 54:241-247(2017). RN [16] RP VARIANTS GLU-32 AND GLY-42, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10739172; DOI=10.1097/00008571-200002000-00007; RA Blackburn A.C., Tzeng H.F., Anders M.W., Board P.G.; RT "Discovery of a functional polymorphism in human glutathione transferase RT zeta by expressed sequence tag database analysis."; RL Pharmacogenetics 10:49-57(2000). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND RP SUBUNIT. RX PubMed=11327815; DOI=10.1021/bi002249z; RA Polekhina G., Board P.G., Blackburn A.C., Parker M.W.; RT "Crystal structure of maleylacetoacetate isomerase/glutathione transferase RT zeta reveals the molecular basis for its remarkable catalytic RT promiscuity."; RL Biochemistry 40:1567-1576(2001). CC -!- FUNCTION: Bifunctional enzyme showing minimal glutathione-conjugating CC activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3- CC diazole and maleylacetoacetate isomerase activity. Has also low CC glutathione peroxidase activity with T-butyl and cumene hydroperoxides. CC Is able to catalyze the glutathione dependent oxygenation of CC dichloroacetic acid to glyoxylic acid. {ECO:0000269|PubMed:10739172}. 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:10739172}; 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:10739172}; CC -!- COFACTOR: CC Name=glutathione; Xref=ChEBI:CHEBI:57925; CC Note=Glutathione is required for the MAAI activity.; CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 5/6. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11327815}. CC -!- INTERACTION: CC O43708; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-748043, EBI-12357161; CC O43708; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-748043, EBI-739467; CC O43708; O43708: GSTZ1; NbExp=7; IntAct=EBI-748043, EBI-748043; CC O43708; P16333: NCK1; NbExp=2; IntAct=EBI-748043, EBI-389883; CC O43708; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-748043, EBI-949255; CC O43708; P47897: QARS1; NbExp=3; IntAct=EBI-748043, EBI-347462; CC O43708; Q8WWU5-7: TCP11; NbExp=3; IntAct=EBI-748043, EBI-17721485; CC O43708; Q12933: TRAF2; NbExp=3; IntAct=EBI-748043, EBI-355744; CC O43708; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-748043, EBI-12030590; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O43708-1; Sequence=Displayed; CC Name=2; CC IsoId=O43708-2; Sequence=VSP_039862; CC Name=3; CC IsoId=O43708-3; Sequence=VSP_047392; CC -!- TISSUE SPECIFICITY: Mostly expressed in liver followed by kidney, CC skeletal muscle and brain. Also expressed in melanocytes, synovium, CC placenta, breast and fetal liver and heart. CC -!- DISEASE: Maleylacetoacetate isomerase deficiency (MAAID) [MIM:617596]: CC An autosomal recessive inborn error of metabolism characterized by mild CC elevations in succinylacetone in blood and urine, usually identified by CC newborn screening. Liver function and coagulation are normal. MAAID is CC a benign disorder. {ECO:0000269|PubMed:27876694}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/gstz1/"; 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; AJ001838; CAA05045.1; -; mRNA. DR EMBL; U86529; AAB96392.1; -; mRNA. DR EMBL; AF053545; AAC33591.1; -; Genomic_DNA. DR EMBL; AF053539; AAC33591.1; JOINED; Genomic_DNA. DR EMBL; AF053540; AAC33591.1; JOINED; Genomic_DNA. DR EMBL; AF053541; AAC33591.1; JOINED; Genomic_DNA. DR EMBL; AF053542; AAC33591.1; JOINED; Genomic_DNA. DR EMBL; AF053543; AAC33591.1; JOINED; Genomic_DNA. DR EMBL; AF053544; AAC33591.1; JOINED; Genomic_DNA. DR EMBL; AF098318; AAD43007.1; -; Genomic_DNA. DR EMBL; AF095582; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AF098311; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AF098312; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AF098313; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AF098314; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AF098315; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AF098316; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AF098317; AAD43007.1; JOINED; Genomic_DNA. DR EMBL; AK315154; BAG37600.1; -; mRNA. DR EMBL; CR456987; CAG33268.1; -; mRNA. DR EMBL; AY316305; AAP69526.1; -; Genomic_DNA. DR EMBL; AC007954; AAF62559.1; -; Genomic_DNA. DR EMBL; CH471061; EAW81278.1; -; Genomic_DNA. DR EMBL; CH471061; EAW81279.1; -; Genomic_DNA. DR EMBL; BC001453; AAH01453.1; -; mRNA. DR CCDS; CCDS9858.1; -. [O43708-1] DR CCDS; CCDS9859.1; -. [O43708-3] DR CCDS; CCDS9860.1; -. [O43708-2] DR RefSeq; NP_001299589.1; NM_001312660.1. [O43708-2] DR RefSeq; NP_665877.1; NM_145870.2. DR RefSeq; NP_665878.2; NM_145871.2. DR PDB; 1FW1; X-ray; 1.90 A; A=1-216. DR PDB; 8E8P; X-ray; 2.28 A; A/B=1-216. DR PDBsum; 1FW1; -. DR PDBsum; 8E8P; -. DR AlphaFoldDB; O43708; -. DR SMR; O43708; -. DR BioGRID; 109209; 23. DR IntAct; O43708; 16. DR MINT; O43708; -. DR STRING; 9606.ENSP00000451976; -. DR ChEMBL; CHEMBL4949; -. DR DrugBank; DB04447; 1,4-Dithiothreitol. DR DrugBank; DB08809; Dichloroacetic acid. DR DrugBank; DB00143; Glutathione. DR DrugBank; DB09462; Glycerin. DR iPTMnet; O43708; -. DR PhosphoSitePlus; O43708; -. DR SwissPalm; O43708; -. DR BioMuta; GSTZ1; -. DR EPD; O43708; -. DR jPOST; O43708; -. DR MassIVE; O43708; -. DR MaxQB; O43708; -. DR PaxDb; 9606-ENSP00000216465; -. DR PeptideAtlas; O43708; -. DR ProteomicsDB; 49126; -. [O43708-1] DR ProteomicsDB; 49127; -. [O43708-2] DR ProteomicsDB; 976; -. DR Pumba; O43708; -. DR Antibodypedia; 188; 277 antibodies from 29 providers. DR DNASU; 2954; -. DR Ensembl; ENST00000361389.8; ENSP00000354959.4; ENSG00000100577.19. [O43708-2] DR Ensembl; ENST00000393734.5; ENSP00000377335.1; ENSG00000100577.19. [O43708-2] DR Ensembl; ENST00000557639.5; ENSP00000451927.1; ENSG00000100577.19. [O43708-2] DR GeneID; 2954; -. DR KEGG; hsa:2954; -. DR UCSC; uc001xtj.4; human. [O43708-1] DR AGR; HGNC:4643; -. DR CTD; 2954; -. DR DisGeNET; 2954; -. DR GeneCards; GSTZ1; -. DR HGNC; HGNC:4643; GSTZ1. DR HPA; ENSG00000100577; Tissue enriched (liver). DR MalaCards; GSTZ1; -. DR MIM; 603758; gene. DR MIM; 617596; phenotype. DR neXtProt; NX_O43708; -. DR OpenTargets; ENSG00000100577; -. DR PharmGKB; PA29031; -. DR VEuPathDB; HostDB:ENSG00000100577; -. DR eggNOG; KOG0868; Eukaryota. DR GeneTree; ENSGT00390000006580; -. DR HOGENOM; CLU_011226_20_3_1; -. DR InParanoid; O43708; -. DR OrthoDB; 986565at2759; -. DR PhylomeDB; O43708; -. DR TreeFam; TF105324; -. DR BioCyc; MetaCyc:HS02114-MONOMER; -. DR BRENDA; 2.5.1.18; 2681. DR BRENDA; 5.2.1.2; 2681. DR PathwayCommons; O43708; -. DR Reactome; R-HSA-156590; Glutathione conjugation. DR Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex. DR Reactome; R-HSA-8963684; Tyrosine catabolism. DR SignaLink; O43708; -. DR UniPathway; UPA00139; UER00340. DR BioGRID-ORCS; 2954; 18 hits in 1164 CRISPR screens. DR ChiTaRS; GSTZ1; human. DR EvolutionaryTrace; O43708; -. DR GeneWiki; GSTZ1; -. DR GenomeRNAi; 2954; -. DR Pharos; O43708; Tbio. DR PRO; PR:O43708; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; O43708; Protein. DR Bgee; ENSG00000100577; Expressed in right lobe of liver and 186 other cell types or tissues. DR ExpressionAtlas; O43708; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004602; F:glutathione peroxidase activity; TAS:ProtInc. DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB. 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; O43708; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Disease variant; Isomerase; Multifunctional enzyme; KW Phenylalanine catabolism; Phosphoprotein; Reference proteome; Transferase; KW Tyrosine catabolism. FT CHAIN 1..216 FT /note="Maleylacetoacetate isomerase" FT /id="PRO_0000186022" 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|PubMed:11327815" FT BINDING 59 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:11327815" 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|PubMed:11327815" FT BINDING 115..117 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 32 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" 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 177 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9WVL0" FT VAR_SEQ 1..55 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039862" FT VAR_SEQ 73..114 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_047392" FT VARIANT 32 FT /note="K -> E (in allele GSTZ1*C; dbSNP:rs7975)" FT /evidence="ECO:0000269|PubMed:10739172, FT ECO:0000269|PubMed:12508121, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9925947, ECO:0000269|Ref.7, FT ECO:0000269|Ref.9" FT /id="VAR_009705" FT VARIANT 42 FT /note="R -> G (in allele GSTZ1*B and allele GSTZ1*C; FT dbSNP:rs7972)" FT /evidence="ECO:0000269|PubMed:10373324, FT ECO:0000269|PubMed:10739172, ECO:0000269|PubMed:12508121, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9417084, FT ECO:0000269|PubMed:9925947, ECO:0000269|Ref.6, FT ECO:0000269|Ref.7, ECO:0000269|Ref.9" FT /id="VAR_009706" FT VARIANT 82 FT /note="M -> T (in dbSNP:rs1046428)" FT /evidence="ECO:0000269|PubMed:10373324, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9396740, FT ECO:0000269|PubMed:9417084, ECO:0000269|PubMed:9925947, FT ECO:0000269|Ref.6, ECO:0000269|Ref.7" FT /id="VAR_009707" FT VARIANT 87..216 FT /note="Missing (in MAAID)" FT /evidence="ECO:0000269|PubMed:27876694" FT /id="VAR_079259" FT VARIANT 99 FT /note="V -> M (in MAAID; decreased maleylacetoacetate FT isomerase activity)" FT /evidence="ECO:0000269|PubMed:27876694" FT /id="VAR_079260" FT VARIANT 133 FT /note="N -> H (in dbSNP:rs2234955)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_014505" FT VARIANT 150 FT /note="A -> V (in MAAID; decreased maleylacetoacetate FT isomerase activity)" FT /evidence="ECO:0000269|PubMed:27876694" FT /id="VAR_079261" FT STRAND 7..10 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 15..26 FT /evidence="ECO:0007829|PDB:1FW1" FT STRAND 32..35 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 48..53 FT /evidence="ECO:0007829|PDB:1FW1" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:1FW1" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 72..82 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 93..109 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 116..122 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 124..149 FT /evidence="ECO:0007829|PDB:1FW1" FT STRAND 150..156 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 161..175 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:1FW1" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:1FW1" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:1FW1" SQ SEQUENCE 216 AA; 24212 MW; 2B3112B8AE6B55E0 CRC64; MQAGKPILYS YFRSSCSWRV RIALALKGID YKTVPINLIK DRGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE EMRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA //