MAAI_HUMAN
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 03-AUG-2022, entry version 217.
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/";
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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 PDBsum; 1FW1; -.
DR AlphaFoldDB; O43708; -.
DR SMR; O43708; -.
DR BioGRID; 109209; 20.
DR IntAct; O43708; 16.
DR MINT; O43708; -.
DR STRING; 9606.ENSP00000216465; -.
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 BioMuta; GSTZ1; -.
DR EPD; O43708; -.
DR jPOST; O43708; -.
DR MassIVE; O43708; -.
DR MaxQB; O43708; -.
DR PaxDb; O43708; -.
DR PeptideAtlas; O43708; -.
DR PRIDE; O43708; -.
DR ProteomicsDB; 49126; -. [O43708-1]
DR ProteomicsDB; 49127; -. [O43708-2]
DR ProteomicsDB; 976; -.
DR Antibodypedia; 188; 243 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 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 PhylomeDB; O43708; -.
DR TreeFam; TF105324; -.
DR BioCyc; MetaCyc:HS02114-MON; -.
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; 16 hits in 1084 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 184 other tissues.
DR ExpressionAtlas; O43708; baseline and differential.
DR Genevisible; O43708; HS.
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 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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 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
