GenomeNet

Database: UniProt/SWISS-PROT
Entry: MAAI_HUMAN
LinkDB: MAAI_HUMAN
Original site: MAAI_HUMAN 
ID   MAAI_HUMAN              Reviewed;         216 AA.
AC   O43708; A6NED0; A6NNB8; A8MWD7; B2RCK3; O15308; O75430; Q6IB17;
AC   Q7Z610; Q9BV63;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 3.
DT   13-FEB-2019, entry version 197.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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,
RP   AND 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
RT   from plants to humans.";
RL   Biochem. J. 328:929-935(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS GLU-32;
RP   GLY-42 AND THR-82.
RX   PubMed=9925947;
RA   Blackburn A.C., Woollatt E., Sutherland G.R., Board P.G.;
RT   "Characterization and chromosome location of the gene GSTZ1 encoding
RT   the 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
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP   GLY-42 AND 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;
RP   GLY-42; 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.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   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.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   GLU-32 AND 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
RT   project: 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
RT   carcinogen 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
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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.,
RA   Buerckstuemmer T., 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
RP   MASS 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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal 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.,
RA   Wang S.P., Rossignol F., Berthier M.T., Giguere Y., Waters P.J.,
RA   Mitchell G.A.;
RT   "Hypersuccinylacetonaemia and normal liver function in
RT   maleylacetoacetate 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
RT   transferase 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
RT   transferase zeta reveals the molecular basis for its remarkable
RT   catalytic promiscuity.";
RL   Biochemistry 40:1567-1576(2001).
CC   -!- FUNCTION: Bifunctional enzyme showing minimal glutathione-
CC       conjugating activity with ethacrynic acid and 7-chloro-4-
CC       nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase
CC       activity. Has also low glutathione peroxidase activity with T-
CC       butyl and cumene hydroperoxides. Is able to catalyze the
CC       glutathione dependent oxygenation of dichloroacetic acid to
CC       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       Self; NbExp=4; IntAct=EBI-748043, EBI-748043;
CC       P16333:NCK1; NbExp=2; IntAct=EBI-748043, EBI-389883;
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         Note=Gene prediction based on EST data.;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in liver followed by kidney,
CC       skeletal muscle and brain. Also expressed in melanocytes,
CC       synovium, placenta, breast and fetal liver and heart.
CC   -!- DISEASE: Maleylacetoacetate isomerase deficiency (MAAID)
CC       [MIM:617596]: An autosomal recessive inborn error of metabolism
CC       characterized by mild elevations in succinylacetone in blood and
CC       urine, usually identified by newborn screening. Liver function and
CC       coagulation are normal. MAAID is a benign disorder.
CC       {ECO:0000269|PubMed:27876694}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/gstz1/";
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   UniGene; Hs.655292; -.
DR   PDB; 1FW1; X-ray; 1.90 A; A=1-216.
DR   PDBsum; 1FW1; -.
DR   ProteinModelPortal; O43708; -.
DR   SMR; O43708; -.
DR   BioGrid; 109209; 9.
DR   IntAct; O43708; 14.
DR   MINT; O43708; -.
DR   STRING; 9606.ENSP00000216465; -.
DR   ChEMBL; CHEMBL4949; -.
DR   DrugBank; DB00143; Glutathione.
DR   iPTMnet; O43708; -.
DR   PhosphoSitePlus; O43708; -.
DR   BioMuta; GSTZ1; -.
DR   EPD; O43708; -.
DR   jPOST; O43708; -.
DR   MaxQB; O43708; -.
DR   PaxDb; O43708; -.
DR   PeptideAtlas; O43708; -.
DR   PRIDE; O43708; -.
DR   ProteomicsDB; 49126; -.
DR   ProteomicsDB; 49127; -. [O43708-2]
DR   DNASU; 2954; -.
DR   Ensembl; ENST00000361389; ENSP00000354959; ENSG00000100577. [O43708-2]
DR   Ensembl; ENST00000393734; ENSP00000377335; ENSG00000100577. [O43708-2]
DR   Ensembl; ENST00000557639; ENSP00000451927; ENSG00000100577. [O43708-2]
DR   GeneID; 2954; -.
DR   KEGG; hsa:2954; -.
DR   UCSC; uc001xtj.4; human. [O43708-1]
DR   CTD; 2954; -.
DR   DisGeNET; 2954; -.
DR   EuPathDB; HostDB:ENSG00000100577.18; -.
DR   GeneCards; GSTZ1; -.
DR   HGNC; HGNC:4643; GSTZ1.
DR   HPA; HPA004701; -.
DR   MalaCards; GSTZ1; -.
DR   MIM; 603758; gene.
DR   MIM; 617596; phenotype.
DR   neXtProt; NX_O43708; -.
DR   OpenTargets; ENSG00000100577; -.
DR   PharmGKB; PA29031; -.
DR   eggNOG; KOG0868; Eukaryota.
DR   eggNOG; COG0625; LUCA.
DR   GeneTree; ENSGT00390000006580; -.
DR   HOGENOM; HOG000125758; -.
DR   HOVERGEN; HBG001501; -.
DR   InParanoid; O43708; -.
DR   KO; K01800; -.
DR   OrthoDB; 1283865at2759; -.
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   Reactome; R-HSA-156590; Glutathione conjugation.
DR   Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-HSA-71182; Phenylalanine and tyrosine catabolism.
DR   UniPathway; UPA00139; UER00340.
DR   ChiTaRS; GSTZ1; human.
DR   EvolutionaryTrace; O43708; -.
DR   GeneWiki; GSTZ1; -.
DR   GenomeRNAi; 2954; -.
DR   PRO; PR:O43708; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000100577; Expressed in 208 organ(s), highest expression level in right lobe of liver.
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:0019120; F:hydrolase activity, acting on acid halide bonds, in C-halide compounds; TAS:Reactome.
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:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
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:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
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; Complete proteome;
KW   Cytoplasm; Disease mutation; Isomerase; Multifunctional enzyme;
KW   Phenylalanine catabolism; Phosphoprotein; Polymorphism;
KW   Reference proteome; Transferase; Tyrosine catabolism.
FT   CHAIN         1    216       Maleylacetoacetate isomerase.
FT                                /FTId=PRO_0000186022.
FT   DOMAIN        4     87       GST N-terminal.
FT   DOMAIN       92    212       GST C-terminal.
FT   REGION       14     19       Glutathione binding.
FT   REGION       71     72       Glutathione binding.
FT   REGION      115    117       Glutathione binding.
FT   BINDING      45     45       Glutathione.
FT                                {ECO:0000269|PubMed:11327815}.
FT   BINDING      59     59       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000269|PubMed:11327815}.
FT   BINDING     111    111       Glutathione.
FT                                {ECO:0000269|PubMed:11327815}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES      32     32       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
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     177    177       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9WVL0}.
FT   VAR_SEQ       1     55       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_039862.
FT   VAR_SEQ      73    114       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_047392.
FT   VARIANT      32     32       K -> E (in allele GSTZ1*C; dbSNP:rs7975).
FT                                {ECO:0000269|PubMed:10739172,
FT                                ECO:0000269|PubMed:12508121,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9925947,
FT                                ECO:0000269|Ref.7, ECO:0000269|Ref.9}.
FT                                /FTId=VAR_009705.
FT   VARIANT      42     42       R -> G (in allele GSTZ1*B and allele
FT                                GSTZ1*C; dbSNP:rs7972).
FT                                {ECO:0000269|PubMed:10373324,
FT                                ECO:0000269|PubMed:10739172,
FT                                ECO:0000269|PubMed:12508121,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9417084,
FT                                ECO:0000269|PubMed:9925947,
FT                                ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT                                ECO:0000269|Ref.9}.
FT                                /FTId=VAR_009706.
FT   VARIANT      82     82       M -> T (in dbSNP:rs1046428).
FT                                {ECO:0000269|PubMed:10373324,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:9396740,
FT                                ECO:0000269|PubMed:9417084,
FT                                ECO:0000269|PubMed:9925947,
FT                                ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
FT                                /FTId=VAR_009707.
FT   VARIANT      87    216       Missing (in MAAID).
FT                                {ECO:0000269|PubMed:27876694}.
FT                                /FTId=VAR_079259.
FT   VARIANT      99     99       V -> M (in MAAID; decreased
FT                                maleylacetoacetate isomerase activity).
FT                                {ECO:0000269|PubMed:27876694}.
FT                                /FTId=VAR_079260.
FT   VARIANT     133    133       N -> H (in dbSNP:rs2234955).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_014505.
FT   VARIANT     150    150       A -> V (in MAAID; decreased
FT                                maleylacetoacetate isomerase activity).
FT                                {ECO:0000269|PubMed:27876694}.
FT                                /FTId=VAR_079261.
FT   STRAND        7     10       {ECO:0000244|PDB:1FW1}.
FT   HELIX        15     26       {ECO:0000244|PDB:1FW1}.
FT   STRAND       32     35       {ECO:0000244|PDB:1FW1}.
FT   HELIX        44     46       {ECO:0000244|PDB:1FW1}.
FT   HELIX        48     53       {ECO:0000244|PDB:1FW1}.
FT   STRAND       61     64       {ECO:0000244|PDB:1FW1}.
FT   STRAND       67     71       {ECO:0000244|PDB:1FW1}.
FT   HELIX        72     82       {ECO:0000244|PDB:1FW1}.
FT   HELIX        93    109       {ECO:0000244|PDB:1FW1}.
FT   HELIX       111    114       {ECO:0000244|PDB:1FW1}.
FT   HELIX       116    122       {ECO:0000244|PDB:1FW1}.
FT   HELIX       124    149       {ECO:0000244|PDB:1FW1}.
FT   STRAND      150    156       {ECO:0000244|PDB:1FW1}.
FT   HELIX       161    175       {ECO:0000244|PDB:1FW1}.
FT   HELIX       184    194       {ECO:0000244|PDB:1FW1}.
FT   HELIX       197    199       {ECO:0000244|PDB:1FW1}.
FT   TURN        200    202       {ECO:0000244|PDB:1FW1}.
FT   HELIX       204    206       {ECO:0000244|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
//
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