GenomeNet

Database: UniProt/SWISS-PROT
Entry: MAAI_MOUSE
LinkDB: MAAI_MOUSE
Original site: MAAI_MOUSE 
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   23-MAY-2018, entry version 156.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RP   BY 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
RT   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.,
RA   Zhang Y., 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
RT   (maleylacetoacetate isomerase) from Mus musculus (form-1 crystal).";
RL   Submitted (FEB-2009) to the PDB data bank.
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. Is able to catalyze the
CC       glutathione dependent oxygenation of dichloroacetic acid to
CC       glyoxylic acid (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 4-maleylacetoacetate = 4-fumarylacetoacetate.
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
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.
CC       {ECO:0000305}.
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   UniGene; Mm.29652; -.
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   ProteinModelPortal; Q9WVL0; -.
DR   SMR; Q9WVL0; -.
DR   BioGrid; 200105; 1.
DR   IntAct; Q9WVL0; 5.
DR   MINT; Q9WVL0; -.
DR   STRING; 10090.ENSMUSP00000053540; -.
DR   iPTMnet; Q9WVL0; -.
DR   PhosphoSitePlus; Q9WVL0; -.
DR   SwissPalm; Q9WVL0; -.
DR   EPD; Q9WVL0; -.
DR   MaxQB; Q9WVL0; -.
DR   PaxDb; Q9WVL0; -.
DR   PeptideAtlas; Q9WVL0; -.
DR   PRIDE; Q9WVL0; -.
DR   TopDownProteomics; Q9WVL0; -.
DR   Ensembl; ENSMUST00000063117; ENSMUSP00000053540; ENSMUSG00000021033.
DR   GeneID; 14874; -.
DR   KEGG; mmu:14874; -.
DR   UCSC; uc007oil.1; mouse.
DR   CTD; 2954; -.
DR   MGI; MGI:1341859; Gstz1.
DR   eggNOG; KOG0868; Eukaryota.
DR   eggNOG; COG0625; LUCA.
DR   GeneTree; ENSGT00390000006580; -.
DR   HOGENOM; HOG000125758; -.
DR   HOVERGEN; HBG001501; -.
DR   InParanoid; Q9WVL0; -.
DR   KO; K01800; -.
DR   OMA; CRQPDTP; -.
DR   OrthoDB; EOG091G0QFQ; -.
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-71182; Phenylalanine and tyrosine catabolism.
DR   UniPathway; UPA00139; UER00340.
DR   ChiTaRS; Gstz1; mouse.
DR   EvolutionaryTrace; Q9WVL0; -.
DR   PRO; PR:Q9WVL0; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000021033; -.
DR   ExpressionAtlas; Q9WVL0; baseline and differential.
DR   Genevisible; Q9WVL0; MM.
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; TAS:MGI.
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   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   3D-structure; Acetylation; Complete proteome; Cytoplasm; Isomerase;
KW   Multifunctional enzyme; Phenylalanine catabolism; Phosphoprotein;
KW   Reference proteome; Transferase; Tyrosine catabolism.
FT   CHAIN         1    216       Maleylacetoacetate isomerase.
FT                                /FTId=PRO_0000186023.
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. {ECO:0000269|Ref.7}.
FT   BINDING      59     59       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000269|Ref.7}.
FT   BINDING     111    111       Glutathione. {ECO:0000269|Ref.7}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:O43708}.
FT   MOD_RES      57     57       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     136    136       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17242355}.
FT   MOD_RES     137    137       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     177    177       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     181    181       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355}.
FT   STRAND        7     10       {ECO:0000244|PDB:2CZ2}.
FT   HELIX        15     26       {ECO:0000244|PDB:2CZ2}.
FT   STRAND       32     35       {ECO:0000244|PDB:2CZ2}.
FT   HELIX        40     42       {ECO:0000244|PDB:2CZ2}.
FT   HELIX        44     46       {ECO:0000244|PDB:2CZ2}.
FT   HELIX        48     53       {ECO:0000244|PDB:2CZ2}.
FT   STRAND       61     64       {ECO:0000244|PDB:2CZ2}.
FT   STRAND       67     71       {ECO:0000244|PDB:2CZ2}.
FT   HELIX        72     82       {ECO:0000244|PDB:2CZ2}.
FT   HELIX        93    109       {ECO:0000244|PDB:2CZ2}.
FT   HELIX       111    114       {ECO:0000244|PDB:2CZ2}.
FT   HELIX       116    122       {ECO:0000244|PDB:2CZ2}.
FT   TURN        124    126       {ECO:0000244|PDB:2CZ2}.
FT   HELIX       127    149       {ECO:0000244|PDB:2CZ2}.
FT   STRAND      150    156       {ECO:0000244|PDB:2CZ2}.
FT   HELIX       161    175       {ECO:0000244|PDB:2CZ2}.
FT   HELIX       184    194       {ECO:0000244|PDB:2CZ2}.
FT   HELIX       197    200       {ECO:0000244|PDB:2CZ2}.
FT   HELIX       204    206       {ECO:0000244|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
//
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