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 03-AUG-2022, entry version 177.
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, Pancreas,
RC 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; Q9WVL0; -.
DR PeptideAtlas; Q9WVL0; -.
DR PRIDE; Q9WVL0; -.
DR ProteomicsDB; 252709; -.
DR TopDownProteomics; Q9WVL0; -.
DR Antibodypedia; 188; 243 antibodies from 29 providers.
DR DNASU; 14874; -.
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 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; 1283865at2759; -.
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 75 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 265 other tissues.
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; 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 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; PF02798; GST_N; 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; 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
