ID MAAI1_DROME Reviewed; 246 AA. AC Q9VHD3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 162. DE RecName: Full=Probable maleylacetoacetate isomerase 1; DE Short=MAAI 1; DE EC=5.2.1.2; DE AltName: Full=Glutathione S-transferase zeta 1; DE EC=2.5.1.18; GN Name=GstZ1; ORFNames=CG9362; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND RP DEVELOPMENTAL STAGE. RX PubMed=22082028; DOI=10.1042/bj20111747; RA Saisawang C., Wongsantichon J., Ketterman A.J.; RT "A preliminary characterization of the cytosolic glutathione transferase RT proteome from Drosophila melanogaster."; RL Biochem. J. 442:181-190(2012). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Catalyzes the glutathione dependent oxygenation of CC dichloroacetic acid to glyoxylic acid in vitro. Possesses low CC glutathione thioltransferase activity toward 4-hydroxynonenal (4-HNE). CC Has no glutathione thioltransferase activity with adrenochrome, CC phenethyl isothiocyanate (PEITC), 5-hydroperoxyeicosatetraenoic acid CC ((5S)-HpETE), prostaglandin A2 (PGA2) or 2-hydroxyethyldisulfide (HED). CC {ECO:0000269|PubMed:22082028}. 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:22082028}; 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:22082028}; CC -!- COFACTOR: CC Name=glutathione; Xref=ChEBI:CHEBI:57925; CC Evidence={ECO:0000269|PubMed:22082028}; CC Note=Glutathione is required for the MAAI activity. CC {ECO:0000269|PubMed:22082028}; CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 5/6. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis. CC {ECO:0000269|PubMed:22082028}. CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}. 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; AE014297; AAF54381.1; -; Genomic_DNA. DR EMBL; AY061527; AAL29075.1; -; mRNA. DR RefSeq; NP_649894.1; NM_141637.3. DR AlphaFoldDB; Q9VHD3; -. DR SMR; Q9VHD3; -. DR BioGRID; 66293; 2. DR STRING; 7227.FBpp0081522; -. DR PaxDb; 7227-FBpp0081522; -. DR DNASU; 41132; -. DR EnsemblMetazoa; FBtr0082044; FBpp0081522; FBgn0037696. DR GeneID; 41132; -. DR KEGG; dme:Dmel_CG9362; -. DR UCSC; CG9362-RA; d. melanogaster. DR AGR; FB:FBgn0037696; -. DR CTD; 2954; -. DR FlyBase; FBgn0037696; GstZ1. DR VEuPathDB; VectorBase:FBgn0037696; -. DR eggNOG; KOG0868; Eukaryota. DR GeneTree; ENSGT00390000006580; -. DR HOGENOM; CLU_011226_20_1_1; -. DR InParanoid; Q9VHD3; -. DR OMA; VYNAHRF; -. DR OrthoDB; 986565at2759; -. DR PhylomeDB; Q9VHD3; -. DR UniPathway; UPA00139; UER00340. DR BioGRID-ORCS; 41132; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 41132; -. DR PRO; PR:Q9VHD3; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0037696; Expressed in Malpighian tubule and 16 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0004364; F:glutathione transferase activity; IDA:FlyBase. DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; ISS:FlyBase. DR GO; GO:0006749; P:glutathione metabolic process; IDA:FlyBase. 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; Q9VHD3; DM. PE 1: Evidence at protein level; KW Cytoplasm; Isomerase; Phenylalanine catabolism; Reference proteome; KW Transferase; Tyrosine catabolism. FT CHAIN 1..246 FT /note="Probable maleylacetoacetate isomerase 1" FT /id="PRO_0000186026" FT DOMAIN 32..116 FT /note="GST N-terminal" FT DOMAIN 121..241 FT /note="GST C-terminal" FT BINDING 42..47 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 88 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 100..101 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 140 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 144..146 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" SQ SEQUENCE 246 AA; 27890 MW; 9DEBC10717E380E4 CRC64; MASATQLTHR GIHLAGLYRS SWSKPLFRHL ATKPILYSYW PSSCSWRVRV ALAIKKIDYD IKPTSLLKTV SGHAYTDEYR EVNPMQKVPS LKIDGHTLCD SVAIIHYLEE TRPQPALLPQ DPVKRAKIRE IVELICSGIQ PLQNVSVLDH IGKDQSLQWA QHWISRGFQG LEKVLSHSAG KFCVGDELSM ADICLVPQVR NARRYKADLT PYPTIVRLNQ ELQELDVFKA THPSTQPDCP PEFAKK //