MAAI1_DROME
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 03-AUG-2022, entry version 157.
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}.
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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; Q9VHD3; -.
DR PRIDE; Q9VHD3; -.
DR DNASU; 41132; -.
DR EnsemblMetazoa; FBtr0082044; FBpp0081522; FBgn0037696.
DR GeneID; 41132; -.
DR KEGG; dme:Dmel_CG9362; -.
DR UCSC; CG9362-RA; d. melanogaster.
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; 1283865at2759; -.
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 tissues.
DR Genevisible; Q9VHD3; DM.
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 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 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
