MAAI2_DROME
ID MAAI2_DROME Reviewed; 227 AA.
AC Q9VHD2; H0RNF8; H8F4P9; Q8INN9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Probable maleylacetoacetate isomerase 2;
DE Short=MAAI 2;
DE EC=5.2.1.2;
DE AltName: Full=Glutathione S-transferase zeta 2;
DE EC=2.5.1.18;
GN Name=GstZ2; ORFNames=CG9363;
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Ovary;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the glutathione dependent oxygenation of
CC dichloroacetic acid to glyoxylic acid in vitro. Has no glutathione
CC thioltransferase activity with 4-hydroxynonenal (4-HNE), 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 -!- INTERACTION:
CC Q9VHD2; Q8INR0: stck; NbExp=4; IntAct=EBI-154819, EBI-116495;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q9VHD2-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VHD2-2; Sequence=VSP_010291;
CC Name=C;
CC IsoId=Q9VHD2-3; Sequence=VSP_010292;
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC {ECO:0000269|PubMed:22082028}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28280.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEV23904.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF54382.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13429.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65133.1; -; Genomic_DNA.
DR EMBL; AY060732; AAL28280.2; ALT_INIT; mRNA.
DR EMBL; BT132880; AEV23904.1; ALT_INIT; mRNA.
DR EMBL; BT133289; AFC88878.1; -; mRNA.
DR RefSeq; NP_649895.1; NM_141638.3. [Q9VHD2-1]
DR RefSeq; NP_731358.1; NM_169286.2. [Q9VHD2-2]
DR RefSeq; NP_996190.1; NM_206468.2. [Q9VHD2-3]
DR AlphaFoldDB; Q9VHD2; -.
DR SMR; Q9VHD2; -.
DR BioGRID; 66294; 1.
DR DIP; DIP-24005N; -.
DR IntAct; Q9VHD2; 3.
DR STRING; 7227.FBpp0081520; -.
DR PaxDb; Q9VHD2; -.
DR PRIDE; Q9VHD2; -.
DR DNASU; 41133; -.
DR EnsemblMetazoa; FBtr0082041; FBpp0081519; FBgn0037697. [Q9VHD2-2]
DR EnsemblMetazoa; FBtr0082042; FBpp0081520; FBgn0037697. [Q9VHD2-1]
DR EnsemblMetazoa; FBtr0082043; FBpp0081521; FBgn0037697. [Q9VHD2-3]
DR GeneID; 41133; -.
DR KEGG; dme:Dmel_CG9363; -.
DR UCSC; CG9363-RA; d. melanogaster. [Q9VHD2-1]
DR CTD; 41133; -.
DR FlyBase; FBgn0037697; GstZ2.
DR VEuPathDB; VectorBase:FBgn0037697; -.
DR eggNOG; KOG0868; Eukaryota.
DR GeneTree; ENSGT00390000006580; -.
DR InParanoid; Q9VHD2; -.
DR OMA; LHIDNHT; -.
DR PhylomeDB; Q9VHD2; -.
DR Reactome; R-DME-156590; Glutathione conjugation.
DR Reactome; R-DME-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-DME-8963684; Tyrosine catabolism.
DR SignaLink; Q9VHD2; -.
DR UniPathway; UPA00139; UER00340.
DR BioGRID-ORCS; 41133; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41133; -.
DR PRO; PR:Q9VHD2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037697; Expressed in insect adult head and 12 other tissues.
DR ExpressionAtlas; Q9VHD2; baseline and differential.
DR Genevisible; Q9VHD2; 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 Alternative splicing; Cytoplasm; Isomerase; Phenylalanine catabolism;
KW Reference proteome; Transferase; Tyrosine catabolism.
FT CHAIN 1..227
FT /note="Probable maleylacetoacetate isomerase 2"
FT /id="PRO_0000186027"
FT DOMAIN 14..97
FT /note="GST N-terminal"
FT DOMAIN 102..222
FT /note="GST C-terminal"
FT BINDING 24..29
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 81..82
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 125..127
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..15
FT /note="MSTNLCPNASSSDIQ -> MSLSAIAK (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_010291"
FT VAR_SEQ 1..15
FT /note="MSTNLCPNASSSDIQ -> MNH (in isoform C)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_010292"
SQ SEQUENCE 227 AA; 25975 MW; C708DD764F48C754 CRC64;
MSTNLCPNAS SSDIQPILYS YWRSSCSWRV RIAMNLKEIP YDIKPISLIK SGGEQHCNEY
REVNPMEQVP ALQIDGHTLI ESVAIMHYLE ETRPQRPLLP QDVHKRAKVR EIVEIICSGI
QPLQNLIVLI HVGEEKKKEW AQHWITRGFR AVEKALSTSA GKYCVGDEIS MADCCLVPQV
FNARRFHVDL RPYPIILRID RELESNPAFR AAHPSNQPDC PPELPNK
