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Q9VHD2

- MAAI2_DROME

UniProt

Q9VHD2 - MAAI2_DROME

Protein

Probable maleylacetoacetate isomerase 2

Gene

GstZ2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid in vitro. Has no glutathione thioltransferase activity with 4-hydroxynonenal (4-HNE), adrenochrome, phenethyl isothiocyanate (PEITC), 5-hydroperoxyeicosatetraenoic acid ((5S)-HpETE), prostaglandin A2 (PGA2) or 2-hydroxyethyldisulfide (HED).1 Publication

    Catalytic activityi

    4-maleylacetoacetate = 4-fumarylacetoacetate.1 Publication
    RX + glutathione = HX + R-S-glutathione.1 Publication

    Cofactori

    Glutathione. Required for the MAAI activity.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551GlutathioneBy similarity
    Binding sitei69 – 691Glutathione; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei121 – 1211GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: FlyBase
    2. maleylacetoacetate isomerase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glutathione metabolic process Source: FlyBase
    2. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
    3. tyrosine catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Transferase

    Keywords - Biological processi

    Phenylalanine catabolism, Tyrosine catabolism

    Enzyme and pathway databases

    ReactomeiREACT_203229. Phenylalanine and tyrosine catabolism.
    UniPathwayiUPA00139; UER00340.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable maleylacetoacetate isomerase 2 (EC:5.2.1.2)
    Short name:
    MAAI 2
    Alternative name(s):
    Glutathione S-transferase zeta 2 (EC:2.5.1.18)
    Gene namesi
    Name:GstZ2
    ORF Names:CG9363
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0037697. GstZ2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 227227Probable maleylacetoacetate isomerase 2PRO_0000186027Add
    BLAST

    Proteomic databases

    PaxDbiQ9VHD2.
    PRIDEiQ9VHD2.

    Expressioni

    Developmental stagei

    Expressed during embryogenesis.1 Publication

    Gene expression databases

    BgeeiQ9VHD2.

    Interactioni

    Protein-protein interaction databases

    BioGridi66294. 1 interaction.
    DIPiDIP-24005N.
    IntActiQ9VHD2. 1 interaction.
    MINTiMINT-1563429.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VHD2.
    SMRiQ9VHD2. Positions 15-224.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 9784GST N-terminalAdd
    BLAST
    Domaini102 – 222121GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 296Glutathione bindingBy similarity
    Regioni81 – 822Glutathione bindingBy similarity
    Regioni125 – 1273Glutathione bindingBy similarity

    Sequence similaritiesi

    Belongs to the GST superfamily. Zeta family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    GeneTreeiENSGT00390000006580.
    InParanoidiQ9VHD2.
    KOiK01800.
    OMAiRAQVRMI.
    OrthoDBiEOG7TF79P.
    PhylomeDBiQ9VHD2.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR005955. Mal_ac_isom.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    TIGRFAMsiTIGR01262. maiA. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q9VHD2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSTNLCPNAS SSDIQPILYS YWRSSCSWRV RIAMNLKEIP YDIKPISLIK    50
    SGGEQHCNEY REVNPMEQVP ALQIDGHTLI ESVAIMHYLE ETRPQRPLLP 100
    QDVHKRAKVR EIVEIICSGI QPLQNLIVLI HVGEEKKKEW AQHWITRGFR 150
    AVEKALSTSA GKYCVGDEIS MADCCLVPQV FNARRFHVDL RPYPIILRID 200
    RELESNPAFR AAHPSNQPDC PPELPNK 227
    Length:227
    Mass (Da):25,975
    Last modified:May 1, 2000 - v1
    Checksum:iC708DD764F48C754
    GO
    Isoform B (identifier: Q9VHD2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MSTNLCPNASSSDIQ → MSLSAIAK

    Show »
    Length:220
    Mass (Da):25,227
    Checksum:iDABCE0A9315EA989
    GO
    Isoform C (identifier: Q9VHD2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MSTNLCPNASSSDIQ → MNH

    Show »
    Length:215
    Mass (Da):24,808
    Checksum:i86D4F06DCD77B834
    GO

    Sequence cautioni

    The sequence AAL28280.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AEV23904.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515MSTNL…SSDIQ → MSLSAIAK in isoform B. 1 PublicationVSP_010291Add
    BLAST
    Alternative sequencei1 – 1515MSTNL…SSDIQ → MNH in isoform C. 1 PublicationVSP_010292Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF54382.1.
    AE014297 Genomic DNA. Translation: AAN13429.1.
    AE014297 Genomic DNA. Translation: AAS65133.1.
    AY060732 mRNA. Translation: AAL28280.2. Different initiation.
    BT132880 mRNA. Translation: AEV23904.1. Different initiation.
    BT133289 mRNA. Translation: AFC88878.1.
    RefSeqiNP_649895.1. NM_141638.3. [Q9VHD2-1]
    NP_731358.1. NM_169286.2. [Q9VHD2-2]
    NP_996190.1. NM_206468.2. [Q9VHD2-3]
    UniGeneiDm.1121.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082042; FBpp0081520; FBgn0037697. [Q9VHD2-1]
    GeneIDi41133.
    KEGGidme:Dmel_CG9363.
    UCSCiCG9363-RA. d. melanogaster. [Q9VHD2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF54382.1 .
    AE014297 Genomic DNA. Translation: AAN13429.1 .
    AE014297 Genomic DNA. Translation: AAS65133.1 .
    AY060732 mRNA. Translation: AAL28280.2 . Different initiation.
    BT132880 mRNA. Translation: AEV23904.1 . Different initiation.
    BT133289 mRNA. Translation: AFC88878.1 .
    RefSeqi NP_649895.1. NM_141638.3. [Q9VHD2-1 ]
    NP_731358.1. NM_169286.2. [Q9VHD2-2 ]
    NP_996190.1. NM_206468.2. [Q9VHD2-3 ]
    UniGenei Dm.1121.

    3D structure databases

    ProteinModelPortali Q9VHD2.
    SMRi Q9VHD2. Positions 15-224.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66294. 1 interaction.
    DIPi DIP-24005N.
    IntActi Q9VHD2. 1 interaction.
    MINTi MINT-1563429.

    Proteomic databases

    PaxDbi Q9VHD2.
    PRIDEi Q9VHD2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082042 ; FBpp0081520 ; FBgn0037697 . [Q9VHD2-1 ]
    GeneIDi 41133.
    KEGGi dme:Dmel_CG9363.
    UCSCi CG9363-RA. d. melanogaster. [Q9VHD2-1 ]

    Organism-specific databases

    CTDi 41133.
    FlyBasei FBgn0037697. GstZ2.

    Phylogenomic databases

    eggNOGi COG0625.
    GeneTreei ENSGT00390000006580.
    InParanoidi Q9VHD2.
    KOi K01800.
    OMAi RAQVRMI.
    OrthoDBi EOG7TF79P.
    PhylomeDBi Q9VHD2.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00340 .
    Reactomei REACT_203229. Phenylalanine and tyrosine catabolism.

    Miscellaneous databases

    GenomeRNAii 41133.
    NextBioi 822335.

    Gene expression databases

    Bgeei Q9VHD2.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR005955. Mal_ac_isom.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR01262. maiA. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster."
      Saisawang C., Wongsantichon J., Ketterman A.J.
      Biochem. J. 442:181-190(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DEVELOPMENTAL STAGE.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Ovary.
    5. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
      Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).

    Entry informationi

    Entry nameiMAAI2_DROME
    AccessioniPrimary (citable) accession number: Q9VHD2
    Secondary accession number(s): H0RNF8, H8F4P9, Q8INN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3