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Q93113

- GST1D_ANOGA

UniProt

Q93113 - GST1D_ANOGA

Protein

Glutathione S-transferase 1, isoform D

Gene

GstD1

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity.2 Publications

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.1 Publication
    1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride.1 Publication

    Enzyme regulationi

    Inhibited by S-hexylglutathione.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Glutathione

    GO - Molecular functioni

    1. DDT-dehydrochlorinase activity Source: UniProtKB-EC
    2. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Lyase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase 1, isoform D (EC:2.5.1.18, EC:4.5.1.1)
    Alternative name(s):
    AgGst1-alpha
    Aggst1-1
    Aggst1-6
    Aggst2-1
    DDT-dehydrochlorinase
    GST class-theta
    Gene namesi
    Name:GstD1
    Synonyms:GST1a
    ORF Names:AGAP004164
    OrganismiAnopheles gambiae (African malaria mosquito)
    Taxonomic identifieri7165 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
    ProteomesiUP000007062: Chromosome 2R

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 209209Glutathione S-transferase 1, isoform DPRO_0000185962Add
    BLAST

    Expressioni

    Developmental stagei

    Expressed in larvae.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    209
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Helixi10 – 2112
    Beta strandi27 – 304
    Helixi33 – 353
    Helixi37 – 393
    Helixi41 – 466
    Beta strandi52 – 576
    Beta strandi60 – 645
    Helixi65 – 7612
    Helixi87 – 10216
    Helixi104 – 11815
    Helixi124 – 14017
    Turni141 – 1433
    Beta strandi149 – 1513
    Helixi154 – 16916
    Helixi177 – 18913
    Helixi193 – 20715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PN9X-ray2.00A/B1-209[»]
    ProteinModelPortaliQ93113.
    SMRiQ93113. Positions 1-209.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93113.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8080GST N-terminalAdd
    BLAST
    Domaini86 – 207122GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 523Glutathione binding
    Regioni64 – 663Glutathione binding

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000125741.
    KOiK00799.
    OMAiAMNESID.

    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.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform D (identifier: Q93113-1) [UniParc]FASTAAdd to Basket

    Also known as: 1-1, 1-6, 2-1

    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

    MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH    50
    CIPTLVDNGF ALWESRAIQI YLAEKYGKDD KLYPKDPQKR AVVNQRLYFD 100
    MGTLYQRFAD YHYPQIFAKQ PANPENEKKM KDAVGFLNTF LEGQEYAAGN 150
    DLTIADLSLA ATIATYEVAG FDFAPYPNVA AWFARCKANA PGYALNQAGA 200
    DEFKAKFLS 209
    Length:209
    Mass (Da):23,445
    Last modified:February 1, 1997 - v1
    Checksum:i3B262EEE21FAA9D0
    GO
    Isoform A (identifier: O77462-1) [UniParc]FASTAAdd to Basket

    Also known as: 1-3

    The sequence of this isoform can be found in the external entry O77462.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:186
    Mass (Da):21,255
    GO
    Isoform B (identifier: O77473-1) [UniParc]FASTAAdd to Basket

    Also known as: 1-4

    The sequence of this isoform can be found in the external entry O77473.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:216
    Mass (Da):24,492
    GO
    Isoform C (identifier: Q93112-1) [UniParc]FASTAAdd to Basket

    Also known as: 1-5

    The sequence of this isoform can be found in the external entry Q93112.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:209
    Mass (Da):23,783
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241V → A in CAA96105. (PubMed:9038148)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z71481 mRNA. Translation: CAA96105.1.
    Z81292 mRNA. Translation: CAB03593.1.
    AF071160 Genomic DNA. Translation: AAC79995.1.
    AAAB01008880 Genomic DNA. Translation: EAA44713.3.
    RefSeqiXP_313050.3. XM_313050.4.

    Genome annotation databases

    EnsemblMetazoaiAGAP004164-RB; AGAP004164-PB; AGAP004164. [Q93113-1]
    GeneIDi1273988.
    KEGGiaga:AgaP_AGAP004164.
    VectorBaseiAGAP004163. Anopheles gambiae.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z71481 mRNA. Translation: CAA96105.1 .
    Z81292 mRNA. Translation: CAB03593.1 .
    AF071160 Genomic DNA. Translation: AAC79995.1 .
    AAAB01008880 Genomic DNA. Translation: EAA44713.3 .
    RefSeqi XP_313050.3. XM_313050.4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PN9 X-ray 2.00 A/B 1-209 [» ]
    ProteinModelPortali Q93113.
    SMRi Q93113. Positions 1-209.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai AGAP004164-RB ; AGAP004164-PB ; AGAP004164 . [Q93113-1 ]
    GeneIDi 1273988.
    KEGGi aga:AgaP_AGAP004164.
    VectorBasei AGAP004163. Anopheles gambiae.

    Organism-specific databases

    CTDi 1273988.

    Phylogenomic databases

    HOGENOMi HOG000125741.
    KOi K00799.
    OMAi AMNESID.

    Miscellaneous databases

    EvolutionaryTracei Q93113.

    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.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and localization of a glutathione S-transferase class I gene from Anopheles gambiae."
      Ranson H., Cornel A.J., Fournier D., Vaughan A., Collins F.H., Hemingway J.
      J. Biol. Chem. 272:5464-5468(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
      Strain: G3 and Zands.
      Tissue: Larva.
    2. "The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family."
      Ranson H., Collins F.H., Hemingway J.
      Proc. Natl. Acad. Sci. U.S.A. 95:14284-14289(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
      Strain: ZAN/U.
    3. "The genome sequence of the malaria mosquito Anopheles gambiae."
      Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F.
      , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
      Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PEST.
    4. "Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae."
      Ranson H., Prapanthadara L., Hemingway J.
      Biochem. J. 324:97-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
      Strain: Zands.
    5. "Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae."
      Chen L., Hall P.R., Zhou X.E., Ranson H., Hemingway J., Meehan E.J.
      Acta Crystallogr. D 59:2211-2217(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH S-HEXYLGLUTATHIONE INHIBITOR, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiGST1D_ANOGA
    AccessioniPrimary (citable) accession number: Q93113
    Secondary accession number(s): Q7PH24, Q94998
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3