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P50163

- TRN2_DATST

UniProt

P50163 - TRN2_DATST

Protein

Tropinone reductase 2

Gene

TR2

Organism
Datura stramonium (Jimsonweed) (Common thornapple)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the stereospecific reduction of tropinone to pseudotropine.

    Catalytic activityi

    Pseudotropine + NADP+ = tropinone + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei146 – 1461Substrate1 Publication
    Active sitei159 – 1591Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 4124NADP1 PublicationAdd
    BLAST
    Nucleotide bindingi192 – 1965NADP1 Publication

    GO - Molecular functioni

    1. tropinone reductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. tropane alkaloid biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13851.
    BRENDAi1.1.1.236. 1839.
    SABIO-RKP50163.
    UniPathwayiUPA00330.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropinone reductase 2 (EC:1.1.1.236)
    Alternative name(s):
    Tropinone reductase II
    Short name:
    TR-II
    Gene namesi
    Name:TR2
    OrganismiDatura stramonium (Jimsonweed) (Common thornapple)
    Taxonomic identifieri4076 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeDatureaeDatura

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 260260Tropinone reductase 2PRO_0000054786Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 166
    Helixi20 – 3112
    Beta strandi35 – 417
    Helixi43 – 5513
    Beta strandi59 – 646
    Helixi70 – 8314
    Turni84 – 863
    Beta strandi90 – 934
    Helixi103 – 1053
    Helixi108 – 11811
    Helixi120 – 13516
    Beta strandi137 – 1448
    Helixi147 – 1493
    Helixi157 – 17620
    Helixi178 – 1803
    Beta strandi182 – 1898
    Helixi195 – 2006
    Helixi204 – 21512
    Beta strandi217 – 2193
    Helixi225 – 23612
    Helixi238 – 2403
    Beta strandi247 – 2515
    Helixi254 – 2563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IPEX-ray2.50A/B2-260[»]
    1IPFX-ray2.50A/B2-260[»]
    2AE1X-ray2.30A1-260[»]
    2AE2X-ray1.90A/B1-260[»]
    ProteinModelPortaliP50163.
    SMRiP50163. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50163.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50163-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGRWNLEGC TALVTGGSRG IGYGIVEELA SLGASVYTCS RNQKELNDCL    50
    TQWRSKGFKV EASVCDLSSR SERQELMNTV ANHFHGKLNI LVNNAGIVIY 100
    KEAKDYTVED YSLIMSINFE AAYHLSVLAH PFLKASERGN VVFISSVSGA 150
    LAVPYEAVYG ATKGAMDQLT RCLAFEWAKD NIRVNGVGPG VIATSLVEMT 200
    IQDPEQKENL NKLIDRCALR RMGEPKELAA MVAFLCFPAA SYVTGQIIYV 250
    DGGLMANCGF 260
    Length:260
    Mass (Da):28,311
    Last modified:October 1, 1996 - v1
    Checksum:i2DBF4963B2CCA303
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20474 mRNA. Translation: AAA33282.1.
    PIRiB48674.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20474 mRNA. Translation: AAA33282.1 .
    PIRi B48674.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IPE X-ray 2.50 A/B 2-260 [» ]
    1IPF X-ray 2.50 A/B 2-260 [» ]
    2AE1 X-ray 2.30 A 1-260 [» ]
    2AE2 X-ray 1.90 A/B 1-260 [» ]
    ProteinModelPortali P50163.
    SMRi P50163. Positions 2-260.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00330 .
    BioCyci MetaCyc:MONOMER-13851.
    BRENDAi 1.1.1.236. 1839.
    SABIO-RK P50163.

    Miscellaneous databases

    EvolutionaryTracei P50163.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor."
      Nakajima K., Hashimoto T., Yamada Y.
      Proc. Natl. Acad. Sci. U.S.A. 90:9591-9595(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Root.
    2. "Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold."
      Nakajima K., Yamashita A., Akama H., Nakatsu T., Kato H., Hashimoto T., Oda J., Yamada Y.
      Proc. Natl. Acad. Sci. U.S.A. 95:4876-4881(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    3. "Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis."
      Yamashita A., Kato H., Wakatsuki S., Tomizaki T., Nakatsu T., Nakajima K., Hashimoto T., Yamada Y., Oda J.
      Biochemistry 38:7630-7637(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.

    Entry informationi

    Entry nameiTRN2_DATST
    AccessioniPrimary (citable) accession number: P50163
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

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

    External Data

    Dasty 3