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P50163

- TRN2_DATST

UniProt

P50163 - TRN2_DATST

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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

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
Complete GO annotation...

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 – 166Combined sources
Helixi20 – 3112Combined sources
Beta strandi35 – 417Combined sources
Helixi43 – 5513Combined sources
Beta strandi59 – 646Combined sources
Helixi70 – 8314Combined sources
Turni84 – 863Combined sources
Beta strandi90 – 934Combined sources
Helixi103 – 1053Combined sources
Helixi108 – 11811Combined sources
Helixi120 – 13516Combined sources
Beta strandi137 – 1448Combined sources
Helixi147 – 1493Combined sources
Helixi157 – 17620Combined sources
Helixi178 – 1803Combined sources
Beta strandi182 – 1898Combined sources
Helixi195 – 2006Combined sources
Helixi204 – 21512Combined sources
Beta strandi217 – 2193Combined sources
Helixi225 – 23612Combined sources
Helixi238 – 2403Combined sources
Beta strandi247 – 2515Combined sources
Helixi254 – 2563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAGRWNLEGC TALVTGGSRG IGYGIVEELA SLGASVYTCS RNQKELNDCL
60 70 80 90 100
TQWRSKGFKV EASVCDLSSR SERQELMNTV ANHFHGKLNI LVNNAGIVIY
110 120 130 140 150
KEAKDYTVED YSLIMSINFE AAYHLSVLAH PFLKASERGN VVFISSVSGA
160 170 180 190 200
LAVPYEAVYG ATKGAMDQLT RCLAFEWAKD NIRVNGVGPG VIATSLVEMT
210 220 230 240 250
IQDPEQKENL NKLIDRCALR RMGEPKELAA MVAFLCFPAA SYVTGQIIYV
260
DGGLMANCGF
Length:260
Mass (Da):28,311
Last modified:October 1, 1996 - v1
Checksum:i2DBF4963B2CCA303
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20474 mRNA. Translation: AAA33282.1.
PIRiB48674.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20474 mRNA. Translation: AAA33282.1 .
PIRi B48674.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 29, 2014
This is version 81 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