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Database: UniProt
Entry: H9BFQ0
LinkDB: H9BFQ0
Original site: H9BFQ0 
ID   TPRL1_ERYCB             Reviewed;         272 AA.
AC   H9BFQ0;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=Tropinone reductase-like 1;
DE            EC=1.1.1.-;
OS   Erythroxylum coca (Coca plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Erythroxylaceae; Erythroxylum.
OX   NCBI_TaxID=289672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=22665766; DOI=10.1073/pnas.1200473109;
RA   Jirschitzka J., Schmidt G.W., Reichelt M., Schneider B., Gershenzon J.,
RA   D'Auria J.C.;
RT   "Plant tropane alkaloid biosynthesis evolved independently in the
RT   Solanaceae and Erythroxylaceae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:10304-10309(2012).
CC   -!- FUNCTION: Has no tropinone reductase activity.
CC       {ECO:0000269|PubMed:22665766}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; JQ015102; AFD32319.1; -; mRNA.
DR   AlphaFoldDB; H9BFQ0; -.
DR   SMR; H9BFQ0; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43180:SF91; -; 1.
DR   PANTHER; PTHR43180; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE (AFU_ORTHOLOGUE AFUA_6G11210); 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase.
FT   CHAIN           1..272
FT                   /note="Tropinone reductase-like 1"
FT                   /id="PRO_0000421861"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         17..41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   272 AA;  28328 MW;  1667D6C75DFFC9C1 CRC64;
     MTSIAGPHKR LEGKVAIITG GASGIGACTA ELFHENGAKV VIADIQDDLG QALATKLGGK
     ACYIHCDVSK EDDVINLVDT TVAKYGRLDI MFNNAGIIEG QGLPVSVVES EKSDLDRLLS
     VNLGGAFLGA KHATRVMVQQ RKGCILFTSS LCTSIAGLSG HAYAASKSGV CGLAKNLTPE
     LGKYGIRVNC ISPYGLVTGI SNISEANREL VEAMLSELGT LSGQTLRADG IAKAALFLAS
     DEAYYVSGIN MVVDGGYSVV NPRLADAIYS KL
//
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