BDH2_SALOF
ID BDH2_SALOF Reviewed; 283 AA.
AC A0A8F5XX49;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=(+)-borneol dehydrogenase 2 {ECO:0000303|PubMed:31927319};
DE Short=SoBDH2 {ECO:0000303|PubMed:31927319};
DE EC=1.1.1.198 {ECO:0000269|PubMed:31927319};
GN Name=BDH2 {ECO:0000303|PubMed:31927319};
OS Salvia officinalis (Sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=38868;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31927319; DOI=10.1016/j.phytochem.2019.112227;
RA Drienovska I., Kolanovic D., Chanique A., Sieber V., Hofer M., Kourist R.;
RT "Molecular cloning and functional characterization of a two highly
RT stereoselective borneol dehydrogenases from Salvia officinalis L.";
RL Phytochemistry 172:112227-112227(2020).
CC -!- FUNCTION: Involved in the biosynthesis of monoterpene natural products
CC related to camphor (PubMed:31927319). Catalayzes the oxidation of (+)-
CC borneol to (+)-camphor (PubMed:31927319). Shows absolute selectivity
CC towards (+)-borneol (PubMed:31927319). Catalyzes the oxidation of (+)-
CC isoborneol to (-)-camphor (PubMed:31927319). Shows absolute selectivity
CC towards (+)-isoborneol (PubMed:31927319).
CC {ECO:0000269|PubMed:31927319}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,2S,4R)-borneol + NAD(+) = (1R,4R)-camphor + H(+) + NADH;
CC Xref=Rhea:RHEA:17329, ChEBI:CHEBI:15378, ChEBI:CHEBI:15393,
CC ChEBI:CHEBI:15396, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.198; Evidence={ECO:0000269|PubMed:31927319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17330;
CC Evidence={ECO:0000269|PubMed:31927319};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48 uM for NAD(+) {ECO:0000269|PubMed:31927319};
CC KM=160 uM for (1R,2S,4R)-borneol {ECO:0000269|PubMed:31927319};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; MT525099; QXO33291.1; -; mRNA.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05326; secoisolariciresinol-DH_like_SDR_c; 1.
DR InterPro; IPR045309; ABA2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..283
FT /note="(+)-borneol dehydrogenase 2"
FT /id="PRO_0000456337"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 174
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19337"
FT BINDING 27..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:31927319"
FT BINDING 51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 76..77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 103..105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
SQ SEQUENCE 283 AA; 30063 MW; 24A839D37D51D1BB CRC64;
MATGAANVES PQSLPLRLLG RVALVTGGSS GIGESIVLLF RKHGAKVCIA DVQDNQGQRL
CETLGGSSDI AFCHCDVTIE DDVKRAVDFT VDKFGTLDIM VNNAGVSGPP CPDIRDFELS
AFDRVFDINV RGVFIGMKHA ARIMIPAKKG SIISISSVAS TMGGLGPHAY TGSKHAVLGL
TKNVAAELGK HGIRVNCVSP YAVATSLALA HLPEAERTED TWDDFRRFVA DNANLQGVEL
TMEDVANAVV FLASDEARYV SGMNLMVDGG FTSTNHALQV FRP
