BDH_LAVIN
ID BDH_LAVIN Reviewed; 259 AA.
AC K4N0V2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Borneol dehydrogenase, mitochondrial {ECO:0000303|PubMed:23058847};
DE Short=LiBDH {ECO:0000303|PubMed:23058847};
DE EC=1.1.1.- {ECO:0000269|PubMed:23058847};
DE Flags: Precursor;
GN Name=BDH {ECO:0000303|PubMed:23058847};
OS Lavandula x intermedia (Lavandin) (Lavandula angustifolia x Lavandula
OS latifolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Lavandulinae;
OC Lavandula.
OX NCBI_TaxID=1196215;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Trichome gland;
RX PubMed=23058847; DOI=10.1016/j.abb.2012.09.013;
RA Sarker L.S., Galata M., Demissie Z.A., Mahmoud S.S.;
RT "Molecular cloning and functional characterization of borneol dehydrogenase
RT from the glandular trichomes of Lavandula x intermedia.";
RL Arch. Biochem. Biophys. 528:163-170(2012).
CC -!- FUNCTION: Involved in the biosynthesis of monoterpenes natural products
CC related to camphor (PubMed:23058847). Catalyzes the conversion of
CC borneol into camphor (PubMed:23058847). {ECO:0000269|PubMed:23058847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=borneol + NAD(+) = camphor + H(+) + NADH;
CC Xref=Rhea:RHEA:68828, ChEBI:CHEBI:15378, ChEBI:CHEBI:28093,
CC ChEBI:CHEBI:36773, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:23058847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68829;
CC Evidence={ECO:0000269|PubMed:23058847};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53.6 uM for borneol {ECO:0000269|PubMed:23058847};
CC Note=kcat is 4x10(-4) sec(-1) with borneol as substrate.
CC {ECO:0000269|PubMed:23058847};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:23058847};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius.
CC {ECO:0000269|PubMed:23058847};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:23058847}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in glandular trichomes of
CC mature flowers. {ECO:0000269|PubMed:23058847}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; JX972167; AFV30207.1; -; mRNA.
DR SMR; K4N0V2; -.
DR BRENDA; 1.1.1.198; 12981.
DR UniPathway; UPA00213; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Mitochondrion; NAD; Oxidoreductase; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..259
FT /note="Borneol dehydrogenase, mitochondrial"
FT /id="PRO_0000455264"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 161
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19337"
FT BINDING 21..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 63..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 90..92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
FT BINDING 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:I6Y778"
SQ SEQUENCE 259 AA; 27270 MW; A7FC947AAD844714 CRC64;
MASTVLRRLE GKVALITGAA SGIGESAARL FSRHGAKVVI ADIQDELALN ICKDLGSTFV
HCDVTKEFDV ETAVNTAVST YGKLDIMLNN AGISGAPKYK ISNTQLSDFK RVVDVNLVGV
FLGTKHAARV MIPNRSGSII STASAATAAA AGTPYPYICS KHGVVGLTRN AAVEMGGHGI
RVNCVSPYYV ATPMTRDDDW IQGCFSNLKG AVLTAEDVAE AALYLASDES KYVSGHNLLV
DGGVSIMNQG CNMFDLMDS
