ID   IDLDH_IPSPI             Reviewed;         253 AA.
AC   G5DGA8;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Ipsdienol dehydrogenase {ECO:0000303|PubMed:22101251};
DE            EC=1.1.1.386 {ECO:0000269|PubMed:22101251};
GN   Name=IDOLDH {ECO:0000303|PubMed:22101251};
OS   Ips pini (Pine engraver beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Ips.
OX   NCBI_TaxID=102803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=22101251; DOI=10.1016/j.ibmb.2011.10.009;
RA   Figueroa-Teran R., Welch W.H., Blomquist G.J., Tittiger C.;
RT   "Ipsdienol dehydrogenase (IDOLDH): a novel oxidoreductase important for Ips
RT   pini pheromone production.";
RL   Insect Biochem. Mol. Biol. 42:81-90(2012).
CC   -!- FUNCTION: Catalyzes the oxidation of racemic ipsdienol and (4R)-(-)-
CC       ipsdienol to form ipsdienone (2-methyl-6-methylene-2,7-octadien-4-one),
CC       an intermediate in the biosynthesis of pheromonal ipsdienol in male
CC       pine engraver beetles. In contrast, (4S)-(+)-ipsdienol is not a
CC       substrate. {ECO:0000269|PubMed:22101251}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4R)-ipsdienol + NADP(+) = H(+) + ipsdienone + NADPH;
CC         Xref=Rhea:RHEA:45116, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:84966, ChEBI:CHEBI:84970;
CC         EC=1.1.1.386; Evidence={ECO:0000269|PubMed:22101251};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4R)-ipsdienol + NAD(+) = H(+) + ipsdienone + NADH;
CC         Xref=Rhea:RHEA:45120, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:84966, ChEBI:CHEBI:84970;
CC         EC=1.1.1.386; Evidence={ECO:0000269|PubMed:22101251};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=17.2 nmol/min/mg enzyme {ECO:0000269|PubMed:22101251};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22101251}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in male midguts. Expressed
CC       at higher level in the anterior midgut of fed males.
CC       {ECO:0000269|PubMed:22101251}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; JN653323; AEQ59233.1; -; mRNA.
DR   AlphaFoldDB; G5DGA8; -.
DR   SMR; G5DGA8; -.
DR   KEGG; ag:AEQ59233; -.
DR   BioCyc; MetaCyc:MON-18350; -.
DR   BRENDA; 1.1.1.386; 7894.
DR   SABIO-RK; G5DGA8; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..253
FT                   /note="Ipsdienol dehydrogenase"
FT                   /id="PRO_0000433622"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00334"
FT   BINDING         63
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00334"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00334"
FT   BINDING         166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00334"
SQ   SEQUENCE   253 AA;  27514 MW;  5BB55F79ACBD91E2 CRC64;
     MMVKIQDSVY LVTGGGSGLG EATAKLLLTE GARVTIFSRN EYKNEFPHDQ VLSVKGDVRS
     ESDVKRALEA TIQKFGKLDG VMHCAGVFQN GDELFNMDTQ QPGDYTVLTD IVTTNLLGTF
     NVNRLAIPYF LTNQPDEEGQ KGIIINCSST SGHSPMSSAV AYSTSKAAII GLSYALAKQL
     STLGIRVMDI APALCDTPMF RRAVGFNQDI ANFRNLFPAR LIQPIEYANA VKHIIETPML
     NGSSYQLDGA LRP