SDR1_AEDAE
ID SDR1_AEDAE Reviewed; 245 AA.
AC D2WKD9; J9HZ43;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Farnesol dehydrogenase {ECO:0000305};
DE EC=1.1.1.216 {ECO:0000269|PubMed:19940247};
DE AltName: Full=NADP(+)-dependent farnesol dehydrogenase 1 {ECO:0000303|PubMed:19940247};
DE Short=AaSDR-1 {ECO:0000303|PubMed:19940247};
GN Name=SDR-1 {ECO:0000303|PubMed:19940247};
GN Synonyms=FOHSDR-1 {ECO:0000312|EMBL:ADB03639.1};
GN ORFNames=AaeL_AAEL017302 {ECO:0000312|EMBL:EJY57755.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000312|EMBL:ADB03639.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=19940247; DOI=10.1073/pnas.0909938106;
RA Mayoral J.G., Nouzova M., Navare A., Noriega F.G.;
RT "NADP+-dependent farnesol dehydrogenase, a corpora allata enzyme involved
RT in juvenile hormone synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21091-21096(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Mediates oxidation of farnesol into farnesal, a precursor of
CC juvenile hormone in the corpora allata (CA), the glands that synthesize
CC juvenile hormone. Able to oxidize C(10) to C(15) isoprenoid and
CC aliphatic alcohols. {ECO:0000269|PubMed:19940247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH;
CC Xref=Rhea:RHEA:14697, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894,
CC ChEBI:CHEBI:16619, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.216; Evidence={ECO:0000269|PubMed:19940247};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=91 uM for (E,E) farnesol {ECO:0000269|PubMed:19940247};
CC KM=97 uM for (Z,Z) farnesol {ECO:0000269|PubMed:19940247};
CC KM=184 uM for 2-decanol {ECO:0000269|PubMed:19940247};
CC KM=208 uM for geraniol (E) {ECO:0000269|PubMed:19940247};
CC KM=109 uM for nerol (Z) {ECO:0000269|PubMed:19940247};
CC KM=133 uM for citronellol {ECO:0000269|PubMed:19940247};
CC KM=195 uM for octanol {ECO:0000269|PubMed:19940247};
CC pH dependence:
CC Optimum pH is 10-11. {ECO:0000269|PubMed:19940247};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19940247}.
CC -!- TISSUE SPECIFICITY: Highly expressed level in the midgut and brain in
CC adult females, and at lower level in the abdominal and thoracic
CC ganglia. High levels are detected in corpora allata (CA), Malpighian
CC tubules and fat body. {ECO:0000269|PubMed:19940247}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; GQ344797; ADB03639.1; -; mRNA.
DR EMBL; CH477512; EJY57755.1; -; Genomic_DNA.
DR RefSeq; XP_011492954.1; XM_011494652.1.
DR AlphaFoldDB; D2WKD9; -.
DR SMR; D2WKD9; -.
DR STRING; 7159.AAEL017302-PA; -.
DR GeneID; 23687722; -.
DR KEGG; aag:23687722; -.
DR VEuPathDB; VectorBase:AAEL017302; -.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_10_1; -.
DR OrthoDB; 1190834at2759; -.
DR PhylomeDB; D2WKD9; -.
DR BioCyc; MetaCyc:MON-15957; -.
DR BRENDA; 1.1.1.216; 149.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0047886; F:farnesol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006718; P:juvenile hormone 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 NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..245
FT /note="Farnesol dehydrogenase"
FT /id="PRO_0000432713"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00334,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT CONFLICT 80
FT /note="K -> E (in Ref. 1; ADB03639)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="A -> S (in Ref. 1; ADB03639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 26542 MW; A60728772A02C335 CRC64;
MDRWAGKVAV VTGASSGIGA AITTDLAKAG MVVVGLARRV ERVEALKANL PESAKPRLHA
VKCDVSKEED ITQVFKWVEK KFGGVDVLVN NAGILRQTDL LGTDNGQMLR EVLDTNVMGL
VLCSQKAYQS MKKRSVDGHI VHINSVVGHK VFDFPQSNIY PASKHAVTAI TETMRNELRN
AGSRIKVTSI SPGVVRTEIL PESIIEGGHA LLESEDISEA VLYVLGTPPR VQVHELTIKP
VGEKF
