DHSO_BOMMO
ID DHSO_BOMMO Reviewed; 348 AA.
AC Q02912;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sorbitol dehydrogenase;
DE Short=SDH;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P07846};
DE AltName: Full=L-iditol 2-dehydrogenase;
DE EC=1.1.1.14 {ECO:0000250|UniProtKB:P07846};
DE AltName: Full=Polyol dehydrogenase {ECO:0000305};
DE AltName: Full=Xylitol dehydrogenase;
DE Short=XDH;
DE EC=1.1.1.9 {ECO:0000250|UniProtKB:P07846};
GN Name=SDH;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8504807; DOI=10.1111/j.1432-1033.1993.tb17862.x;
RA Niimi T., Yamashita O., Yaginuma T.;
RT "A cold-inducible Bombyx gene encoding a protein similar to mammalian
RT sorbitol dehydrogenase. Yolk nuclei-dependent gene expression in diapause
RT eggs.";
RL Eur. J. Biochem. 213:1125-1131(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tokai X Asahi; TISSUE=Fat body;
RX PubMed=8933178; DOI=10.1111/j.1365-2583.1996.tb00101.x;
RA Niimi T., Yamashita O., Yaginuma T.;
RT "Structure of the Bombyx sorbitol dehydrogenase gene: a possible
RT alternative use of the promoter.";
RL Insect Mol. Biol. 5:269-280(1996).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-
CC dependent oxidation of various sugar alcohols. Is active with xylitol,
CC L-iditol and D-sorbitol (D-glucitol) as substrates, leading to the C2-
CC oxidized products D-xylulose, L-sorbose and D-fructose, respectively
CC (By similarity). Is a key enzyme in the polyol pathway that
CC interconverts glucose and fructose via sorbitol, which constitutes an
CC important alternate route for glucose metabolism (By similarity).
CC {ECO:0000250|UniProtKB:P07846, ECO:0000250|UniProtKB:Q00796}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH;
CC Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P07846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-iditol + NAD(+) = H(+) + keto-L-sorbose + NADH;
CC Xref=Rhea:RHEA:10160, ChEBI:CHEBI:13172, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18202, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.14;
CC Evidence={ECO:0000250|UniProtKB:P07846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+);
CC Xref=Rhea:RHEA:33031, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:48095, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P07846};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INDUCTION: By cold.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; D13371; BAA02634.1; -; mRNA.
DR EMBL; D66906; BAA11030.1; -; Genomic_DNA.
DR PIR; S32484; S32484.
DR RefSeq; NP_001037311.1; NM_001043846.1.
DR AlphaFoldDB; Q02912; -.
DR SMR; Q02912; -.
DR GeneID; 101738079; -.
DR InParanoid; Q02912; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05285; sorbitol_DH; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Stress response;
KW Zinc.
FT CHAIN 1..348
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000160820"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
SQ SEQUENCE 348 AA; 37158 MW; 2985304E9ADE6FF0 CRC64;
MTENYAAVLH GANDVRIEKI PVPEINDDEV LIKIDCVGIC GSDVKLYSTG TCGADVIDKP
IVIGHEGAGT VVKVGDKVSS LRVGDRVAIE PTQPCRSCEL CKRGKYNLCV EPRYCSSMGA
PGNLCRYYKH VADFCHKLPD NLTMEEGAAV QPLAIVIHAC NRAKITLGSK IVILGAGPIG
ILCAMSAKAM GASKIILTDV VQSRLDAALE LGADNVLLVR REYTDEEVVE KIVKLLGDRP
DVSIDACGYG SAQRVALLVT KTAGLVLVVG IADKTVELPL SQALLREVDV VGSFRIMNTY
QPALAAVSSG AIPLDKFITH RFPLNKTKEA LDLAKSGAAM KILIHVQN
