DHSO_PIG
ID DHSO_PIG Reviewed; 97 AA.
AC Q29318;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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};
DE Flags: Fragment;
GN Name=SORD;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|EMBL:CAA23205.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine {ECO:0000312|EMBL:CAA23205.1};
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(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. May play a role in
CC sperm motility by using sorbitol as an alternative energy source for
CC sperm motility (By similarity). {ECO:0000250|UniProtKB:P07846,
CC 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;
CC Evidence={ECO:0000250|UniProtKB:P07846};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P07846};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P07846}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q64442}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q64442}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q64442}. Note=Associated with mitochondria of
CC the midpiece and near the plasma membrane in the principal piece of the
CC flagellum. Also found in the epididymosome, secreted by the epididymal
CC epithelium and that transfers proteins from the epididymal fluid to the
CC sperm surface. {ECO:0000250|UniProtKB:Q64442}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; F14714; CAA23205.1; -; mRNA.
DR STRING; 9823.ENSSSCP00000005040; -.
DR PaxDb; Q29318; -.
DR PeptideAtlas; Q29318; -.
DR eggNOG; KOG0024; Eukaryota.
DR InParanoid; Q29318; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0006062; P:sorbitol catabolic process; IBA:GO_Central.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR Pfam; PF08240; ADH_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Flagellum; Membrane; Metal-binding; Mitochondrion;
KW NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..>97
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000160818"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT NON_TER 97
SQ SEQUENCE 97 AA; 10327 MW; B681170DD30868CB CRC64;
MAAAKPENLS LVVHGPGDLR LENYPIPEPG PNXVLLKMHS VGICGSDVHY WQHGRIGNFV
VKKPMVLGHE ASGTXVKVGS LVTHLKPGDR XAXEPGA
