DHSO_BOVIN
ID DHSO_BOVIN Reviewed; 356 AA.
AC Q58D31; Q0II66;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000303|PubMed:9143345};
DE Short=SDH {ECO:0000303|PubMed:9143345};
DE EC=1.1.1.- {ECO:0000269|PubMed:9143345};
DE AltName: Full=L-iditol 2-dehydrogenase {ECO:0000305|PubMed:9143345};
DE EC=1.1.1.14 {ECO:0000269|PubMed:9143345};
DE AltName: Full=Polyol dehydrogenase {ECO:0000305};
DE AltName: Full=Xylitol dehydrogenase {ECO:0000305|PubMed:9143345};
DE Short=XDH;
DE EC=1.1.1.9 {ECO:0000269|PubMed:9143345};
GN Name=SORD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=9143345; DOI=10.1006/abbi.1997.9882;
RA Marini I., Bucchioni L., Borella P., Del Corso A., Mura U.;
RT "Sorbitol dehydrogenase from bovine lens: purification and properties.";
RL Arch. Biochem. Biophys. 340:383-391(1997).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-
CC dependent oxidation of various sugar alcohols. Is mostly active with
CC xylitol, D-sorbitol (D-glucitol) and L-iditol as substrates, leading to
CC the C2-oxidized products D-xylulose, D-fructose and L-sorbose,
CC respectively (PubMed:9143345). Is a key enzyme in the polyol pathway
CC that interconverts glucose and fructose via sorbitol, which constitutes
CC an 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). Cannot use NADP(+) as the electron
CC acceptor. Has no activity on ethanol, methanol, glycerol, galactitol
CC and fructose 6-phosphate (PubMed:9143345).
CC {ECO:0000250|UniProtKB:Q00796, ECO:0000269|PubMed:9143345}.
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:0000269|PubMed:9143345};
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:0000269|PubMed:9143345};
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:0000269|PubMed:9143345};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:9143345};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9143345};
CC -!- ACTIVITY REGULATION: Inhibited in vitro by metal chelators such as EDTA
CC and 1,10-phenanthroline. {ECO:0000269|PubMed:9143345}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 mM for D-sorbitol (at pH 8.0) {ECO:0000269|PubMed:9143345};
CC KM=3.2 mM for xylitol (at pH 8.0) {ECO:0000269|PubMed:9143345};
CC KM=20 mM for L-iditol (at pH 8.0) {ECO:0000269|PubMed:9143345};
CC KM=67 mM for ribitol (at pH 8.0) {ECO:0000269|PubMed:9143345};
CC KM=381 mM for D-mannitol (at pH 8.0) {ECO:0000269|PubMed:9143345};
CC KM=268 mM for L-threitol (at pH 8.0) {ECO:0000269|PubMed:9143345};
CC KM=180 mM for D-fructose (at pH 7.4) {ECO:0000269|PubMed:9143345};
CC KM=670 mM for L-sorbose (at pH 7.4) {ECO:0000269|PubMed:9143345};
CC KM=260 mM for D-ribulose (at pH 7.4) {ECO:0000269|PubMed:9143345};
CC KM=0.052 mM for NADH (at pH 7.4) {ECO:0000269|PubMed:9143345};
CC KM=0.089 mM for NAD(+) (at pH 8.0) {ECO:0000269|PubMed:9143345};
CC Note=kcat is 29 sec(-1) for D-sorbitol oxidation (at pH 8.0). kcat is
CC 26 sec(-1) for xylitol oxidation (at pH 8.0). kcat is 21 sec(-1) for
CC L-iditol oxidation (at pH 8.0). kcat is 22 sec(-1) for ribitol
CC oxidation (at pH 8.0). kcat is 24 sec(-1) for D-mannitol oxidation
CC (at pH 8.0). kcat is 12 sec(-1) for L-threitol oxidation (at pH 8.0).
CC kcat is 162 sec(-1) for D-fructose reduction (at pH 7.4). kcat is 153
CC sec(-1) for L-sorbose reduction (at pH 7.4). kcat is 198 sec(-1) for
CC D-ribulose reduction (at pH 7.4). {ECO:0000269|PubMed:9143345};
CC pH dependence:
CC Optimum pH is about 9 for D-sorbitol oxidation, and 7.4 for D-
CC fructose reduction. {ECO:0000269|PubMed:9143345};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9143345}.
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 -!- TISSUE SPECIFICITY: Expressed in lens. {ECO:0000269|PubMed:9143345}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; BT021766; AAX46613.1; -; mRNA.
DR EMBL; BC122783; AAI22784.2; -; mRNA.
DR RefSeq; NP_001032397.1; NM_001037320.1.
DR AlphaFoldDB; Q58D31; -.
DR SMR; Q58D31; -.
DR STRING; 9913.ENSBTAP00000035716; -.
DR PaxDb; Q58D31; -.
DR PeptideAtlas; Q58D31; -.
DR PRIDE; Q58D31; -.
DR Ensembl; ENSBTAT00000035849; ENSBTAP00000035716; ENSBTAG00000025496.
DR GeneID; 508954; -.
DR KEGG; bta:508954; -.
DR CTD; 6652; -.
DR VEuPathDB; HostDB:ENSBTAG00000025496; -.
DR VGNC; VGNC:35131; SORD.
DR eggNOG; KOG0024; Eukaryota.
DR GeneTree; ENSGT00550000074781; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; Q58D31; -.
DR OMA; ETWYAMS; -.
DR OrthoDB; 1019156at2759; -.
DR TreeFam; TF313060; -.
DR SABIO-RK; Q58D31; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000025496; Expressed in liver and 105 other tissues.
DR ExpressionAtlas; Q58D31; baseline and differential.
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 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 1: Evidence at protein level;
KW Cell projection; Cilium; Flagellum; Membrane; Metal-binding; Mitochondrion;
KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..356
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000239652"
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 BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 272..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 296..298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
SQ SEQUENCE 356 AA; 38099 MW; F7E3ACD6712E71B1 CRC64;
MAAAKPENLS LVVHGPGDLR LENYPIPEPG PNEVLLKMHS VGICGSDVHY WQHGRIGDFV
VKKPMVLGHE ASGTVVKVGS LVRHLQPGDR VAIEPGAPRE TDEFCKIGRY NLSPTIFFCA
TPPDDGNLCR FYKHNANFCY KLPDNVTFEE GALIEPLSVG IHACRRAGVT LGNKVLVCGA
GPIGLVSLLA AKAMGAAQVV VTDLSASRLS KAKEVGADFI LQISNESPQE IAKKVEGLLG
SKPEVTIECT GVETSIQAGI YATHSGGTLV LVGLGSEMTS VPLVHAATRE VDIKGVFRYC
NTWPMAISML ASKSVNVKPL VTHRFPLEKA LEAFETSKKG LGLKVMIKCD PNDQNP
