ID A0A0D9RBA9_CHLSB Unreviewed; 319 AA.
AC A0A0D9RBA9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000256|ARBA:ARBA00026132, ECO:0000256|RuleBase:RU369026};
DE Short=SDH {ECO:0000256|RuleBase:RU369026};
DE Short=XDH {ECO:0000256|RuleBase:RU369026};
DE EC=1.1.1.14 {ECO:0000256|ARBA:ARBA00026109, ECO:0000256|RuleBase:RU369026};
DE EC=1.1.1.9 {ECO:0000256|ARBA:ARBA00026119, ECO:0000256|RuleBase:RU369026};
DE AltName: Full=L-iditol 2-dehydrogenase {ECO:0000256|ARBA:ARBA00030853, ECO:0000256|RuleBase:RU369026};
DE AltName: Full=Polyol dehydrogenase {ECO:0000256|ARBA:ARBA00032485, ECO:0000256|RuleBase:RU369026};
DE AltName: Full=Xylitol dehydrogenase {ECO:0000256|ARBA:ARBA00031806, ECO:0000256|RuleBase:RU369026};
GN Name=SORD {ECO:0000313|Ensembl:ENSCSAP00000005898.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005898.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005898.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005898.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-
CC dependent oxidation of various sugar alcohols. Is active with D-
CC sorbitol (D-glucitol) leading to the C2-oxidized product D-fructose. Is
CC a key enzyme in the polyol pathway that interconverts glucose and
CC fructose via sorbitol, which constitutes an important alternate route
CC for glucose metabolism. May play a role in sperm motility by using
CC sorbitol as an alternative energy source for sperm motility.
CC {ECO:0000256|RuleBase:RU369026}.
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:0000256|RuleBase:RU369026};
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:0000256|ARBA:ARBA00024563,
CC ECO:0000256|RuleBase:RU369026};
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:0000256|ARBA:ARBA00024582,
CC ECO:0000256|RuleBase:RU369026};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU369026};
CC Note=Binds 1 or 2 Zn(2+) ions per subunit.
CC {ECO:0000256|RuleBase:RU369026};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU369026}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000256|ARBA:ARBA00004230, ECO:0000256|RuleBase:RU369026}.
CC Mitochondrion membrane {ECO:0000256|RuleBase:RU369026}; Peripheral
CC membrane protein {ECO:0000256|RuleBase:RU369026}. Note=Associated with
CC mitochondria of the midpiece and near the plasma membrane in the
CC principal piece of the flagellum. Also found in the epididymosome,
CC secreted by the epididymal epithelium and that transfers proteins from
CC the epididymal fluid to the sperm surface.
CC {ECO:0000256|RuleBase:RU369026}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AQIB01116115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9RBA9; -.
DR STRING; 60711.ENSCSAP00000005898; -.
DR Ensembl; ENSCSAT00000007729.1; ENSCSAP00000005898.1; ENSCSAG00000009647.1.
DR eggNOG; KOG0024; Eukaryota.
DR GeneTree; ENSGT00550000074781; -.
DR OMA; VCEMSGH; -.
DR Proteomes; UP000029965; Chromosome 26.
DR Bgee; ENSCSAG00000009647; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0047833; F:D-sorbitol dehydrogenase (acceptor) activity; IEA:Ensembl.
DR GO; GO:0046526; F:D-xylulose reductase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0046370; P:fructose biosynthetic process; IEA:Ensembl.
DR GO; GO:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; IEA:Ensembl.
DR GO; GO:0051160; P:L-xylitol catabolic process; IEA:Ensembl.
DR GO; GO:0006062; P:sorbitol catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05285; sorbitol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR045306; SDH-like.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU369026};
KW Cell projection {ECO:0000256|ARBA:ARBA00023069};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Flagellum {ECO:0000256|ARBA:ARBA00022846};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277}; NAD {ECO:0000256|RuleBase:RU369026};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU369026};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 1..105
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 145..274
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 319 AA; 34163 MW; 2486A7591A987936 CRC64;
MHSVGICGSD VHYWEEGRIG NFIVKKPMVL GHEASGTVEK VGSLVKHLKP GDRVAIEPGV
PRENDEFCKS GRYNLSPSIF FCATPPDDGN LCRFYKHNAA FCYKLPDNVT YEEGALIEPL
SVGIHACRRG GVTLGHRVLV CGAGPIGVVS LLVAKAMGAA QVVVTDLSAP RLSKAKEIGA
DLVLQISKES PQEIAGKVEG LLGCKPEVTI ECTGAEASIQ AGIYATRSGG TLVLVGLGSE
MTTIPLLHAA VREVDIKGVF RYCNTWPVAI SMLASKSVNI KPLVTHRFPL EKALEAFETF
KKGLGLKIML KCDPNDQNP
//
