ID A0A2I2V1M2_FELCA Unreviewed; 356 AA.
AC A0A2I2V1M2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSFCAP00000038695.1,
GN ECO:0000313|VGNC:VGNC:80836};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000038695.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000038695.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000038695.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000038695.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000038695.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000038695.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000038695.1};
RG Ensembl;
RL Submitted (SEP-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; AANG04001761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003987246.1; XM_003987197.4.
DR AlphaFoldDB; A0A2I2V1M2; -.
DR STRING; 9685.ENSFCAP00000038695; -.
DR PaxDb; 9685-ENSFCAP00000021912; -.
DR Ensembl; ENSFCAT00000044106.3; ENSFCAP00000038695.1; ENSFCAG00000032311.3.
DR GeneID; 101088085; -.
DR KEGG; fca:101088085; -.
DR CTD; 6652; -.
DR VGNC; VGNC:80836; SORD.
DR GeneTree; ENSGT00550000074781; -.
DR InParanoid; A0A2I2V1M2; -.
DR OMA; VCEMSGH; -.
DR OrthoDB; 3017546at2759; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000032311; Expressed in liver and 10 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; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR020843; PKS_ER.
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 SMART; SM00829; PKS_ER; 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:UP000011712};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 15..347
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 356 AA; 38343 MW; 7C3E05AC07B6FF77 CRC64;
MAAAKPENLS LVVHGPGDLR LENYPIPEPG PNEVLLRMHS VGICGSDVHY WQHGRIGDFI
VKKPMVLGHE ASGTVVKVGS LVKHLKPGDR VAIEPGALRE MDEFCKIGRY NLSPSIFFCA
TPPDDGNLCR FYKHNADFCY KLPDNVTFEE GALIEPLSVG IHACRRAGIT LGNKVFVCGA
GPIGLVTLIV AKAMGAAQVV VTDLSATRLS KAKEVGADFV LQISKESPKE IASKVEDLLG
CKPEVTIECS GVELSIQAGI YATRSGGTLV LVGLGSEMTT VPLVHAATRE VDIKGVFRYC
NTWPMAISML ASKSVNVKPL VTHRFPLEKA LEAFETSRKG LGLKVMLKCD PNDQNP
//
