ID G1M8V0_AILME Unreviewed; 346 AA.
AC G1M8V0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 76.
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:ENSAMEP00000015770.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000015770.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000015770.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000015770.2}
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 AlphaFoldDB; G1M8V0; -.
DR STRING; 9646.ENSAMEP00000015770; -.
DR Ensembl; ENSAMET00000016425.2; ENSAMEP00000015770.2; ENSAMEG00000014949.2.
DR eggNOG; KOG0024; Eukaryota.
DR GeneTree; ENSGT00550000074781; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR OrthoDB; 3017546at2759; -.
DR TreeFam; TF313060; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; 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:UP000008912};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 4..337
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 37217 MW; B1C41A9B1F83DDBC CRC64;
MDPSCTTTHF KENYPIPEPG PNEVLLKMHS VGICGSDVHY WQHGRIGDFV VEKPMVLGHE
ASGTVVKVGS LVKHLKAGDR VAIEPGALRE MDEFCKIGRY NLSPSIFFCA TPPDDGNLCR
FYKHNADFCY KLPDNVTFEE GALIEPLSVG IHACRRAGIT LGNKVFVCGA GPIGLVTLIV
AKAMGAAQVL VTDLSASRLS KAKEVGADII LQISKESPKE VASKVEGLLG CKPEVTIECT
GAEPAIQSGI YATRSGGTLV LVGLGSEMTT VPLVHAAVRE VDIKGVFRYC NTWPMAISML
ASKSVNVMPL VTHRFPLEKA LEAFETARKG LGLKVMLKCD PNDQNP
//
