DHSO1_YEAST
ID DHSO1_YEAST Reviewed; 357 AA.
AC P35497; D6VWX7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Sorbitol dehydrogenase 1 {ECO:0000305|PubMed:8125328};
DE Short=SDH 1;
DE EC=1.1.1.- {ECO:0000269|PubMed:8125328};
DE AltName: Full=Polyol dehydrogenase {ECO:0000305};
DE AltName: Full=Xylitol dehydrogenase;
DE EC=1.1.1.9 {ECO:0000269|PubMed:8125328};
GN Name=SOR1; Synonyms=SDH1 {ECO:0000303|PubMed:8125328};
GN OrderedLocusNames=YJR159W; ORFNames=J2395;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND INDUCTION BY SORBITOL.
RX PubMed=8125328; DOI=10.1016/0378-1119(94)90741-2;
RA Sarthy A.V., Schopp C., Idler K.B.;
RT "Cloning and sequence determination of the gene encoding sorbitol
RT dehydrogenase from Saccharomyces cerevisiae.";
RL Gene 140:121-126(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-
CC dependent oxidation of various sugar alcohols. Is active with D-
CC sorbitol (D-glucitol) and xylitol as substrates, leading to the C2-
CC oxidized product D-fructose and D-xylulose, respectively. Is likely
CC involved in the utilization of D-sorbitol as a sole carbon source for
CC growth. Has no activity on mannitol and primary alcohols such as
CC ethanol. {ECO:0000269|PubMed:8125328}.
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:8125328};
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:8125328};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q00796};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q00796};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q00796}.
CC -!- INDUCTION: Induced by sorbitol. {ECO:0000269|PubMed:8125328}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L11039; AAA35027.1; -; Genomic_DNA.
DR EMBL; Z49659; CAA89692.1; -; Genomic_DNA.
DR EMBL; AY693012; AAT93031.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08943.1; -; Genomic_DNA.
DR PIR; S55941; S55941.
DR RefSeq; NP_012693.1; NM_001181817.1.
DR AlphaFoldDB; P35497; -.
DR SMR; P35497; -.
DR BioGRID; 33913; 95.
DR DIP; DIP-1511N; -.
DR IntAct; P35497; 7.
DR MINT; P35497; -.
DR STRING; 4932.YJR159W; -.
DR PaxDb; P35497; -.
DR PRIDE; P35497; -.
DR EnsemblFungi; YJR159W_mRNA; YJR159W; YJR159W.
DR GeneID; 853624; -.
DR KEGG; sce:YJR159W; -.
DR SGD; S000003920; SOR1.
DR VEuPathDB; FungiDB:YJR159W; -.
DR eggNOG; KOG0024; Eukaryota.
DR GeneTree; ENSGT00390000004074; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; P35497; -.
DR OMA; EYKSGHY; -.
DR BioCyc; YEAST:YJR159W-MON; -.
DR BRENDA; 1.1.1.14; 984.
DR Reactome; R-SCE-5652227; Fructose biosynthesis.
DR Reactome; R-SCE-5661270; Formation of xylulose-5-phosphate.
DR PRO; PR:P35497; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P35497; protein.
DR GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019318; P:hexose metabolic process; IEP:SGD.
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 Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..357
FT /note="Sorbitol dehydrogenase 1"
FT /id="PRO_0000160821"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 275..277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 299..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
SQ SEQUENCE 357 AA; 38166 MW; 16843C2040A3334A CRC64;
MSQNSNPAVV LEKVGDIAIE QRPIPTIKDP HYVKLAIKAT GICGSDIHYY RSGGIGKYIL
KAPMVLGHES SGQVVEVGDA VTRVKVGDRV AIEPGVPSRY SDETKEGRYN LCPHMAFAAT
PPIDGTLVKY YLSPEDFLVK LPEGVSYEEG ACVEPLSVGV HSNKLAGVRF GTKVVVFGAG
PVGLLTGAVA RAFGATDVIF VDVFDNKLQR AKDFGATNTF NSSQFSTDKA QDLADGVQKL
LGGNHADVVF ECSGADVCID AAVKTTKVGG TMVQVGMGKN YTNFPIAEVS GKEMKLIGCF
RYSFGDYRDA VNLVATGKVN VKPLITHKFK FEDAAKAYDY NIAHGGEVVK TIIFGPE
