DHSO_SCHPO
ID DHSO_SCHPO Reviewed; 360 AA.
AC P36624;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Sorbitol dehydrogenase;
DE Short=SDH;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P35497};
DE AltName: Full=Polyol dehydrogenase {ECO:0000305};
DE AltName: Full=Protein tms1;
GN Name=tms1; ORFNames=SPBC1773.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-360, AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8223615; DOI=10.1111/j.1432-1033.1993.tb18299.x;
RA Wagner P., Grimaldi M., Jenkins J.R.;
RT "Putative dehydrogenase tms1 suppresses growth arrest induced by a p53
RT tumour mutant in fission yeast.";
RL Eur. J. Biochem. 217:731-736(1993).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-
CC dependent oxidation of various sugar alcohols. Is active with D-
CC sorbitol (D-glucitol) as substrate, leading to the C2-oxidized product
CC D-fructose (By similarity). Suppresses growth arrest induced by a p53
CC tumor mutant in fission yeast (PubMed:8223615).
CC {ECO:0000250|UniProtKB:P35497, ECO:0000269|PubMed:8223615}.
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:0000250|UniProtKB:P35497};
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU329671; CAA21910.1; -; Genomic_DNA.
DR EMBL; X74422; CAA52443.1; ALT_INIT; Genomic_DNA.
DR PIR; T39670; S35981.
DR RefSeq; NP_595120.1; NM_001021027.2.
DR AlphaFoldDB; P36624; -.
DR SMR; P36624; -.
DR BioGRID; 276656; 1.
DR STRING; 4896.SPBC1773.05c.1; -.
DR MaxQB; P36624; -.
DR PaxDb; P36624; -.
DR PRIDE; P36624; -.
DR EnsemblFungi; SPBC1773.05c.1; SPBC1773.05c.1:pep; SPBC1773.05c.
DR GeneID; 2540119; -.
DR KEGG; spo:SPBC1773.05c; -.
DR PomBase; SPBC1773.05c; tms1.
DR VEuPathDB; FungiDB:SPBC1773.05c; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; P36624; -.
DR OMA; EYKSGHY; -.
DR PhylomeDB; P36624; -.
DR Reactome; R-SPO-5652227; Fructose biosynthesis.
DR Reactome; R-SPO-5661270; Formation of xylulose-5-phosphate.
DR PRO; PR:P36624; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0046526; F:D-xylulose reductase activity; ISO:PomBase.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; ISO:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 3: Inferred from homology;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..360
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000160823"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
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 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 277..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 301..303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
SQ SEQUENCE 360 AA; 38851 MW; ADEB3DDBA163224C CRC64;
MAPAEKAFVL RKKMDTAIED RPGQTLTDDH QVKVAIKATG ICGSDVHYWK EGGIGDFILK
KPMILGHESA GVVVEVGKGV SSLKPGDPVA VEPGCVCRLC DYCRSGRYNL CPHMEFAATP
PYDGTLRTYY ITTEDFCTKL PKQISVEEGA LFEPMSVAVH AMTRGNLKCG SRVLVMGCGT
VGLLMMAVAK AYGAIDIVAV DASPSRVEFA QKYVGAKPFT PIAAKENESL PDYAQRYKQA
IIEKYGEFDF AVDATGVGIC IHTAVLALKR GGTFVQAGNG KPVIDFPINH IINYEINVLG
SFRYAHGCYK QSLFLVSNGL VDVKPLITHR FAFKDALKAY ETVASGEEGV LKVIIGGPDA
