DHSO_ALKHC
ID DHSO_ALKHC Reviewed; 343 AA.
AC Q9Z9U1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000250|UniProtKB:Q06004};
DE Short=SDH {ECO:0000250|UniProtKB:Q06004};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q06004};
DE AltName: Full=Glucitol dehydrogenase {ECO:0000250|UniProtKB:Q06004};
DE AltName: Full=L-iditol 2-dehydrogenase {ECO:0000250|UniProtKB:Q06004};
DE EC=1.1.1.14 {ECO:0000250|UniProtKB:Q06004};
DE AltName: Full=Polyol dehydrogenase {ECO:0000250|UniProtKB:Q06004};
DE AltName: Full=Xylitol dehydrogenase {ECO:0000250|UniProtKB:Q06004};
DE EC=1.1.1.9 {ECO:0000250|UniProtKB:Q06004};
GN Name=gutB; OrderedLocusNames=BH0189;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10086842; DOI=10.1007/s007920050096;
RA Takami H., Nakasone K., Ogasawara N., Hirama C., Nakamura Y., Masui N.,
RA Fuji F., Takaki Y., Inoue A., Horikoshi K.;
RT "Sequencing of three lambda clones from the genome of alkaliphilic Bacillus
RT sp. strain C-125.";
RL Extremophiles 3:29-34(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the NAD(+)-dependent
CC oxidation of various sugar alcohols. Is active with D-sorbitol (D-
CC glucitol), xylitol and L-iditol as substrates, leading to the C2-
CC oxidized products D-fructose, D-xylulose and L-sorbose, respectively.
CC {ECO:0000250|UniProtKB:Q06004}.
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:Q06004};
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:0000250|UniProtKB:Q06004};
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:0000250|UniProtKB:Q06004};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q06004};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q06004};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q06004}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB011837; BAA75341.1; -; Genomic_DNA.
DR EMBL; BA000004; BAB03908.1; -; Genomic_DNA.
DR PIR; E83673; E83673.
DR RefSeq; WP_010896371.1; NC_002570.2.
DR AlphaFoldDB; Q9Z9U1; -.
DR SMR; Q9Z9U1; -.
DR STRING; 272558.10172801; -.
DR EnsemblBacteria; BAB03908; BAB03908; BAB03908.
DR KEGG; bha:BH0189; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_9; -.
DR OMA; GVFHNTP; -.
DR OrthoDB; 972769at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 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..343
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000160824"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 262..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
SQ SEQUENCE 343 AA; 36889 MW; 20961F7C34676DFA CRC64;
MKALVKTQHG TGHFAVQEKP EPTPGKHQVK IKVKYTGVCG SDIHTYEGHY PVAAPVTLGH
EFSGEIVELG EGVTGFNVGD RVTSETTYSI CGKCSYCTSG DYNLCSHRKG LGNQQDGSFA
KYVIARQESL HHLPAGVDDR SAAMTEPLAC THHAIAKTSI NKGDLVVVTG PGPIGLLAAQ
VAKSHGGTVI ITGLSNDQVR LKKAKEVGID YAIDTQEVDI KELVSELTDG YGADVVLECS
GAVPAAKQGI DLLRKKGQYA QVGLFAQPEI QFNFEKIIQK EISVVGSRSQ KPADWEPALS
LLNEKKVNAK TLVTHEYTIS EWDKAYHAIK SGEAIKVLLT PID
