SDH_CERSP
ID SDH_CERSP Reviewed; 256 AA.
AC Q59787;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000303|PubMed:7551049};
DE Short=SDH {ECO:0000303|PubMed:7551049};
DE EC=1.1.1.- {ECO:0000269|PubMed:7551049};
DE AltName: Full=Galactitol 2-dehydrogenase {ECO:0000305};
DE EC=1.1.1.16 {ECO:0000269|PubMed:7551049};
DE AltName: Full=L-iditol 2-dehydrogenase {ECO:0000305};
DE EC=1.1.1.14 {ECO:0000305|PubMed:7551049};
DE AltName: Full=Polyol dehydrogenase {ECO:0000303|PubMed:7551049};
GN Name=polS; Synonyms=smoS;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND INDUCTION.
RC STRAIN=DSM 8371 / Si4;
RX PubMed=7551049; DOI=10.1099/13500872-141-8-1857;
RA Schauder S., Schneider K.-H., Giffhorn F.;
RT "Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization
RT of a short-chain sorbitol dehydrogenase.";
RL Microbiology 141:1857-1863(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RX PubMed=15805591; DOI=10.1107/s0907444904034390;
RA Philippsen A., Schirmer T., Stein M.A., Giffhorn F., Stetefeld J.;
RT "Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter
RT sphaeroides at 2.4 A resolution.";
RL Acta Crystallogr. D 61:374-379(2005).
CC -!- FUNCTION: Catalyzes the oxidation of D-sorbitol (D-glucitol) to D-
CC fructose. Can also catalyze the oxidation of galactitol to D-tagatose
CC and the oxidation of L-iditol, with lower efficiency.
CC {ECO:0000269|PubMed:7551049}.
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:7551049};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33033;
CC Evidence={ECO:0000305|PubMed:7551049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactitol + NAD(+) = H(+) + keto-D-tagatose + NADH;
CC Xref=Rhea:RHEA:20685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16813,
CC ChEBI:CHEBI:47693, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.16;
CC Evidence={ECO:0000269|PubMed:7551049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20686;
CC Evidence={ECO:0000305|PubMed:7551049};
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:0000305|PubMed:7551049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10161;
CC Evidence={ECO:0000305|PubMed:7551049};
CC -!- ACTIVITY REGULATION: Inhibited by DTT, N-bromosuccinimide and
CC iodoacetic acid. {ECO:0000269|PubMed:7551049}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.2 mM for D-sorbitol {ECO:0000269|PubMed:7551049};
CC KM=1.5 mM for galactitol {ECO:0000269|PubMed:7551049};
CC KM=0.06 mM for NAD(+) (in the presence of D-sorbitol)
CC {ECO:0000269|PubMed:7551049};
CC KM=160 mM for D-fructose {ECO:0000269|PubMed:7551049};
CC KM=13 mM for D-tagatose {ECO:0000269|PubMed:7551049};
CC KM=0.13 mM for NADH (in the presence of D-fructose)
CC {ECO:0000269|PubMed:7551049};
CC pH dependence:
CC Optimum pH is 11 for substrate oxidation and 6.0-7.2 for sugar
CC reduction. {ECO:0000269|PubMed:7551049};
CC -!- SUBUNIT: Homodimer (PubMed:7551049). May function as a tetramer in vivo
CC (PubMed:15805591). {ECO:0000269|PubMed:15805591,
CC ECO:0000269|PubMed:7551049}.
CC -!- INDUCTION: Induced by growth on D-sorbitol.
CC {ECO:0000269|PubMed:7551049}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF018073; AAC45770.1; -; Genomic_DNA.
DR PDB; 1K2W; X-ray; 2.40 A; A/B=1-256.
DR PDBsum; 1K2W; -.
DR AlphaFoldDB; Q59787; -.
DR SMR; Q59787; -.
DR EvolutionaryTrace; Q59787; -.
DR GO; GO:0047713; F:galactitol 2-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing; NAD;
KW Oxidoreductase.
FT CHAIN 1..256
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000054655"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 15..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 59..60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 182..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:1K2W"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1K2W"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1K2W"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:1K2W"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:1K2W"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 150..170
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1K2W"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:1K2W"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1K2W"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1K2W"
SQ SEQUENCE 256 AA; 27014 MW; 33CD7BC17598B02A CRC64;
MRLDGKTALI TGSARGIGRA FAEAYVREGA RVAIADINLE AARATAAEIG PAACAIALDV
TDQASIDRCV AELLDRWGSI DILVNNAALF DLAPIVEITR ESYDRLFAIN VSGTLFMMQA
VARAMIAGGR GGKIINMASQ AGRRGEALVG VYCATKAAVI SLTQSAGLNL IRHGINVNAI
APGVVDGEHW DGVDAKFADY ENLPRGEKKR QVGAAVPFGR MGRAEDLTGM AIFLATPEAD
YIVAQTYNVD GGNWMS
