Reviewed, UniProtKB/Swiss-Prot Q59787 (DHSO_RHOSH)

Names and origin

Protein names

Recommended name:
    Sorbitol dehydrogenase
    EC=1.1.1.14
Alternative name(s):
    L-iditol 2-dehydrogenase
    Polyol dehydrogenase

Gene names

Name:	polS
Synonyms:	smoS

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidation of D-glucitol (sorbitol) to D-fructose, galactitol to D-tagatose and of L-iditol.
Catalytic activity	L-iditol + NAD(+) = L-sorbose + NADH.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-iditol 2-dehydrogenase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 256

256

Sorbitol dehydrogenase

PRO_0000054655

Regions

Nucleotide binding

5 – 34

30

NAD By similarity

Sites

Active site

152

1

Proton acceptor By similarity

Binding site

139

1

Substrate By similarity

Secondary structure

1

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256

Helix Strand Turn

Details...

Turn

2 – 5

4

Beta strand

6 – 11

6

Helix

16 – 27

12

Beta strand

30 – 37

8

Helix

39 – 49

11

Beta strand

53 – 57

5

Helix

63 – 77

15

Beta strand

82 – 85

4

Helix

95 – 97

3

Helix

100 – 110

11

Helix

112 – 128

17

Beta strand

132 – 137

6

Helix

140 – 142

3

Helix

150 – 170

21

Helix

171 – 173

3

Beta strand

175 – 182

8

Helix

190 – 201

12

Helix

207 – 215

9

Helix

224 – 233

10

Helix

237 – 239

3

Beta strand

246 – 250

5

Sequences

	Sequence		Length	Mass (Da)
	Q59787-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 33CD7BC17598B02A	FASTA	256	27,014
	10 20 30 40 50 60 MRLDGKTALI TGSARGIGRA FAEAYVREGA RVAIADINLE AARATAAEIG PAACAIALDV 70 80 90 100 110 120 TDQASIDRCV AELLDRWGSI DILVNNAALF DLAPIVEITR ESYDRLFAIN VSGTLFMMQA 130 140 150 160 170 180 VARAMIAGGR GGKIINMASQ AGRRGEALVG VYCATKAAVI SLTQSAGLNL IRHGINVNAI 190 200 210 220 230 240 APGVVDGEHW DGVDAKFADY ENLPRGEKKR QVGAAVPFGR MGRAEDLTGM AIFLATPEAD 250 YIVAQTYNVD GGNWMS

References

[1]	"Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase." Schauder S., Schneider K.-H., Giffhorn F. Microbiology 141:1857-1863(1995) [PubMed: 7551049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: SI-4.
[2]	"Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution." Philippsen A., Schirmer T., Stein M.A., Giffhorn F., Stetefeld J. Acta Crystallogr. D 61:374-379(2005) [PubMed: 15805591] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF018073 Genomic DNA. Translation: AAC45770.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K2W	X-ray	2.40	A/B	1-256	[»]
1UZO	model	-	A	1-256	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR002198. DHase_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHSO_RHOSH

Accession

Primary (citable) accession number: Q59787

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)