[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=SI-4; PubMed=7551049 [NCBI, ExPASy, EBI, Israel, Japan] Schauder S., Schneider K.-H., Giffhorn F.; "Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase."; Microbiology 141:1857-1863(1995).
[2]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1107/S0907444904034390; PubMed=15805591 [NCBI, ExPASy, EBI, Israel, Japan] Philippsen A., Schirmer T., Stein M.A., Giffhorn F., Stetefeld J.; "Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution."; Acta Crystallogr. D 61:374-379(2005).

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: Homodimer.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF018073; AAC45770.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1K2W; X-ray; 2.40 A; A/B=1-256.	[ExPASy / RCSB / EBI]
1UZO; Model; -; A=1-256.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1K2W; -.
1UZO; -.

ModBase

Q59787.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 256`	`256`	`Sorbitol dehydrogenase.`	`PRO_0000054655`
`NP_BIND`	`5 34`	`30`	`NAD (By similarity).`
`ACT_SITE`	`152 152`		`Proton acceptor (By similarity).`
`BINDING`	`139 139`		`Substrate (By similarity).`
`TURN`	`2 5`	`4`
`STRAND`	`6 11`	`6`
`HELIX`	`16 27`	`12`
`STRAND`	`30 37`	`8`
`HELIX`	`39 49`	`11`
`STRAND`	`53 57`	`5`
`HELIX`	`63 77`	`15`
`STRAND`	`82 85`	`4`
`HELIX`	`95 97`	`3`
`HELIX`	`100 110`	`11`
`HELIX`	`112 128`	`17`
`STRAND`	`132 137`	`6`
`HELIX`	`140 142`	`3`
`HELIX`	`150 170`	`21`
`HELIX`	`171 173`	`3`
`STRAND`	`175 182`	`8`
`HELIX`	`190 201`	`12`
`HELIX`	`207 215`	`9`
`HELIX`	`224 233`	`10`
`HELIX`	`237 239`	`3`
`STRAND`	`246 250`	`5`

Sequence information

Length: 256 AA [This is the length of the unprocessed precursor]

Molecular weight: 27014 Da [This is the MW of the unprocessed precursor]

CRC64: 33CD7BC17598B02A [This is a checksum on the sequence]

        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

Q59787 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools