[1]	PROTEIN SEQUENCE. TISSUE=Liver; PubMed=6705798 [NCBI, ExPASy, EBI, Israel, Japan] Jeffery J., Cederlund E., Joernvall H.; "Sorbitol dehydrogenase. The primary structure of the sheep-liver enzyme."; Eur. J. Biochem. 140:7-16(1984).
[2]	SIMILARITY TO ZINC ALCOHOL DEHYDROGENASES. PubMed=6368230 [NCBI, ExPASy, EBI, Israel, Japan] Joernvall H., von Bahr-Lindstroem H., Jeffery J.; "Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family."; Eur. J. Biochem. 140:17-23(1984).
[3]	3D-STRUCTURE MODELING. DOI=10.1021/bi00348a025; PubMed=2936393 [NCBI, ExPASy, EBI, Israel, Japan] Eklund H., Horjales E., Joernvall H., Branden C.I., Jeffery J.; "Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases."; Biochemistry 24:8005-8012(1985).

Comments

CATALYTIC ACTIVITY: L-iditol + NAD⁺ = L-sorbose + NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase 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

PIR

S10065; S10065.

3D structure databases

PDB

1SDG; Model; -; A=1-347.

[ExPASy / RCSB / EBI]

1SDG; -.

P07846; 1-354.

Ontologies

GO:0003939;	Molecular function: L-iditol 2-dehydrogenase activity (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

Phylogenomic databases

HOVERGEN

P07846; -.

Other

ProtoNet

P07846.

UniRef

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

Keywords

3D-structure; Acetylation; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 354`	`354`	`Sorbitol dehydrogenase.`	`PRO_0000160819`
`METAL`	`43 43`		`Zinc; catalytic (By similarity).`
`METAL`	`67 67`		`Zinc; catalytic (By similarity).`
`METAL`	`68 68`		`Zinc; catalytic (By similarity).`
`MOD_RES`	`1 1`		`N-acetylalanine.`
`STRAND`	`4 11`	`8`
`STRAND`	`19 25`	`7`
`STRAND`	`32 41`	`10`
`HELIX`	`44 51`	`8`
`STRAND`	`62 64`	`3`
`STRAND`	`68 76`	`9`
`STRAND`	`88 91`	`4`
`STRAND`	`98 100`	`3`
`HELIX`	`101 103`	`3`
`STRAND`	`126 129`	`4`
`STRAND`	`131 133`	`3`
`HELIX`	`134 136`	`3`
`STRAND`	`137 139`	`3`
`TURN`	`146 148`	`3`
`HELIX`	`149 152`	`4`
`HELIX`	`154 163`	`10`
`TURN`	`164 166`	`3`
`STRAND`	`172 176`	`5`
`HELIX`	`180 191`	`12`
`STRAND`	`195 200`	`6`
`HELIX`	`204 206`	`3`
`HELIX`	`207 212`	`6`
`STRAND`	`217 219`	`3`
`HELIX`	`221 223`	`3`
`HELIX`	`228 235`	`8`
`TURN`	`236 238`	`3`
`STRAND`	`241 247`	`7`
`HELIX`	`250 258`	`9`
`TURN`	`262 264`	`3`
`STRAND`	`266 269`	`4`
`STRAND`	`274 276`	`3`
`STRAND`	`287 289`	`3`
`HELIX`	`297 309`	`13`
`HELIX`	`316 318`	`3`
`STRAND`	`319 321`	`3`
`HELIX`	`325 327`	`3`
`HELIX`	`328 335`	`8`
`STRAND`	`336 339`	`4`
`STRAND`	`342 346`	`5`

Sequence information

Length: 354 AA [This is the length of the unprocessed precursor]

Molecular weight: 37831 Da [This is the MW of the unprocessed precursor]

CRC64: D5FE56BC06F87389 [This is a checksum on the sequence]

        10         20         30         40         50         60 
AKPAAENLSL VVHGPGDLRL ENYPIPEPGP NEVLLKMHSV GICGSDVHYW QGRIGDFVVK 

        70         80         90        100        110        120 
KPMVLGHEAS GTVVKVGSLV RHLQPGDRVA IQPGAPRQTD EFCKIGRYNL SPTIFFCATP 

       130        140        150        160        170        180 
PDDGNLCRFY KHNANFCYKL PDNVTFEEGA LIEPLSVGIH ACRRAGVTLG NKVLVCGAGP 

       190        200        210        220        230        240 
IGLVNLLAAK AMGAAQVVVT DLSASRLSKA KEVGADFILE ISNESPEEIA KKVEGLLGSK 

       250        260        270        280        290        300 
PEVTIECTGV ETSIQAGIYA THSGGTLVLV GLGSEMTSVP LVHAATREVD IKGVFRYCNT 

       310        320        330        340        350 
WPMAISMLAS KSVNVKPLVT HRFPLEKALE AFETSKKGLG LKVMIKCDPS DQNP

P07846 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