[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Hypothalamus; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: L-iditol + NAD⁺ = L-sorbose + NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Homotetramer (By similarity).
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

EMBL

BT021766; AAX46613.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC122783; AAI22784.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001032397.1; -.

UniGene

Bt.16122

3D structure databases

SMR

Q58D31; 1-355, 2-356.

ModBase

Q58D31.

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.

BLOCKS

Q58D31.

Genome annotation databases

Ensembl

ENSBTAG00000025496; Bos taurus. [Contig view]

GeneID

508954; -.

KEGG

bta:508954; -.

Phylogenomic databases

HOVERGEN

Q58D31; -.

Other

ProtoNet

Q58D31.

UniRef

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

Keywords

Acetylation; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 356`	`355`	`Sorbitol dehydrogenase.`	`PRO_0000239652`
`METAL`	`44 44`		`Zinc; catalytic (By similarity).`
`METAL`	`69 69`		`Zinc; catalytic (By similarity).`
`METAL`	`70 70`		`Zinc; catalytic (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`

Sequence information

Length: 356 AA [This is the length of the unprocessed precursor]

Molecular weight: 38099 Da [This is the MW of the unprocessed precursor]

CRC64: F7E3ACD6712E71B1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAKPENLS LVVHGPGDLR LENYPIPEPG PNEVLLKMHS VGICGSDVHY WQHGRIGDFV 

        70         80         90        100        110        120 
VKKPMVLGHE ASGTVVKVGS LVRHLQPGDR VAIEPGAPRE TDEFCKIGRY NLSPTIFFCA 

       130        140        150        160        170        180 
TPPDDGNLCR FYKHNANFCY KLPDNVTFEE GALIEPLSVG IHACRRAGVT LGNKVLVCGA 

       190        200        210        220        230        240 
GPIGLVSLLA AKAMGAAQVV VTDLSASRLS KAKEVGADFI LQISNESPQE IAKKVEGLLG 

       250        260        270        280        290        300 
SKPEVTIECT GVETSIQAGI YATHSGGTLV LVGLGSEMTS VPLVHAATRE VDIKGVFRYC 

       310        320        330        340        350 
NTWPMAISML ASKSVNVKPL VTHRFPLEKA LEAFETSKKG LGLKVMIKCD PNDQNP

Q58D31 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