[1]	PROTEIN SEQUENCE. STRAIN=A, and D; PubMed=3904726 [NCBI, ExPASy, EBI, Israel, Japan] Dothie J.M., Giglio J.R., Moore C.H., Taylor S.S., Hartley B.S.; "Ribitol dehydrogenase of Klebsiella aerogenes. Sequence and properties of wild-type and mutant strains."; Biochem. J. 230:569-578(1985).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2933028 [NCBI, ExPASy, EBI, Israel, Japan] Loviny T., Norton P.M., Hartley B.S.; "Ribitol dehydrogenase of Klebsiella aerogenes. Sequence of the structural gene."; Biochem. J. 230:579-585(1985).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68. PubMed=3891331 [NCBI, ExPASy, EBI, Israel, Japan] Wu J.C., Anderton-Loviny T., Smith C.A., Hartley B.S.; "Structure of wild-type and mutant repressors and of the control region of the rbt operon of Klebsiella aerogenes."; EMBO J. 4:1339-1344(1985).

Comments

CATALYTIC ACTIVITY: Ribitol + NAD⁺ = D-ribulose + NADH.
SUBUNIT: Homotetramer.
MISCELLANEOUS: The sequence shown is that of strain A.
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

M25606; AAA25140.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02448; CAA26292.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A94585; DEKBR.
S07134; S07134.

3D structure databases

HSSP

Q9HFV6; 1JA9. [HSSP ENTRY / PDB]

ModBase

P00335.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12237; -.

Ontologies

GO:0050255;	Molecular function: ribitol 2-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

PROSITE

PS00061; ADH_SHORT; 1.

Other

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

Keywords

Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 249`	`249`	`Ribitol 2-dehydrogenase.`	`PRO_0000054756`
`NP_BIND`	`20 43`	`24`	`NAD (By similarity).`
`ACT_SITE`	`160 160`		`Proton acceptor (By similarity).`
`VARIANT`	`196 196`	`1`	`A -> P (in strain: D).`
`CONFLICT`	`146 147`		`AV -> SS (in Ref. 2; AAA25140).`
`CONFLICT`	`212 212`		`N -> D (in Ref. 1; AA sequence).`

Sequence information

Length: 249 AA [This is the length of the unprocessed precursor]

Molecular weight: 26514 Da [This is the MW of the unprocessed precursor]

CRC64: C34896C276CC8FBC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKHSVSSMNT SLSGKVAAIT GAASGIGLEC ARTLLGAGAK VVLIDREGEK LNKLVAELGE 

        70         80         90        100        110        120 
NAFALQVDLM QADQVDNLLQ GILQLTGRLD IFHANAGAYI GGPVAEGDPD VWDRVLHLNI 

       130        140        150        160        170        180 
NAAFRCVRSV LPHLIAQKSG DIIFTAVIAG VVPVIWEPVY TASKFAVQAF VHTTRRQVAQ 

       190        200        210        220        230        240 
YGVRVGAVLP GPVVTALLDD WPKAKMDEAL ANGSLMQPIE VAESVLFMVT RSKNVTVRDI 


VILPNSVDL

P00335 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