[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; Mizobuchi K.; Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan] Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."; Nucleic Acids Res. 23:2105-2119(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

CATALYTIC ACTIVITY: D-mannonate + NAD⁺ = D-fructuronate + NADH.
PATHWAY: Carbohydrate metabolism; pentose and glucuronate interconversion .
SIMILARITY: Belongs to the mannitol dehydrogenase family. UxuB subfamily.

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

D13329; BAA02591.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97219.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77279.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78316.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S56548; S56548.

RefSeq

AP_004815.1; -.
NP_418743.1; -.

3D structure databases

HSSP

O08355; 1LJ8. [HSSP ENTRY / PDB]

ModBase

P39160.

Protein-protein interaction databases

DIP

DIP:11109N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:MANNONOXIDOREDUCT-MON; -.
MetaCyc:MANNONOXIDOREDUCT-MON; -.

Organism-specific databases

EchoBASE

EB4150; -.

EcoGene

EG20248; uxuB.

Ontologies

GO:0008866;	Molecular function: fructuronate reductase 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

IPR013328; DHase_multihelical.
IPR013118; Mannitol_DHase_C.
IPR000669; Mannitol_DHase_core.
IPR013131; Mannitol_DHase_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF01232; Mannitol_dh; 1.
PF08125; Mannitol_dh_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00084; MTLDHDRGNASE.

PROSITE

PS00974; MANNITOL_DHGENASE; 1.

Genome annotation databases

GeneID

946795; -.

GenomeReviews

U00096_GR; b4323.
AP009048_GR; JW4286.

KEGG

ecj:JW4286; -.
eco:b4323; -.

Phylogenomic databases

HOGENOM

P39160; -.

Genome annotation databases

CMR

P39160; b4323.

Other

UniRef

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

Keywords

Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 486`	`486`	`D-mannonate oxidoreductase.`	`PRO_0000170747`
`NP_BIND`	`25 36`	`12`	`NAD (By similarity).`

Sequence information

Length: 486 AA [This is the length of the unprocessed precursor]

Molecular weight: 53580 Da [This is the MW of the unprocessed precursor]

CRC64: 7835638682AF7B87 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTIVDSNLP VARPSWDHSR LESRIVHLGC GAFHRAHQAL YTHHLLESTD SDWGICEVNL 

        70         80         90        100        110        120 
MPGNDRVLIE NLKKQQLLYT VAEKGAESTE LKIIGSMKEA LHPEIDGCEG ILNAMARPQT 

       130        140        150        160        170        180 
AIVSLTVTEK GYCADAASGQ LDLNNPLIKH DLENPTAPKS AIGYIVEALR LRREKGLKAF 

       190        200        210        220        230        240 
TVMSCDNVRE NGHVAKVAVL GLAQARDPQL AAWIEENVTF PCTMVDRIVP AATPETLQEI 

       250        260        270        280        290        300 
ADQLGVYDPC AIACEPFRQW VIEDNFVNGR PDWDKVGAQF VADVVPFEMM KLRMLNGSHS 

       310        320        330        340        350        360 
FLAYLGYLGG YETIADTVTN PAYRKAAFAL MMQEQAPTLS MPEGTDLNAY ATLLIERFSN 

       370        380        390        400        410        420 
PSLRHRTWQI AMDGSQKLPQ RLLDPVRLHL QNGGSWRHLA LGVAGWMRYT QGVDEQGNAI 

       430        440        450        460        470        480 
DVVDPMLAEF QKINAQYQGA DRVKALLGLS GIFADDLPQN ADFVGAVTAA YQQLCERGAR 


ECVAAL

P39160 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