NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=O111:H- / M92 / EPEC;
PubMed=7682279 [NCBI, ExPASy, EBI, Israel, Japan]
Bastin D.A., Stevenson G., Brown P.K., Haase A., Reeves P.R.;
"Repeat unit polysaccharides of bacteria: a model for polymerization resembling that of ribosomes and fatty acid synthetase, with a novel mechanism for determining chain length.";
Mol. Microbiol. 7:725-734(1993).

Comments

CATALYTIC ACTIVITY: UDP-glucose + 2 NAD⁺ + H₂O = UDP-glucuronate + 2 NADH.
PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronate biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1 .
PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis .
PTM: Phosphorylated on a tyrosine residue. It results in a significant increase of the dehydrogenase activity (By similarity).
SIMILARITY: Belongs to the UDP-glucose/GDP-mannose 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

Z17241; CAA78939.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33668; S33668.

3D structure databases

HSSP

Q07172; 1DLJ. [HSSP ENTRY / PDB]

ModBase

Q04872.

Ontologies

GO:0003979;	Molecular function: UDP-glucose 6-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

IPR016040; NAD(P)-bd.
IPR017476; Nucleotide_sugar_DH.
IPR014027; UDP-Glc/GDP-Man_DHase_C.
IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
IPR001732; UDP-Glc/GDP-Man_DHase_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.

Pfam

PF00984; UDPG_MGDP_dh; 1.
PF03720; UDPG_MGDP_dh_C; 1.
PF03721; UDPG_MGDP_dh_N; 1.
Pfam graphical view of domain structure.

Other

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

Keywords

NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 388`	`388`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074044`
`NP_BIND`	`2 19`	`18`	`NAD (Potential).`
`ACT_SITE`	`253 253`		`By similarity.`

Sequence information

Length: 388 AA [This is the length of the unprocessed precursor]

Molecular weight: 43289 Da [This is the MW of the unprocessed precursor]

CRC64: E85B4550BB1FA02F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKITISGTGY VGLSNGILIA QHHEVVALDI VPTKVEMLNQ KKSPIVDKEI EEYLATKQLN 

        70         80         90        100        110        120 
FRATTDKYDA YRDGTYVIIA TPTDYDPKTN YFNTSSVESV IRDVVDINPN AVMVIKSTIP 

       130        140        150        160        170        180 
VGFTNLLKER LGIDNIFFSP EFLREGRALY DNLHPSRIVI GERSERAGRF AALLQEGAVK 

       190        200        210        220        230        240 
KDIPTLFTDS TEAEAIKLFA NTYLALRVAY FNELDSYAES LGLNSRQIIE GVCLDPRIGN 

       250        260        270        280        290        300 
HYNNPSFGYG GYCLPKDTKQ LLANYASVPN NIIGAIVDAN RTRKDFIADS ILARKPKVVG 

       310        320        330        340        350        360 
VYRLIMKSGS DNFRASSIQG IMKRIKAKGV PVIIYEPVMV EDEFFHSRVV RDLTAFKNEA 

       370        380 
DIIISNRMTS ELADVADKVY TRGLFGSD

Q04872 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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