NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K5;
PubMed=8801416 [NCBI, ExPASy, EBI, Israel, Japan]
Petit C., Rigg G., Pazzani C., Smith A., Sieberth V., Stevens M., Boulnois G., Jann K., Roberts I.S.;
"Region 2 of the Escherichia coli K5 capsule gene cluster encoding proteins for the biosynthesis of the K5 polysaccharide.";
Mol. Microbiol. 17:611-620(1995).

Comments

FUNCTION: Catalyzes the formation of UDP-glucuronic acid which is required for K5 capsule synthesis.
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: Context: Capsular polysaccharide biosynthesis (CPS).
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

X77617; CAA54708.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S70197; S70197.

3D structure databases

HSSP

Q07172; 1DLI. [HSSP ENTRY / PDB]

ModBase

Q47329.

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.
IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
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.

PANTHER

PTHR11374; UDPG_MGDP_DH_Creg; 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

Capsule biogenesis/degradation; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 392`	`392`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074045`
`NP_BIND`	`6 23`	`18`	`NAD (Potential).`
`ACT_SITE`	`257 257`		`By similarity.`

Sequence information

Length: 392 AA [This is the length of the unprocessed precursor]

Molecular weight: 44108 Da [This is the MW of the unprocessed precursor]

CRC64: 69E15A27FCD25C79 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFGTLKITVS GAGYVGLSNG ILMAQNHEVV AFDTHQKKVD LLNDKLSPIE DKEIENYLST 

        70         80         90        100        110        120 
KILNFRATTN KYEAYKNANY VIIATPTNYD PGSNYFDTSS VEAVIRDVTE INPNAIMVVK 

       130        140        150        160        170        180 
STVPVGFTKT IKEHLGINNI IFSPEFLREG RALYDNLHPS RIIIGECSER AERLAVLFQE 

       190        200        210        220        230        240 
GAIKQNIPVL FTDSTEAEAI KLFSNTYLAM RVAFFNELDS YAESFGLNTR QIIDGVCLDP 

       250        260        270        280        290        300 
RIGNYYNNPS FGYGGYCLPK DTKQLLANYQ SVPNKLISAI VDANRTRKDF ITNVILKHRP 

       310        320        330        340        350        360 
QVVGVYRLIM KSGSDNFRDS SILGIIKRIK KKGVKVIIYE PLISGDTFFN SPLERELAIF 

       370        380        390 
KGKADIIITN RMSEELNDVV DKVYSRDLFK CD

Q47329 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