Reviewed, UniProtKB/Swiss-Prot Q47329 (UDG5_ECOLX)

Names and origin

Protein names

Recommended name:
    UDP-glucose 6-dehydrogenase
      Short name=UDP-Glc dehydrogenase
      Short name=UDP-GlcDH
      Short name=UDPGDH
    EC=1.1.1.22

Gene names

Name:

kfiD

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (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-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. Capsule biogenesis; capsule polysaccharide biosynthesis.
Post-translational modification	Phosphorylated on a tyrosine residue. It results in a significant increase of the dehydrogenase activity By similarity.
Sequence similarities	Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Ontologies

Keywords
Biological process	Capsule biogenesis/degradation
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro UDP-glucose 6-dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	UDP-glucose 6-dehydrogenase		PRO_0000074045
Regions
	Nucleotide binding	6 – 23	18	NAD Potential
Sites
	Active site	257	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q47329-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 69E15A27FCD25C79	FASTA	392	44,108
	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

References

[1]

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77617 Genomic DNA. Translation: CAA54708.1.
PIR	S70197.
3D structure databases
SMR	Q47329. Positions 5-392.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.22. 246.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR016040. NAD(P)-bd_dom. IPR017476. Nucleotide_sugar_DH. IPR014027. UDP-Glc/GDP-Man_DH_C. IPR014026. UDP-Glc/GDP-Man_DH_dimer. IPR014028. UDP-Glc/GDP-Man_DH_dimer-bd. IPR001732. UDP-Glc/GDP-Man_DH_N. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 1 hit.
PANTHER	PTHR11374. UDPG_MGDP_DH_Creg. 1 hit.
Pfam	PF00984. UDPG_MGDP_dh. 1 hit. PF03720. UDPG_MGDP_dh_C. 1 hit. PF03721. UDPG_MGDP_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR03026. NDP-sugDHase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

UDG5_ECOLX

Accession

Primary (citable) accession number: Q47329

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)