Reviewed, UniProtKB/Swiss-Prot Q04872 (UDG_ECO11)

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:

ugd

Organism

Escherichia coli O111:H-

Taxonomic identifier

168927 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH.
Pathway	Nucleotide-sugar biosynthesis; UDP-glucuronate biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1. Bacterial outer membrane biogenesis; lipopolysaccharide 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
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD 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 – 388	388	UDP-glucose 6-dehydrogenase		PRO_0000074044
Regions
	Nucleotide binding	2 – 19	18	NAD Potential
Sites
	Active site	253	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04872-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: E85B4550BB1FA02F	FASTA	388	43,289
	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

References

[1]

"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." Bastin D.A., Stevenson G., Brown P.K., Haase A., Reeves P.R. Mol. Microbiol. 7:725-734(1993) [PubMed: 7682279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O111:H- / M92 / EPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z17241 Genomic DNA. Translation: CAA78939.1.
PIR	S33668.
3D structure databases
HSSP	HSSP built from PDB template 1DLJ based on UniProtKB Q07172.
ModBase	Search...
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 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]
ProtoNet	Search...

Entry information

Entry name

UDG_ECO11

Accession

Primary (citable) accession number: Q04872

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 25, 2008
This is version 52 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)