Reviewed, UniProtKB/Swiss-Prot Q05026 (GALE_NEIGO)

Names and origin

Protein names

Recommended name:
    UDP-glucose 4-epimerase
    EC=5.1.3.2
Alternative name(s):
    UDP-galactose 4-epimerase
    Galactowaldenase

Gene names

Name:

galE

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays an essential role in the incorporation of galactose into meningococcal lipopolysaccharide surface molecules, which are important for pathogenesis.
Catalytic activity	UDP-glucose = UDP-galactose.
Cofactor	NAD.
Pathway	Carbohydrate metabolism; galactose metabolism.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the sugar epimerase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Galactose metabolism
Ligand	NAD
Molecular function	Isomerase
Gene Ontology (GO)
Biological process	galactose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	UDP-glucose 4-epimerase activity Inferred from electronic annotation. Source: EC coenzyme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	UDP-glucose 4-epimerase		PRO_0000183211
Regions
	Nucleotide binding	2 – 33	32	NAD By similarity
Sites
	Active site	149	1	Proton acceptor By similarity
	Binding site	124	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05026-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: C6A905035A083984	FASTA	338	36,885
	10 20 30 40 50 60 MTVLITGGTG FIGSHTAVSL VQSGYDAVIL DNLCNSSAAV LPRLRQITGR NIPFYQGDIR 70 80 90 100 110 120 DCQILRQIFS EHEIESVIHF AGLKAVGESV AEPTKYYGNN VYGSLVLAEE MARAGVLKIV 130 140 150 160 170 180 FSSSATVYGD AEKVPYTEDM RPGDTANPYG ASKAMVERML TDIQKADPRW SVILLRYFNP 190 200 210 220 230 240 IGAHESGLIG EQPNGVPNNL LPYICQVASG RLPQLSVFGG DYPTPDGTGM RDYIHVMDLA 250 260 270 280 290 300 EGHIAAMKAK GGVAGVHLFN LGSGRAYSVL EIIRAFEAAS GLHIPYRIQP RRAGDLACSY 310 320 330 ADPSHTKQQT GWETKRGLQQ MMEDSWRWVS RNPGRYGD

References

[1]	"The role of galE in the biosynthesis and function of gonococcal lipopolysaccharide." Robertson B.D., Frosch M., van Putten J.P.M. Mol. Microbiol. 8:891-901(1993) [PubMed: 8355614] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MS11.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z21508 Genomic DNA. Translation: CAA79721.1.
PIR	S34984.
3D structure databases
HSSP	HSSP built from PDB template 1XEL based on UniProtKB P09147.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.1.3.2. 588.
Family and domain databases
InterPro	IPR001509. Epimerase_deHydtase. IPR005886. GalE. IPR016040. NAD(P)-bd_dom. IPR008089. Nuc_sugar_epim. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR10366:SF39. GalE. 1 hit.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
PRINTS	PR01713. NUCEPIMERASE.
TIGRFAMs	TIGR01179. galE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GALE_NEIGO

Accession

Primary (citable) accession number: Q05026

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 50 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)