P09147 (GALE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-glucose 4-epimerase
EC=5.1.3.2

Alternative name(s):
Galactowaldenase
UDP-galactose 4-epimerase

Gene names

Name:	galE
Synonyms:	galD
Ordered Locus Names:	b0759, JW0742

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	UDP-glucose = UDP-galactose.
Cofactor	NAD.
Pathway	Carbohydrate metabolism; galactose metabolism.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the sugar epimerase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Galactose metabolism
Ligand	NAD
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	colanic acid biosynthetic process Inferred from mutant phenotype. Source: EcoCyc galactose catabolic process via UDP-galactose Inferred from mutant phenotype. Source: EcoCyc
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	NAD+ binding Inferred from direct assay. Source: EcoCyc UDP-glucose 4-epimerase activity Inferred from direct assay. Source: EcoCyc
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_0000183203

Regions

Nucleotide binding

2 – 33

32

NAD

Sites

Active site

149

1

Proton acceptor

Binding site

124

1

Substrate

Experimental info

Sequence conflict

140 – 145

6

FPTGTP → LLPIPG Ref.6

Secondary structure

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338

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Turn

7 – 9

3

Helix

11 – 22

12

Beta strand

26 – 31

6

Beta strand

34 – 36

3

Helix

40 – 48

9

Beta strand

53 – 56

4

Helix

62 – 71

10

Beta strand

76 – 79

4

Helix

86 – 91

6

Helix

93 – 113

21

Beta strand

118 – 124

7

Helix

125 – 128

4

Beta strand

133 – 136

4

Helix

148 – 166

19

Beta strand

171 – 177

7

Beta strand

179 – 181

3

Beta strand

187 – 189

3

Beta strand

194 – 196

3

Helix

200 – 208

9

Beta strand

211 – 213

3

Beta strand

215 – 218

4

Beta strand

222 – 228

7

Beta strand

233 – 235

3

Helix

236 – 250

15

Beta strand

255 – 262

8

Helix

269 – 280

12

Beta strand

286 – 289

4

Helix

304 – 310

7

Helix

318 – 331

14

Sequences

	Sequence		Length	Mass (Da)
	P09147 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 5CA8B4F7903F7792	FASTA	338	37,265
	10 20 30 40 50 60 MRVLVTGGSG YIGSHTCVQL LQNGHDVIIL DNLCNSKRSV LPVIERLGGK HPTFVEGDIR 70 80 90 100 110 120 NEALMTEILH DHAIDTVIHF AGLKAVGESV QKPLEYYDNN VNGTLRLISA MRAANVKNFI 130 140 150 160 170 180 FSSSATVYGD QPKIPYVESF PTGTPQSPYG KSKLMVEQIL TDLQKAQPDW SIALLRYFNP 190 200 210 220 230 240 VGAHPSGDMG EDPQGIPNNL MPYIAQVAVG RRDSLAIFGN DYPTEDGTGV RDYIHVMDLA 250 260 270 280 290 300 DGHVVAMEKL ANKPGVHIYN LGAGVGNSVL DVVNAFSKAC GKPVNYHFAP RREGDLPAYW 310 320 330 ADASKADREL NWRVTRTLDE MAQDTWHWQS RHPQGYPD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequences of the gal E gene and the gal T gene of E. coli." Lemaire H.-G., Mueller-Hill B. Nucleic Acids Res. 14:7705-7711(1986) [PubMed: 3022232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Lemaire H.-G. Submitted (APR-1988) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Completed sequence of pKG1800, a vector for determination of transcription terminators." Bernardi F., Bernardi A. DNA Seq. 1:147-150(1990) [PubMed: 2134186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
[7]	"Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene." Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R. Microbiol. Res. 150:347-361(1995) [PubMed: 8564363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31. Strain: K12.
[8]	"Segment-specific mutagenesis of the regulatory region in the Escherichia coli galactose operon: isolation of mutations reducing the initiation of transcription and translation." Busby S., Dreyfus M. Gene 21:121-131(1983) [PubMed: 6301942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[9]	"The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5-A resolution." Bauer A.J., Rayment I., Frey P.A., Holden H.M. Proteins 12:372-381(1992) [PubMed: 1579570] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[10]	"Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli." Thoden J.B., Frey P.A., Holden H.M. Biochemistry 35:2557-2566(1996) [PubMed: 8611559] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[11]	"High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol." Thoden J.B., Frey P.A., Holden H.M. Protein Sci. 5:2149-2161(1996) [PubMed: 8931134] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[12]	"Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli." Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M. Biochemistry 36:6294-6304(1997) [PubMed: 9174344] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE.
[13]	"Molecular structures of the S124A, S124T, and S124V site-directed mutants of UDP-galactose 4-epimerase from Escherichia coli." Thoden J.B., Gulick A.M., Holden H.M. Biochemistry 36:10685-10695(1997) [PubMed: 9271499] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS ALA-124; THR-124 AND VAL-124 IN COMPLEX WITH NAD AND SUBSTRATE.
[14]	"Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli." Thoden J.B., Holden H.M. Biochemistry 37:11469-11477(1998) [PubMed: 9708982] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF DOUBLE MUTANT ALA-124/PHE-149 IN COMPLEX WITH SUBSTRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06226 Genomic DNA. Translation: CAA29573.1.
U00096 Genomic DNA. Translation: AAC73846.1.
AP009048 Genomic DNA. Translation: BAA35421.1.
X51449 Genomic DNA. Translation: CAA35813.1.
U07867 Genomic DNA. Translation: AAB06890.1.
J01613 Genomic DNA. Translation: AAA87978.1.

PIR

XUECUG. S02089.

RefSeq

NP_415280.3. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A9Y	X-ray	1.80	A	1-338	[»]
1A9Z	X-ray	1.90	A	1-338	[»]
1KVQ	X-ray	2.15	A	1-338	[»]
1KVR	X-ray	1.90	A	1-338	[»]
1KVS	X-ray	2.15	A	1-338	[»]
1KVT	X-ray	2.15	A	1-338	[»]
1KVU	X-ray	1.90	A	1-338	[»]
1LRJ	X-ray	1.90	A	1-338	[»]
1LRK	X-ray	1.75	A	1-338	[»]
1LRL	X-ray	1.80	A	1-338	[»]
1NAH	X-ray	1.80	A	1-338	[»]
1NAI	X-ray	2.00	A	1-338	[»]
1UDA	X-ray	1.80	A	1-338	[»]
1UDB	X-ray	1.65	A	1-338	[»]
1UDC	X-ray	1.65	A	1-338	[»]
1XEL	X-ray	1.80	A	1-338	[»]
2UDP	X-ray	1.80	A/B	1-338	[»]

ProteinModelPortal

P09147.

SMR

P09147. Positions 1-338.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9728N.

IntAct

P09147. 5 interactions.

2D gel databases

SWISS-2DPAGE

P09147.

2DBase-Ecoli

P09147.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004431; EBESCP00000004431; EBESCG00000003616.
EBESCT00000004432; EBESCP00000004432; EBESCG00000003616.
EBESCT00000004433; EBESCP00000004433; EBESCG00000003616.
EBESCT00000014770; EBESCP00000014061; EBESCG00000013830.

GeneID

945354.

GenomeReviews

Gene locus JW0742 in contig AP009048_GR.
Gene locus b0759 in contig U00096_GR.

KEGG

ecj:JW0742.
eco:b0759.

PATRIC

32116719. VBIEscCol129921_0785.

Organism-specific databases

EchoBASE

EB0357.

EcoGene

EG10362. galE.

Phylogenomic databases

eggNOG

COG1087.

GeneTree

EBGT00050000008809.

HOGENOM

HBG755066.

OMA

PYQESFP.

PhylomeDB

P09147.

ProtClustDB

PRK10675.

Enzyme and pathway databases

BioCyc

EcoCyc:UDPGLUCEPIM-MONOMER.
MetaCyc:UDPGLUCEPIM-MONOMER.

Gene expression databases

Genevestigator

P09147.

Family and domain databases

InterPro

IPR001509. Epimerase_deHydtase.
IPR005886. GalE.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K01784.

PANTHER

PTHR10366:SF39. GalE. 1 hit.

Pfam

PF01370. Epimerase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01179. GalE. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GALE_ECOLI

Accession

Primary (citable) accession number: P09147
Secondary accession number(s): Q47493

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program