RegulonDB

Gene
Name:	galE
Synonym(s):	ECK0748, EG10362, b0759, galD
Genome position(nucleotides):	791039 <-- 792055
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	54.38
External database links:

ASAP:	ABE-0002575
CGSC:	724
ECHOBASE:	EB0357
ECOLIHUB:	galE
MIM:	230350
OU-MICROARRAY:	b0759
STRING:	511145.b0759
COLOMBOS:	galE

Gene

Name:

galE

Synonym(s):

ECK0748, EG10362, b0759, galD

Genome position(nucleotides):

791039 <-- 792055

Strand:

reverse

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

54.38

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

MIM:

OU-MICROARRAY:

STRING:

COLOMBOS:

Type

Positions

Sequence

Comment

4 -> 325

LVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGKHPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRAANVKNFIFSSSATVYGDQPKIPYVESFPTGTPQSPYGKSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNLMPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKLANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYWADASKADRELNWRVTRTLDEMAQDT

11 -> 12

UniProt: NAD.

31 -> 36

DNLCNS

UniProt: NAD.

58 -> 59

UniProt: NAD.

80 -> 84

FAGLK

UniProt: NAD.

Type

Positions

Sequence

Comment

4 -> 325

11 -> 12

UniProt: NAD.

31 -> 36

DNLCNS

UniProt: NAD.

58 -> 59

UniProt: NAD.

80 -> 84

FAGLK

UniProt: NAD.

124 -> 124

UniProt: No major structural changes. Catalytic efficiency is very low and affinity binding is 21% of the wild-type enzyme..

140 -> 145

FPTGTP

UniProt: In Ref. 6; CAA35813..

149 -> 149

UniProt: No major structural changes. Catalytic efficiency is very low and affinity binding is 12% of the wild-type enzyme..

153 -> 153

K153M, K153A decrease activity by more than 10³.

199 -> 200

UniProt: Substrate binding; Sequence Annotation Type: region of interest.

216 -> 218

AIF

UniProt: Substrate binding; Sequence Annotation Type: region of interest.

292 -> 295

REGD

UniProt: Substrate binding; Sequence Annotation Type: region of interest.

299 -> 299

UniProt: Loss of epimerase activity with UDP-Gal by almost 5-fold, but it results in a gain of epimerase activity with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) by 230-fold with minimal changes in its three-dimensional structure..

Multifun Terms (GenProtEC)

1 - metabolism --> 1.1 - carbon utilization --> 1.1.1 - carbon compounds

1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.2 - colanic acid (M antigen)

1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.7 - galactose metabolism

6 - cell structure --> 6.3 - surface antigens (ECA, O antigen of LPS)

6 - cell structure --> 6.7 - capsule (M and K antigens)

Gene Ontology Terms (GO)

cellular_component

GO:0005737 - cytoplasm
GO:0005829 - cytosol

molecular_function

GO:0005515 - protein binding
GO:0016853 - isomerase activity
GO:0003978 - UDP-glucose 4-epimerase activity
GO:0016857 - racemase and epimerase activity, acting on carbohydrates and derivatives
GO:0042802 - identical protein binding
GO:0070403 - NAD+ binding

biological_process

GO:0005975 - carbohydrate metabolic process
GO:0006012 - galactose metabolic process
GO:0009242 - colanic acid biosynthetic process
GO:0033499 - galactose catabolic process via UDP-galactose

Transcriptional Regulation
	Display Regulation
Activated by:	CRP, GalS, GalR
Repressed by:	CRP, H-NS, GalS, HU, GalR

Transcriptional Regulation

Display Regulation

Activated by:

CRP, GalS, GalR

Repressed by:

CRP, H-NS, GalS, HU, GalR

	Type	Name	Post Left	Post Right	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
	promoter	TSS_936	789995		reverse	nd	[RS-EPT-CBR]	[6]

Type

Name

Post Left

Post Right

Strand

Notes

Evidence (Confirmed, Strong, Weak)

References

promoter

TSS_936

789995

reverse

[RS-EPT-CBR]

[6]

Evidence
[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Evidence

[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Reference(s)
[1] Barat B., Bhattacharyya D., 2001, UDP-galactose 4-epimerase from Escherichia coli: formation of catalytic site during reversible folding., Arch Biochem Biophys 391(2):188-96
[2] Bhattacharyya U., Dhar G., Bhaduri A., 1999, An arginine residue is essential for stretching and binding of the substrate on UDP-glucose-4-epimerase from Escherichia coli. Use of a stacked and quenched uridine nucleotide fluorophore as probe., J Biol Chem 274(21):14573-8
[3] Deeley R., Blackburn P., Ferdinand W., 1975, The first enzyme of the gal operon in inducible and operator-constitutive strains of Escherichia coli. A comparison of the porperties and amino-terminal sequences of UDP galactose 4-epimerase., Eur J Biochem 60(2):371-7
[4] Dutta S., Maiti NR., Bhattacharyya D., 1997, Reversible folding of UDP-galactose 4-epimerase from Escherichia coli., Eur J Biochem 244(2):407-13
[5] Nayar S., Bhattacharyya D., 2001, UDP-galactose 4-epimerase from Escherichia coli: equilibrium unfolding studies., Indian J Biochem Biophys 38(6):353-60
[6] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

Reference(s)

[1] Barat B., Bhattacharyya D., 2001, UDP-galactose 4-epimerase from Escherichia coli: formation of catalytic site during reversible folding., Arch Biochem Biophys 391(2):188-96

[2] Bhattacharyya U., Dhar G., Bhaduri A., 1999, An arginine residue is essential for stretching and binding of the substrate on UDP-glucose-4-epimerase from Escherichia coli. Use of a stacked and quenched uridine nucleotide fluorophore as probe., J Biol Chem 274(21):14573-8

[3] Deeley R., Blackburn P., Ferdinand W., 1975, The first enzyme of the gal operon in inducible and operator-constitutive strains of Escherichia coli. A comparison of the porperties and amino-terminal sequences of UDP galactose 4-epimerase., Eur J Biochem 60(2):371-7

[4] Dutta S., Maiti NR., Bhattacharyya D., 1997, Reversible folding of UDP-galactose 4-epimerase from Escherichia coli., Eur J Biochem 244(2):407-13

[5] Nayar S., Bhattacharyya D., 2001, UDP-galactose 4-epimerase from Escherichia coli: equilibrium unfolding studies., Indian J Biochem Biophys 38(6):353-60

[6] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.