RegulonDB RegulonDB 10.9: Gene Form
   

galE gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

modF galT galE GalS GalR H-NS CRP H-NS H-NS H-NS HU HU GalR GalS Spot42 galEp3 galEp3 galEp2 galEp2 galEp1 galEp1 galKp galKp TSS_936 TSS_936

Gene      
Name: galE    Texpresso search in the literature
Synonym(s): ECK0748, EG10362, b0759, galD
Genome position(nucleotides): 791039 <-- 792055 Genome Browser
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


Product      
Name: UDP-glucose 4-epimerase
Synonym(s): GalD, GalE
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 37.265
Isoelectric point: 6.313
Motif(s):
 
Type Positions Sequence
149 -> 149 Y
216 -> 218 AIF
292 -> 295 REGD
299 -> 299 Y
4 -> 325 LVTGGSGYIGSHTCVQLLQNGHDVIILDNLCNSKRSVLPVIERLGGKHPTFVEGDIRNEALMTEILHDHAIDTVIHFAGLKAVGESVQKPLEYYDNNVNGTLRLISAMRAANVKNFIFSSSATVYGDQPKIPYVESFPTGTPQSPYGKSKLMVEQILTDLQKAQPDWSIALLRYFNPVGAHPSGDMGEDPQGIPNNLMPYIAQVAVGRRDSLAIFGNDYPTEDGTGVRDYIHVMDLADGHVVAMEKLANKPGVHIYNLGAGVGNSVLDVVNAFSKACGKPVNYHFAPRREGDLPAYWADASKADRELNWRVTRTLDEMAQDT

 
Classification:
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
Note(s): Note(s): ...[more].
Reference(s): [1] Barat B., et al., 2001
[2] Bhattacharyya U., et al., 1999
[3] Deeley R., et al., 1975
[4] Dutta S., et al., 1997
[5] Nayar S., et al., 2001
External database links:  
DIP:
 DIP-9728N
ECOCYC:
 UDPGLUCEPIM-MONOMER
ECOLIWIKI:
 b0759
INTERPRO:
 IPR036291
INTERPRO:
 IPR016040
INTERPRO:
 IPR005886
MODBASE:
 P09147
PDB:
 1LRK
PDB:
 1LRL
PDB:
 1NAH
PDB:
 1NAI
PDB:
 1UDA
PDB:
 1UDB
PDB:
 1UDC
PDB:
 1XEL
PDB:
 2UDP
PDB:
 5GY7
PDB:
 1LRJ
PDB:
 1KVU
PDB:
 1KVT
PDB:
 1KVS
PDB:
 1KVR
PDB:
 1KVQ
PDB:
 1A9Z
PDB:
 1A9Y
PFAM:
 PF16363
PRIDE:
 P09147
REFSEQ:
 NP_415280
SMR:
 P09147
UNIPROT:
 P09147


Operon      
Name: galETKM         
Operon arrangement:
Transcription unit        Promoter
galK
galE
galET
galETK
galETKM
galE
galET
galETK
galETKM
galE
galET
galETK
galETKM
galETKM


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


Elements in the selected gene context region unrelated to any object in RegulonDB      

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


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.

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