RegulonDB RegulonDB 10.7: Gene Form
   

uidA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

uidA uidB uidC uidR UidR CRP UxuR uidAp uidAp uidCp6 uidCp6 uidCp5 uidCp5

Gene      
Name: uidA    Texpresso search in the literature
Synonym(s): ECK1612, EG11055, b1617, gurA, gusA
Genome position(nucleotides): 1694260 <-- 1696071 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
52.26
External database links:  
ASAP:
ABE-0005410
CGSC:
36
ECHOBASE:
EB1048
MIM:
253220
OU-MICROARRAY:
b1617
PORTECO:
uidA
REGULONDB:
b1617
STRING:
511145.b1617
M3D: uidA
COLOMBOS: uidA
PortEco: b1617


Product      
Name: β-glucuronidase
Synonym(s): GurA, GusA, UidA
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 68.447
Isoelectric point: 5.118
Motif(s):
 
Type Positions Sequence
184 -> 272 VDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIR
12 -> 180 IKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTP
274 -> 593 VAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNF

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.1 - carbon utilization --> 1.1.1 - carbon compounds
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
GO:0032991 - protein-containing complex
molecular_function GO:0016787 - hydrolase activity
GO:0004553 - hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 - hydrolase activity, acting on glycosyl bonds
GO:0004566 - beta-glucuronidase activity
GO:0030246 - carbohydrate binding
GO:0042802 - identical protein binding
biological_process GO:0008152 - metabolic process
GO:0005975 - carbohydrate metabolic process
GO:0019391 - glucuronoside catabolic process
Note(s): Note(s): ...[more].
Reference(s): [1] Ahmad S., et al., 2012
[2] Borisenkov MF., et al., 2011
[3] Briciu-Burghina C., et al., 2015
[4] Deckert K., et al., 2012
[5] Khan KM., et al., 2014
[6] Kong R., et al., 2014
[7] LoGuidice A., et al., 2012
[8] Man S., et al., 2011
[9] Novel M., et al., 1974
[10] Novel M., et al., 1976
[11] Novel M., et al., 1976
[12] Rasmussen TS., et al., 2011
[13] Wilkinson SM., et al., 2011
External database links:  
CAZY:
GH2
DIP:
DIP-11086N
ECOCYC:
BETA-GLUCURONID-MONOMER
ECOLIWIKI:
b1617
INTERPRO:
IPR013783
INTERPRO:
IPR017853
INTERPRO:
IPR023230
INTERPRO:
IPR023232
INTERPRO:
IPR008979
INTERPRO:
IPR036156
INTERPRO:
IPR006101
INTERPRO:
IPR006102
INTERPRO:
IPR006103
INTERPRO:
IPR006104
MODBASE:
P05804
PDB:
5CZK
PDB:
4JHZ
PDB:
3LPG
PDB:
3LPF
PDB:
3K4D
PDB:
3K4A
PDB:
3K46
PFAM:
PF02836
PFAM:
PF02837
PFAM:
PF00703
PRIDE:
P05804
PRINTS:
PR00132
PROSITE:
PS00608
PROSITE:
PS00719
PROTEINMODELPORTAL:
P05804
REFSEQ:
NP_416134
SMR:
P05804
UNIPROT:
P05804


Operon      
Name: uidABC         
Operon arrangement:
Transcription unit        Promoter
uidABC


Transcriptional Regulation      
Display Regulation             
Activated by: CRP
Repressed by: UidR, UxuR


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 uidCp5 1692988 reverse Similarity to the consensus
Read more >
[ICWHO] [14]
  promoter uidCp6 1693006 reverse Similarity to the consensus
Read more >
[ICWHO] [14]


Evidence    

 [ICWHO] Inferred computationally without human oversight



Reference(s)    

 [1] Ahmad S., Hughes MA., Yeh LA., Scott JE., 2012, Potential repurposing of known drugs as potent bacterial β-glucuronidase inhibitors., J Biomol Screen 17(7):957-65

 [2] Borisenkov MF., Bakutova LA., Latkin DS., Golovchenko VV., Vityazev FV., 2011, Interaction of microbial β-glucuronidase with vegetable pectins., J Agric Food Chem 59(18):9922-6

 [3] Briciu-Burghina C., Heery B., Regan F., 2015, Continuous fluorometric method for measuring β-glucuronidase activity: comparative analysis of three fluorogenic substrates., Analyst 140(17):5953-64

 [4] Deckert K., Budiardjo SJ., Brunner LC., Lovell S., Karanicolas J., 2012, Designing allosteric control into enzymes by chemical rescue of structure., J Am Chem Soc 134(24):10055-60

 [5] Khan KM., Fakhri MI., Shaikh NN., Saad SM., Hussain S., Perveen S., Choudhary MI., 2014, β-glucuronidase inhibitory studies on coumarin derivatives., Med Chem 10(8):778-82

 [6] Kong R., Liu T., Zhu X., Ahmad S., Williams AL., Phan AT., Zhao H., Scott JE., Yeh LA., Wong ST., 2014, Old drug new use--amoxapine and its metabolites as potent bacterial β-glucuronidase inhibitors for alleviating cancer drug toxicity., Clin Cancer Res 20(13):3521-30

 [7] LoGuidice A., Wallace BD., Bendel L., Redinbo MR., Boelsterli UA., 2012, Pharmacologic targeting of bacterial β-glucuronidase alleviates nonsteroidal anti-inflammatory drug-induced enteropathy in mice., J Pharmacol Exp Ther 341(2):447-54

 [8] Man S., Cheng R., Miao C., Gong Q., Gu Y., Lu X., Han F., Yu W., 2011, Artificial trans-encoded small non-coding RNAs specifically silence the selected gene expression in bacteria., Nucleic Acids Res 39(8):e50

 [9] Novel M., Novel G., 1974, [Escherichia coli K 12 mutants, able to grow on methyl-beta-galacturonide: simple constitutive mutants for the synthesis of beta-glucuronidase and double mutants also derepressed for the synthesis of 2 enzymes for glucuronate utilization]., C R Acad Sci Hebd Seances Acad Sci D 279(8):695-8

 [10] Novel M., Novel G., 1976, Regulation of beta-glucuronidase synthesis in Escherichia coli K-12: constitutive mutants specifically derepressed for uidA expression., J Bacteriol 127(1):406-17

 [11] Novel M., Novel G., 1976, Regulation of beta-glucuronidase synthesis in Escherichia coli K-12: pleiotropic constitutive mutations affecting uxu and uidA expression., J Bacteriol 127(1):418-32

 [12] Rasmussen TS., Koldso H., Nakagawa S., Kato A., Schiott B., Jensen HH., 2011, Synthesis of uronic-noeurostegine--a potent bacterial β-glucuronidase inhibitor., Org Biomol Chem 9(22):7807-13

 [13] Wilkinson SM., Watson MA., Willis AC., McLeod MD., 2011, Experimental and kinetic studies of the Escherichia coli glucuronylsynthase: an engineered enzyme for the synthesis of glucuronide conjugates., J Org Chem 76(7):1992-2000

 [14] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78


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