RegulonDB RegulonDB 10.10: Gene Form
   

acnB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

acnB yacH yacL Fis CRP ArcA ArcA Fis ArcA ArcA ArcA ArcA ArcA Fis terminator anti-terminator anti-anti-terminator terminator anti-terminator anti-anti-terminator yacLp yacLp TSS_259 TSS_259 TSS_258 TSS_258 TSS_257 TSS_257 TSS_256 TSS_256 TSS_255 TSS_255 acnBp2 acnBp2 acnBp acnBp yacHp5 yacHp5 yacHp3 yacHp3 TSS_254 TSS_254

Gene      
Name: acnB    Texpresso search in the literature
Synonym(s): ECK0117, EG12316, b0118, yacI, yacJ
Genome position(nucleotides): 131615 --> 134212 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 55.89
External database links:  
ASAP:
 ABE-0000411
CGSC:
 36955
ECHOBASE:
 EB2222
ECOLIHUB:
 acnB
OU-MICROARRAY:
 b0118
STRING:
 511145.b0118
COLOMBOS: acnB


Product      
Name: AcnB
Synonym(s): YacI, YacJ
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 93.498
Isoelectric point: 5.041
Motif(s):
 
Type Positions Sequence
769 -> 769 C
4 -> 156 EYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPLLTPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWF
168 -> 382 VTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGIEPDQPGVVGPIKQIEALQQKGFPLAYVGDVVGTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESDRGF
244 -> 246 SSR
414 -> 416 QDT

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.1 - carbon utilization --> 1.1.1 - carbon compounds
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.4 - TCA cycle
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
molecular_function GO:0047780 - citrate dehydratase activity
GO:0005515 - protein binding
GO:0016829 - lyase activity
GO:0046872 - metal ion binding
GO:0003723 - RNA binding
GO:0003729 - mRNA binding
GO:0051536 - iron-sulfur cluster binding
GO:0051539 - 4 iron, 4 sulfur cluster binding
GO:0003994 - aconitate hydratase activity
GO:0047456 - 2-methylisocitrate dehydratase activity
GO:0003730 - mRNA 3'-UTR binding
biological_process GO:0006097 - glyoxylate cycle
GO:0006099 - tricarboxylic acid cycle
GO:0006417 - regulation of translation
GO:0019629 - propionate catabolic process, 2-methylcitrate cycle
Note(s): Note(s): ...[more].
Reference(s): [1] Calderon IL., et al., 2009
[2] Kim CW., et al., 2007
[3] Maciag M., et al., 2012
[4] Stefanopoulou M., et al., 2011
External database links:  
DIP:
 DIP-9044N
ECOCYC:
 ACONITATEDEHYDRB-MONOMER
ECOLIWIKI:
 b0118
INTERPRO:
 IPR036008
INTERPRO:
 IPR036288
INTERPRO:
 IPR018136
INTERPRO:
 IPR015933
INTERPRO:
 IPR015932
INTERPRO:
 IPR015931
INTERPRO:
 IPR015929
INTERPRO:
 IPR015928
INTERPRO:
 IPR004406
INTERPRO:
 IPR001030
MODBASE:
 P36683
PANTHER:
 PTHR43160:SF1
PDB:
 1L5J
PFAM:
 PF06434
PFAM:
 PF00330
PFAM:
 PF11791
PRIDE:
 P36683
PRODB:
 PRO_000022043
PROSITE:
 PS01244
PROSITE:
 PS00450
REFSEQ:
 NP_414660
SMR:
 P36683
UNIPROT:
 P36683


Operon      
Name: acnB         
Operon arrangement:
Transcription unit        Promoter
acnB
acnB


Transcriptional Regulation      
Display Regulation             
Activated by: CRP
Repressed by: Cra, ArcA, Fis


RNA cis-regulatory element    
Attenuation: Transcriptional


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_254 130229 forward nd [RS-EPT-CBR] [5]
  promoter yacHp3 131307 reverse nd [ICWHO] [6]
  promoter yacHp5 131466 reverse nd [ICWHO] [6]
  promoter TSS_255 131743 forward nd [RS-EPT-CBR] [5]
  promoter TSS_256 132124 forward nd [RS-EPT-CBR] [5]
  promoter TSS_257 132840 forward nd [RS-EPT-CBR] [5]
  promoter TSS_258 133449 forward nd [RS-EPT-CBR] [5]
  promoter TSS_259 133468 forward nd [RS-EPT-CBR] [5]


Evidence    

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

 [ICWHO] Inferred computationally without human oversight


Reference(s)    

 [1] Calderon IL., Elias AO., Fuentes EL., Pradenas GA., Castro ME., Arenas FA., Perez JM., Vasquez CC., 2009, Tellurite-mediated disabling of [4Fe-4S] clusters of Escherichia coli dehydratases., Microbiology 155(Pt 6):1840-6

 [2] Kim CW., Han KS., Ryu KS., Kim BH., Kim KH., Choi SI., Seong BL., 2007, N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers., Protein Sci 16(4):635-43

 [3] Maciag M., Nowicki D., Szalewska-Palasz A., Wegrzyn G., 2012, Central carbon metabolism influences fidelity of DNA replication in Escherichia coli., Mutat Res 731(1-2):99-106

 [4] Stefanopoulou M., Kokoschka M., Sheldrick WS., Wolters DA., 2011, Cell response of Escherichia coli to cisplatin-induced stress., Proteomics 11(21):4174-88

 [5] 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.

 [6] 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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