RegulonDB RegulonDB 11.2: Gene Form
   

narH gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

narG narH narJ narI narS narK FNR NarL Fis NarL NarL NarL NarL Fis IHF NarL NarL NarL RstA TSS_1555 TSS_1555 narGp narGp

Gene      
Name: narH    Texpresso search in the literature
Synonym(s): ECK1219, EG10639, b1225, chlC
Genome position(nucleotides): 1283604 --> 1285142
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 53.74
External database links:  
ASAP:
 ABE-0004121
CGSC:
 18118
ECHOBASE:
 EB0633
ECOLIHUB:
 narH
OU-MICROARRAY:
 b1225
STRING:
 511145.b1225
COLOMBOS: narH


Product      
Name: nitrate reductase A subunit β
Synonym(s): ChlC, NarH
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 58.066
Isoelectric point: 6.751
Motif(s):
 
Type Positions Sequence Comment
7 -> 35 VGMVLNLDKCIGCHTCSVTCKNVWTSREG UniProt: 4Fe-4S ferredoxin-type 1.
175 -> 206 TFMMYLPRLCEHCLNPACVATCPSGAIYKREE UniProt: 4Fe-4S ferredoxin-type 2.
176 -> 272 FMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGV
208 -> 237 GIVLIDQDKCRGWRMCITGCPYKKIYFNWK UniProt: 4Fe-4S ferredoxin-type 3.
359 -> 437 LSPIQSAADAGELGSNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTE

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.7 - anaerobic respiration
  1 - metabolism --> 1.4 - energy production/transport --> 1.4.2 - electron acceptors
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0031224 - intrinsic component of membrane
GO:0031235 - intrinsic component of the cytoplasmic side of the plasma membrane
GO:0009325 - nitrate reductase complex
GO:0044799 - NarGHI complex
molecular_function GO:0005515 - protein binding
GO:0009055 - electron transfer activity
GO:0046872 - metal ion binding
GO:0016491 - oxidoreductase activity
GO:0051536 - iron-sulfur cluster binding
GO:0051539 - 4 iron, 4 sulfur cluster binding
GO:0008940 - nitrate reductase activity
GO:0051538 - 3 iron, 4 sulfur cluster binding
biological_process GO:0009061 - anaerobic respiration
GO:0019645 - anaerobic electron transport chain
GO:0042126 - nitrate metabolic process
GO:0042128 - nitrate assimilation
Note(s): Note(s): ...[more].
Reference(s): [1] Augier V., et al., 1993
[2] Augier V., et al., 1993
[3] Guigliarelli B., et al., 1992
[4] Guigliarelli B., et al., 1996
External database links:  
ALPHAFOLD:
 P11349
DIP:
 DIP-10312N
ECOCYC:
 NARH-MONOMER
ECOLIWIKI:
 b1225
INTERPRO:
 IPR006547
INTERPRO:
 IPR029263
INTERPRO:
 IPR038262
INTERPRO:
 IPR017896
MODBASE:
 P11349
PDB:
 3IR7
PDB:
 3IR6
PDB:
 3IR5
PDB:
 3EGW
PDB:
 1Y5N
PDB:
 1Y5L
PDB:
 1Y5I
PDB:
 1Y4Z
PDB:
 1SIW
PDB:
 1Q16
PDB:
 1R27
PFAM:
 PF14711
PFAM:
 PF13247
PRIDE:
 P11349
PRODB:
 PRO_000023352
PROSITE:
 PS51379
REFSEQ:
 NP_415743
SMR:
 P11349
UNIPROT:
 P11349


Operon      
Name: narGHJI         
Operon arrangement:
Transcription unit        Promoter
narGHJI


Transcriptional Regulation      
Display Regulation             
Activated by: FNR, IHF, RstA, NarL
Repressed by: Fis


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_1555 1280972 forward nd [RS-EPT-CBR] [5]


Evidence    

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


Reference(s)    

 [1] Augier V., Asso M., Guigliarelli B., More C., Bertrand P., Santini CL., Blasco F., Chippaux M., Giordano G., 1993, Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes., Biochemistry 32(19):5099-108

 [2] Augier V., Guigliarelli B., Asso M., Bertrand P., Frixon C., Giordano G., Chippaux M., Blasco F., 1993, Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes., Biochemistry 32(8):2013-23

 [3] Guigliarelli B., Asso M., More C., Augier V., Blasco F., Pommier J., Giordano G., Bertrand P., 1992, EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism., Eur J Biochem 207(1):61-8

 [4] Guigliarelli B., Magalon A., Asso M., Bertrand P., Frixon C., Giordano G., Blasco F., 1996, Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters., Biochemistry 35(15):4828-36

 [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.

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