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5.A.3.1.1
Anaerobic, respiratory, membrane-bound nitrate reductase, NarGHI. Two protons are consumed in the cytoplasm while two protons are released in the periplasm, contributing to the pmf (Simon et al., 2008).

Accession Number:P11349
Protein Name:NarH aka B1225
Length:512
Molecular Weight:58066.00
Species:Escherichia coli [83333]
Location1 / Topology2 / Orientation3: Cell membrane1 / Peripheral membrane protein2
Substrate Electrons

Cross database links:

Genevestigator: P11349
EchoBASE: EB0633
EcoGene: EG10639
eggNOG: COG1140
HEGENOM: HBG461345
DIP: DIP-10312N
RefSeq: AP_001853.1    NP_415743.1   
Entrez Gene ID: 945780   
Drugbank: Drugbank Link   
BioCyc: EcoCyc:NARH-MONOMER    ECOL168927:B1225-MONOMER    MetaCyc:NARH-MONOMER   
KEGG: ecj:JW1216    eco:b1225   

Gene Ontology

GO:0031224 C:intrinsic to membrane
GO:0009325 C:nitrate reductase complex
GO:0005886 C:plasma membrane
GO:0051538 F:3 iron, 4 sulfur cluster binding
GO:0051539 F:4 iron, 4 sulfur cluster binding
GO:0009055 F:electron carrier activity
GO:0046872 F:metal ion binding
GO:0008940 F:nitrate reductase activity
GO:0005515 F:protein binding
GO:0009061 P:anaerobic respiration
GO:0017004 P:cytochrome complex assembly
GO:0022900 P:electron transport chain
GO:0042128 P:nitrate assimilation
GO:0006810 P:transport

References (13)

[1] “Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer.”  Blasco F.et.al.   2674654
[2] “A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.”  Oshima T.et.al.   8905232
[3] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[5] “narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes.”  Sodergren E.J.et.al.   2832376
[6] “Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli.”  Sodergren E.J.et.al.   3053688
[7] “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.”  Guigliarelli B.et.al.   1321049
[8] “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.”  Augier V.et.al.   8383531
[9] “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.”  Augier V.et.al.   8388253
[10] “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.”  Guigliarelli B.et.al.   8664273
[11] “The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters.”  Rothery R.A.et.al.   9516445
[12] “Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A.”  Bertero M.G.et.al.   12910261
[13] “Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes.”  Jormakka M.et.al.   14725769
Structure:
1Q16   1R27   1SIW   1Y4Z   1Y5I   1Y5L   1Y5N   3EGW   3IR5   3IR6   [...more]

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE 
61:	KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS 
121:	QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL 
181:	PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK 
241:	SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF 
301:	LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS 
361:	PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PVLRALKRML AMRHYKRAET 
421:	VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF 
481:	GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP