TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


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:P09152
Protein Name:NarG aka NARC aka BISD aka B1224
Length:1247
Molecular Weight:140489.00
Species:Escherichia coli [83333]
Location1 / Topology2 / Orientation3: Cell membrane1 / Peripheral membrane protein2
Substrate Electrons

Cross database links:

Genevestigator: P09152
EchoBASE: EB0632
EcoGene: EG10638
eggNOG: COG5013
HEGENOM: HBG496975
DIP: DIP-10311N
RefSeq: AP_001852.1    NP_415742.1   
Entrez Gene ID: 945782   
Pfam: PF00384    PF01568   
Drugbank: Drugbank Link   
BioCyc: EcoCyc:NARG-MONOMER    ECOL168927:B1224-MONOMER    MetaCyc:NARG-MONOMER   
KEGG: ecj:JW1215    eco:b1224   

Gene Ontology

GO:0031224 C:intrinsic to membrane
GO:0009325 C:nitrate reductase complex
GO:0005886 C:plasma membrane
GO:0051539 F:4 iron, 4 sulfur cluster binding
GO:0009055 F:electron carrier activity
GO:0030151 F:molybdenum 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 (17)

[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] “Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon.”  Blasco F.et.al.   2233673
[3] “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
[4] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[5] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[6] “Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene.”  McPherson M.J.et.al.   6094247
[7] “Delineation of two distinct regulatory domains in the 5' region of the nar operon of Escherichia coli.”  Li S.F.et.al.   2995309
[8] “The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells.”  Noji S.et.al.   2668029
[9] “Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals.”  Li S.F.et.al.   3308846
[10] “Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli.”  Sodergren E.J.et.al.   3053688
[11] “Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit.”  Magalon A.et.al.   9585550
[12] “NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli.”  Blasco F.et.al.   9632249
[13] “Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli.”  Chan C.S.et.al.   16540088
[14] “NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly.”  Vergnes A.et.al.   16286471
[15] “Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase.”  Zakian S.et.al.   20236317
[16] “Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A.”  Bertero M.G.et.al.   12910261
[17] “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:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
1:	MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW 
61:	KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPMMRKRLMK 
121:	MWREAKALHS DPVEAWASII EDADKAKSFK QARGRGGFVR SSWQEVNELI AASNVYTIKN 
181:	YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE 
241:	SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ 
301:	GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY AAGRMLRAAD 
361:	LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK WNLEQRDGKT GEETELQLSL 
421:	LGSQDEIAEV GFPYFGGDGT EHFNKVELEN VLLHKLPVKR LQLADGSTAL VTTVYDLTLA 
481:	NYGLERGLND VNCATSYDDV KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII 
541:	VGAGLNHWYH LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ 
601:	RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA ERMGWLPSAP 
661:	QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP ENGKNHPRNL FIWRSNLLGS 
721:	SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC 
781:	LYSDIILPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG 
841:	HLGKETDIVT LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF 
901:	TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI DAAEMILTLA 
961:	PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI QAQPRKIISS PTWSGLEDEH 
1021:	VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ WMRDFGESLL VYRPPIDTRS VKEVIGQKSN 
1081:	GNQEKALNFL TPHQKWGIHS TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN 
1141:	SNGALTARAV VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG 
1201:	GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK