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P09152 (NARG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Respiratory nitrate reductase 1 alpha chain

EC=1.7.99.4
Alternative name(s):
Nitrate reductase A subunit alpha
Quinol-nitrate oxidoreductase subunit alpha
Gene names
Name:narG
Synonyms:bisD, narC
Ordered Locus Names:b1224, JW1215
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Catalytic activity

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactor

Binds 1 4Fe-4S cluster per subunit.

Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.

Subunit structure

Dimer of heterotrimers each composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane. Interacts with the NarJ chaperone. Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Cell membrane; Peripheral membrane protein.

Induction

By nitrate.

Domain

Apoenzyme contains at least 2 NarJ-binding sites, one interfering with membrane anchoring and another being involved in molybdenum insertion. The first binding-site is a short peptide sequence near the N-terminus that contains a twin-arginine homologous motif. Ref.14 Ref.15

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 12471246Respiratory nitrate reductase 1 alpha chain
PRO_0000063233

Regions

Domain43 – 107654Fe-4S Mo/W bis-MGD-type

Sites

Metal binding501Iron-sulfur (4Fe-4S); via pros nitrogen
Metal binding541Iron-sulfur (4Fe-4S)
Metal binding581Iron-sulfur (4Fe-4S)
Metal binding931Iron-sulfur (4Fe-4S)
Metal binding2231Molybdenum

Experimental info

Mutagenesis501H → S: Loss of activity. Ref.12
Sequence conflict101Y → K AA sequence Ref.11

Secondary structure

......................................................................................................................................................................................................................................................... 1247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09152 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 640ABAD5FF01DF25

FASTA1,247140,489
        10         20         30         40         50         60 
MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW 

        70         80         90        100        110        120 
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPMMRKRLMK 

       130        140        150        160        170        180 
MWREAKALHS DPVEAWASII EDADKAKSFK QARGRGGFVR SSWQEVNELI AASNVYTIKN 

       190        200        210        220        230        240 
YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE 

       250        260        270        280        290        300 
SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ 

       310        320        330        340        350        360 
GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY AAGRMLRAAD 

       370        380        390        400        410        420 
LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK WNLEQRDGKT GEETELQLSL 

       430        440        450        460        470        480 
LGSQDEIAEV GFPYFGGDGT EHFNKVELEN VLLHKLPVKR LQLADGSTAL VTTVYDLTLA 

       490        500        510        520        530        540 
NYGLERGLND VNCATSYDDV KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII 

       550        560        570        580        590        600 
VGAGLNHWYH LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ 

       610        620        630        640        650        660 
RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA ERMGWLPSAP 

       670        680        690        700        710        720 
QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP ENGKNHPRNL FIWRSNLLGS 

       730        740        750        760        770        780 
SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC 

       790        800        810        820        830        840 
LYSDIILPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG 

       850        860        870        880        890        900 
HLGKETDIVT LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF 

       910        920        930        940        950        960 
TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI DAAEMILTLA 

       970        980        990       1000       1010       1020 
PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI QAQPRKIISS PTWSGLEDEH 

      1030       1040       1050       1060       1070       1080 
VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ WMRDFGESLL VYRPPIDTRS VKEVIGQKSN 

      1090       1100       1110       1120       1130       1140 
GNQEKALNFL TPHQKWGIHS TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN 

      1150       1160       1170       1180       1190       1200 
SNGALTARAV VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG 

      1210       1220       1230       1240 
GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK 

« Hide

References

« Hide 'large scale' references
[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., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.
Mol. Gen. Genet. 218:249-256(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / TG1.
[2]"Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon."
Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.
Mol. Gen. Genet. 222:104-111(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / TG1.
[3]Blasco F.
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
Strain: K12 / TG1.
[4]"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., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene."
McPherson M.J., Baron A.J., Pappin D.J.C., Wootton J.C.
FEBS Lett. 177:260-264(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
Strain: K12.
[8]"Delineation of two distinct regulatory domains in the 5' region of the nar operon of Escherichia coli."
Li S.F., Rabi T., Demoss J.A.
J. Bacteriol. 164:25-32(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
Strain: PK27.
[9]"The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells."
Noji S., Nohno T., Saito T., Taniguchi S.
FEBS Lett. 252:139-143(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
Strain: K12.
[10]"Promoter region of the nar operon of Escherichia coli: nucleotide sequence and transcription initiation signals."
Li S.F., Demoss J.A.
J. Bacteriol. 169:4614-4620(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[11]"Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli."
Sodergren E.J., Hsu P.Y., Demoss J.A.
J. Biol. Chem. 263:16156-16162(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
[12]"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., Asso M., Guigliarelli B., Rothery R.A., Bertrand P., Giordano G., Blasco F.
Biochemistry 37:7363-7370(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-50, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
[13]"NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli."
Blasco F., Dos Santos J.P., Magalon A., Frixon C., Guigliarelli B., Santini C.L., Giordano G.
Mol. Microbiol. 28:435-447(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NARJ.
[14]"Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli."
Chan C.S., Howell J.M., Workentine M.L., Turner R.J.
Biochem. Biophys. Res. Commun. 343:244-251(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NARJ, DOMAIN.
[15]"NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly."
Vergnes A., Pommier J., Toci R., Blasco F., Giordano G., Magalon A.
J. Biol. Chem. 281:2170-2176(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NARJ, DOMAIN.
Strain: K12 / MC4100 / JA176.
[16]"Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase."
Zakian S., Lafitte D., Vergnes A., Pimentel C., Sebban-Kreuzer C., Toci R., Claude J.B., Guerlesquin F., Magalon A.
FEBS J. 277:1886-1895(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NARJ.
[17]"Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A."
Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J.
Nat. Struct. Biol. 10:681-687(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[18]"Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes."
Jormakka M., Richardson D., Byrne B., Iwata S.
Structure 12:95-104(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-1247.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16181 Genomic DNA. Translation: CAA34303.1.
X01164 Genomic DNA. Translation: CAA25611.1.
M11586 Genomic DNA. Translation: AAA24201.1.
U00096 Genomic DNA. Translation: AAC74308.1.
AP009048 Genomic DNA. Translation: BAA36094.1.
X15996 Genomic DNA. Translation: CAA34127.1.
L36649 Genomic DNA. Translation: AAA64296.1.
PIRRDECNA. E64869.
RefSeqNP_415742.1. NC_000913.3.
YP_489494.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90A1-1247[»]
1R27X-ray2.00A/C2-1247[»]
1SIWX-ray2.20A2-1246[»]
1Y4ZX-ray2.00A2-1246[»]
1Y5IX-ray1.90A2-1246[»]
1Y5LX-ray2.50A2-1246[»]
1Y5NX-ray2.50A2-1246[»]
3EGWX-ray1.90A2-1245[»]
3IR5X-ray2.30A1-1247[»]
3IR6X-ray2.80A1-1247[»]
3IR7X-ray2.50A1-1247[»]
ProteinModelPortalP09152.
SMRP09152. Positions 2-1245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10311N.
IntActP09152. 22 interactions.
MINTMINT-1233973.
STRING511145.b1224.

Protein family/group databases

TCDB5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbP09152.
PRIDEP09152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74308; AAC74308; b1224.
BAA36094; BAA36094; BAA36094.
GeneID12934277.
945782.
KEGGecj:Y75_p1199.
eco:b1224.
PATRIC32117708. VBIEscCol129921_1276.

Organism-specific databases

EchoBASEEB0632.
EcoGeneEG10638. narG.

Phylogenomic databases

eggNOGCOG5013.
HOGENOMHOG000237341.
KOK00370.
OMADKPSQYF.
OrthoDBEOG6RC3JS.
PhylomeDBP09152.
ProtClustDBCLSK868288.

Enzyme and pathway databases

BioCycEcoCyc:NARG-MONOMER.
ECOL316407:JW1215-MONOMER.
MetaCyc:NARG-MONOMER.

Gene expression databases

GenevestigatorP09152.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006468. NarG.
IPR028189. Nitr_red_alph_N.
[Graphical view]
PfamPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
PF14710. Nitr_red_alph_N. 1 hit.
[Graphical view]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
TIGRFAMsTIGR01580. narG. 1 hit.
PROSITEPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09152.
PROP09152.

Entry information

Entry nameNARG_ECOLI
AccessionPrimary (citable) accession number: P09152
Secondary accession number(s): P78294
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene