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P11349

- NARH_ECOLI

UniProt

P11349 - NARH_ECOLI

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Protein
Respiratory nitrate reductase 1 beta chain
Gene
narH, b1225, JW1216
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactori

Binds 3 4Fe-4S clusters per subunit.
Binds 1 3Fe-4S cluster per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161Iron-sulfur 1 (4Fe-4S)
Metal bindingi19 – 191Iron-sulfur 1 (4Fe-4S)
Metal bindingi22 – 221Iron-sulfur 1 (4Fe-4S)
Metal bindingi26 – 261Iron-sulfur 2 (4Fe-4S)
Metal bindingi184 – 1841Iron-sulfur 3 (4Fe-4S)
Metal bindingi187 – 1871Iron-sulfur 3 (4Fe-4S)
Metal bindingi192 – 1921Iron-sulfur 3 (4Fe-4S)
Metal bindingi196 – 1961Iron-sulfur 4 (3Fe-4S)
Metal bindingi217 – 2171Iron-sulfur 4 (3Fe-4S)
Metal bindingi223 – 2231Iron-sulfur 4 (3Fe-4S)
Metal bindingi227 – 2271Iron-sulfur 3 (4Fe-4S)
Metal bindingi244 – 2441Iron-sulfur 2 (4Fe-4S)
Metal bindingi247 – 2471Iron-sulfur 2 (4Fe-4S)
Metal bindingi259 – 2591Iron-sulfur 2 (4Fe-4S)
Metal bindingi263 – 2631Iron-sulfur 1 (4Fe-4S)

GO - Molecular functioni

  1. 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. nitrate reductase activity Source: UniProtKB-EC
  5. protein binding Source: IntAct

GO - Biological processi

  1. anaerobic respiration Source: EcoCyc
  2. cytochrome complex assembly Source: EcoCyc
  3. nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Nitrate assimilation, Transport

Keywords - Ligandi

3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:NARH-MONOMER.
ECOL316407:JW1216-MONOMER.
MetaCyc:NARH-MONOMER.

Protein family/group databases

TCDBi5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase 1 beta chain (EC:1.7.99.4)
Alternative name(s):
Nitrate reductase A subunit beta
Quinol-nitrate oxidoreductase subunit beta
Gene namesi
Name:narH
Ordered Locus Names:b1225, JW1216
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10639. narH.

Subcellular locationi

GO - Cellular componenti

  1. intrinsic component of membrane Source: EcoCyc
  2. membrane Source: UniProtKB
  3. nitrate reductase complex Source: InterPro
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Respiratory nitrate reductase 1 beta chain
PRO_0000096720Add
BLAST

Proteomic databases

PaxDbiP11349.
PRIDEiP11349.

Expressioni

Inductioni

By nitrate.

Gene expression databases

GenevestigatoriP11349.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
narGP0915211EBI-555067,EBI-547248
narZP193194EBI-555067,EBI-547262

Protein-protein interaction databases

DIPiDIP-10312N.
IntActiP11349. 13 interactions.
MINTiMINT-1260007.
STRINGi511145.b1225.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210
Turni13 – 153
Helixi21 – 3010
Beta strandi41 – 499
Turni51 – 577
Helixi59 – 624
Beta strandi65 – 684
Beta strandi74 – 763
Helixi81 – 855
Turni86 – 894
Helixi97 – 1004
Beta strandi104 – 1063
Helixi109 – 1135
Beta strandi126 – 1283
Turni129 – 1313
Turni142 – 1487
Helixi152 – 1554
Helixi159 – 1613
Helixi167 – 1704
Helixi172 – 1743
Beta strandi178 – 1825
Helixi191 – 1944
Beta strandi201 – 2044
Turni205 – 2073
Beta strandi210 – 2123
Turni214 – 2163
Helixi223 – 2264
Beta strandi232 – 2354
Turni236 – 2394
Beta strandi240 – 2434
Helixi248 – 2514
Turni252 – 2543
Helixi258 – 2614
Beta strandi268 – 2769
Helixi277 – 2793
Helixi280 – 2845
Helixi289 – 2913
Helixi292 – 2976
Helixi306 – 3149
Helixi319 – 3257
Helixi329 – 3346
Beta strandi341 – 3433
Helixi345 – 3473
Beta strandi352 – 3565
Beta strandi366 – 3683
Helixi380 – 3823
Beta strandi383 – 3853
Helixi387 – 3948
Helixi399 – 42022
Helixi428 – 4325
Helixi437 – 44711
Helixi452 – 4554
Turni463 – 4664
Helixi469 – 4757

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q16X-ray1.90B1-512[»]
1R27X-ray2.00B/D1-512[»]
1SIWX-ray2.20B1-512[»]
1Y4ZX-ray2.00B1-512[»]
1Y5IX-ray1.90B1-512[»]
1Y5LX-ray2.50B1-512[»]
1Y5NX-ray2.50B1-512[»]
3EGWX-ray1.90B1-509[»]
3IR5X-ray2.30B1-512[»]
3IR6X-ray2.80B1-512[»]
3IR7X-ray2.50B1-512[»]
ProteinModelPortaliP11349.
SMRiP11349. Positions 1-509.

Miscellaneous databases

EvolutionaryTraceiP11349.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 35294Fe-4S ferredoxin-type 1
Add
BLAST
Domaini175 – 206324Fe-4S ferredoxin-type 2
Add
BLAST
Domaini208 – 237304Fe-4S ferredoxin-type 3
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1140.
HOGENOMiHOG000237353.
KOiK00371.
OMAiPHAWEDQ.
OrthoDBiEOG6X3W4C.
PhylomeDBiP11349.

Family and domain databases

Gene3Di1.10.3650.10. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR029263. Nitr_red_bet_C.
IPR006547. NO3_Rdtase_bsu.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF14711. Nitr_red_bet_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01660. narH. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11349-1 [UniParc]FASTAAdd to Basket

« Hide

MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ    50
GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY 100
YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG 150
EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA 200
IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR 250
IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF 300
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL 350
PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK 400
PVLRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA 450
NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID 500
AIDVTSKTEP HP 512
Length:512
Mass (Da):58,066
Last modified:February 1, 1996 - v3
Checksum:i2E7719C8D078BAEA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti398 – 41720DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20147 Genomic DNA. Translation: AAA24195.1.
U00096 Genomic DNA. Translation: AAC74309.1.
AP009048 Genomic DNA. Translation: BAA36095.1.
X16181 Genomic DNA. Translation: CAA34304.1.
PIRiF64869. RDECNB.
RefSeqiNP_415743.1. NC_000913.3.
YP_489495.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74309; AAC74309; b1225.
BAA36095; BAA36095; BAA36095.
GeneIDi12933237.
945780.
KEGGiecj:Y75_p1200.
eco:b1225.
PATRICi32117710. VBIEscCol129921_1277.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M20147 Genomic DNA. Translation: AAA24195.1 .
U00096 Genomic DNA. Translation: AAC74309.1 .
AP009048 Genomic DNA. Translation: BAA36095.1 .
X16181 Genomic DNA. Translation: CAA34304.1 .
PIRi F64869. RDECNB.
RefSeqi NP_415743.1. NC_000913.3.
YP_489495.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q16 X-ray 1.90 B 1-512 [» ]
1R27 X-ray 2.00 B/D 1-512 [» ]
1SIW X-ray 2.20 B 1-512 [» ]
1Y4Z X-ray 2.00 B 1-512 [» ]
1Y5I X-ray 1.90 B 1-512 [» ]
1Y5L X-ray 2.50 B 1-512 [» ]
1Y5N X-ray 2.50 B 1-512 [» ]
3EGW X-ray 1.90 B 1-509 [» ]
3IR5 X-ray 2.30 B 1-512 [» ]
3IR6 X-ray 2.80 B 1-512 [» ]
3IR7 X-ray 2.50 B 1-512 [» ]
ProteinModelPortali P11349.
SMRi P11349. Positions 1-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10312N.
IntActi P11349. 13 interactions.
MINTi MINT-1260007.
STRINGi 511145.b1225.

Protein family/group databases

TCDBi 5.A.3.1.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbi P11349.
PRIDEi P11349.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74309 ; AAC74309 ; b1225 .
BAA36095 ; BAA36095 ; BAA36095 .
GeneIDi 12933237.
945780.
KEGGi ecj:Y75_p1200.
eco:b1225.
PATRICi 32117710. VBIEscCol129921_1277.

Organism-specific databases

EchoBASEi EB0633.
EcoGenei EG10639. narH.

Phylogenomic databases

eggNOGi COG1140.
HOGENOMi HOG000237353.
KOi K00371.
OMAi PHAWEDQ.
OrthoDBi EOG6X3W4C.
PhylomeDBi P11349.

Enzyme and pathway databases

BioCyci EcoCyc:NARH-MONOMER.
ECOL316407:JW1216-MONOMER.
MetaCyc:NARH-MONOMER.

Miscellaneous databases

EvolutionaryTracei P11349.
PROi P11349.

Gene expression databases

Genevestigatori P11349.

Family and domain databases

Gene3Di 1.10.3650.10. 1 hit.
InterProi IPR017896. 4Fe4S_Fe-S-bd.
IPR029263. Nitr_red_bet_C.
IPR006547. NO3_Rdtase_bsu.
[Graphical view ]
Pfami PF13247. Fer4_11. 1 hit.
PF14711. Nitr_red_bet_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01660. narH. 1 hit.
PROSITEi PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Blasco F.
    Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 398-417.
    Strain: K12 / TG1.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes."
    Sodergren E.J., Demoss J.A.
    J. Bacteriol. 170:1721-1729(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-512.
  7. "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 1-10.
  8. "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., Asso M., More C., Augier V., Blasco F., Pommier J., Giordano G., Bertrand P.
    Eur. J. Biochem. 207:61-68(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
  9. "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., Guigliarelli B., Asso M., Bertrand P., Frixon C., Giordano G., Chippaux M., Blasco F.
    Biochemistry 32:2013-2023(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYSTEINE RESIDUES, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
  10. "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., Asso M., Guigliarelli B., More C., Bertrand P., Santini C.-L., Blasco F., Chippaux M., Giordano G.
    Biochemistry 32:5099-5108(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYSTEINE RESIDUES, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
  11. "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., Magalon A., Asso M., Bertrand P., Frixon C., Giordano G., Blasco F.
    Biochemistry 35:4828-4836(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYSTEINE RESIDUES, EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
  12. "The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters."
    Rothery R.A., Magalon A., Giordano G., Guigliarelli B., Blasco F., Weiner J.H.
    J. Biol. Chem. 273:7462-7469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: EPR SPECTROSCOPY, REDOX POTENTIOMETRY OF IRON-SULFUR CLUSTERS.
  13. "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).
  14. "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 43-512.

Entry informationi

Entry nameiNARH_ECOLI
AccessioniPrimary (citable) accession number: P11349
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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