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Protein

Respiratory nitrate reductase 1 beta chain

Gene

narH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi16Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi19Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi22Iron-sulfur 1 (4Fe-4S)2 Publications1
Metal bindingi26Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi184Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi187Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi192Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi196Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi217Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi223Iron-sulfur 4 (3Fe-4S)2 Publications1
Metal bindingi227Iron-sulfur 3 (4Fe-4S)2 Publications1
Metal bindingi244Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi247Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi259Iron-sulfur 2 (4Fe-4S)2 Publications1
Metal bindingi263Iron-sulfur 1 (4Fe-4S)2 Publications1

GO - Molecular functioni

  • 3 iron, 4 sulfur cluster binding Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron carrier activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • nitrate reductase activity Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • nitrate assimilation Source: UniProtKB-KW
  • nitrate metabolic process Source: EcoCyc
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.
BRENDAi1.7.5.1. 2026.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10639. narH.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • intrinsic component of membrane Source: EcoCyc
  • intrinsic component of the cytoplasmic side of the plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
  • NarGHI complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000967201 – 512Respiratory nitrate reductase 1 beta chainAdd BLAST512

Proteomic databases

PaxDbiP11349.
PRIDEiP11349.

Expressioni

Inductioni

By nitrate.

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.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4262231. 20 interactors.
DIPiDIP-10312N.
IntActiP11349. 13 interactors.
MINTiMINT-1260007.
STRINGi511145.b1225.

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 12Combined sources10
Turni13 – 15Combined sources3
Helixi21 – 30Combined sources10
Beta strandi41 – 49Combined sources9
Turni51 – 57Combined sources7
Helixi59 – 62Combined sources4
Beta strandi65 – 68Combined sources4
Beta strandi74 – 76Combined sources3
Helixi81 – 85Combined sources5
Turni86 – 89Combined sources4
Helixi97 – 100Combined sources4
Beta strandi104 – 106Combined sources3
Helixi109 – 113Combined sources5
Beta strandi126 – 128Combined sources3
Turni129 – 131Combined sources3
Turni142 – 148Combined sources7
Helixi152 – 155Combined sources4
Helixi159 – 161Combined sources3
Helixi167 – 170Combined sources4
Helixi172 – 174Combined sources3
Beta strandi178 – 182Combined sources5
Helixi191 – 194Combined sources4
Beta strandi201 – 204Combined sources4
Turni205 – 207Combined sources3
Beta strandi210 – 212Combined sources3
Turni214 – 216Combined sources3
Helixi223 – 226Combined sources4
Beta strandi232 – 235Combined sources4
Turni236 – 239Combined sources4
Beta strandi240 – 243Combined sources4
Helixi248 – 251Combined sources4
Turni252 – 254Combined sources3
Helixi258 – 261Combined sources4
Beta strandi268 – 276Combined sources9
Helixi277 – 279Combined sources3
Helixi280 – 284Combined sources5
Helixi289 – 291Combined sources3
Helixi292 – 297Combined sources6
Helixi306 – 314Combined sources9
Helixi319 – 325Combined sources7
Helixi329 – 334Combined sources6
Beta strandi341 – 343Combined sources3
Helixi345 – 347Combined sources3
Beta strandi352 – 356Combined sources5
Beta strandi366 – 368Combined sources3
Helixi380 – 382Combined sources3
Beta strandi383 – 385Combined sources3
Helixi387 – 394Combined sources8
Helixi399 – 420Combined sources22
Helixi428 – 432Combined sources5
Helixi437 – 447Combined sources11
Helixi452 – 455Combined sources4
Turni463 – 466Combined sources4
Helixi469 – 475Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11349.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 354Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST29
Domaini175 – 2064Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32
Domaini208 – 2374Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30

Sequence similaritiesi

Contains 3 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108IUE. Bacteria.
COG1140. LUCA.
HOGENOMiHOG000237353.
InParanoidiP11349.
KOiK00371.
OMAiQSPIYKM.
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

        10         20         30         40         50
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ
60 70 80 90 100
GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY
110 120 130 140 150
YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG
160 170 180 190 200
EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA
210 220 230 240 250
IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR
260 270 280 290 300
IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF
310 320 330 340 350
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL
360 370 380 390 400
PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK
410 420 430 440 450
PVLRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA
460 470 480 490 500
NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID
510
AIDVTSKTEP HP
Length:512
Mass (Da):58,066
Last modified:February 1, 1996 - v3
Checksum:i2E7719C8D078BAEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti398 – 417DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195 (PubMed:2832376).CuratedAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000702650.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74309; AAC74309; b1225.
BAA36095; BAA36095; BAA36095.
GeneIDi945780.
KEGGiecj:JW1216.
eco:b1225.
PATRICi32117710. VBIEscCol129921_1277.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000702650.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262231. 20 interactors.
DIPiDIP-10312N.
IntActiP11349. 13 interactors.
MINTiMINT-1260007.
STRINGi511145.b1225.

Protein family/group databases

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

Proteomic databases

PaxDbiP11349.
PRIDEiP11349.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74309; AAC74309; b1225.
BAA36095; BAA36095; BAA36095.
GeneIDi945780.
KEGGiecj:JW1216.
eco:b1225.
PATRICi32117710. VBIEscCol129921_1277.

Organism-specific databases

EchoBASEiEB0633.
EcoGeneiEG10639. narH.

Phylogenomic databases

eggNOGiENOG4108IUE. Bacteria.
COG1140. LUCA.
HOGENOMiHOG000237353.
InParanoidiP11349.
KOiK00371.
OMAiQSPIYKM.
PhylomeDBiP11349.

Enzyme and pathway databases

BioCyciEcoCyc:NARH-MONOMER.
ECOL316407:JW1216-MONOMER.
MetaCyc:NARH-MONOMER.
BRENDAi1.7.5.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP11349.
PROiP11349.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.