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Protein

Respiratory nitrate reductase 2 beta chain

Gene

narY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and 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:
  • [4Fe-4S] clusterBy similarityNote: Binds 3 [4Fe-4S] clusters per subunit.By similarity
  • [3Fe-4S] clusterBy similarityNote: Binds 1 [3Fe-4S] cluster per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi16Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi19Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi22Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi26Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi183Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi186Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi191Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi195Iron-sulfur 4 (3Fe-4S)By similarity1
Metal bindingi216Iron-sulfur 4 (3Fe-4S)By similarity1
Metal bindingi222Iron-sulfur 4 (3Fe-4S)By similarity1
Metal bindingi226Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi243Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi246Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi258Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi262Iron-sulfur 1 (4Fe-4S)By similarity1

GO - Molecular functioni

GO - Biological processi

  • anaerobic electron transport chain Source: EcoCyc
  • anaerobic respiration Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • 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:NARY-MONOMER.
ECOL316407:JW1462-MONOMER.
MetaCyc:NARY-MONOMER.

Protein family/group databases

TCDBi5.A.3.1.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase 2 beta chain (EC:1.7.99.4)
Gene namesi
Name:narY
Ordered Locus Names:b1467, JW1462
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10647. narY.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • membrane Source: GO_Central
  • nitrate reductase complex Source: EcoCyc
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000967341 – 514Respiratory nitrate reductase 2 beta chainAdd BLAST514

Proteomic databases

PaxDbiP19318.
PRIDEiP19318.

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
narGP091523EBI-555059,EBI-547248
narWP193173EBI-555059,EBI-555088

Protein-protein interaction databases

BioGridi4262894. 5 interactors.
DIPiDIP-10323N.
IntActiP19318. 14 interactors.
MINTiMINT-1251788.
STRINGi511145.b1467.

Structurei

3D structure databases

ProteinModelPortaliP19318.
SMRiP19318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 354Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST29
Domaini174 – 2054Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32
Domaini207 – 2364Fe-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.
InParanoidiP19318.
KOiK00371.
OMAiEPMKVSW.
PhylomeDBiP19318.

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.

P19318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TGREGMEYAW FNNVETKPGI
60 70 80 90 100
GYPKNWEDQE EWQGGWVRDV NGKIRPRLGN KMGVITKIFA NPVVPQIDDY
110 120 130 140 150
YEPFTFDYEH LHSAPEGKHI PTARPRSLID GKRMDKVIWG PNWEELLGGE
160 170 180 190 200
FEKRARDRNF EAMQKEMYGQ FENTFMMYLP RLCEHCLNPS CVATCPSGAI
210 220 230 240 250
YKREEDGIVL IDQDKCRGWR LCISGCPYKK IYFNWKSGKS EKCIFCYPRI
260 270 280 290 300
ESGQPTVCSE TCVGRIRYLG VLLYDADRIE EAASTEREVD LYERQCEVFL
310 320 330 340 350
DPHDPSVIEE ALKQGIPQNV IDAAQRSPVY KMAMDWKLAL PLHPEYRTLP
360 370 380 390 400
MVWYVPPLSP IQSYADAGGL PKSEGVLPAI ESLRIPVQYL ANMLSAGDTG
410 420 430 440 450
PVLRALKRMM AMRHYMRSQT VEGVTDTRAI DEVGLSVAQV EEMYRYLAIA
460 470 480 490 500
NYEDRFVIPT SHREMAGDAF AERNGCGFTF GDGCHGSDSK FNLFNSSRID
510
AINITEVRDK AEGE
Length:514
Mass (Da):58,558
Last modified:November 1, 1997 - v2
Checksum:i82D997DB093CD818
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti325 – 326QR → HG in CAA34965 (PubMed:2233673).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17110 Genomic DNA. Translation: CAA34965.1.
U00096 Genomic DNA. Translation: AAC74549.1.
AP009048 Genomic DNA. Translation: BAA15104.1.
PIRiF64899.
RefSeqiNP_415984.1. NC_000913.3.
WP_000702535.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74549; AAC74549; b1467.
BAA15104; BAA15104; BAA15104.
GeneIDi946034.
KEGGiecj:JW1462.
eco:b1467.
PATRICi32118226. VBIEscCol129921_1533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17110 Genomic DNA. Translation: CAA34965.1.
U00096 Genomic DNA. Translation: AAC74549.1.
AP009048 Genomic DNA. Translation: BAA15104.1.
PIRiF64899.
RefSeqiNP_415984.1. NC_000913.3.
WP_000702535.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP19318.
SMRiP19318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262894. 5 interactors.
DIPiDIP-10323N.
IntActiP19318. 14 interactors.
MINTiMINT-1251788.
STRINGi511145.b1467.

Protein family/group databases

TCDBi5.A.3.1.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbiP19318.
PRIDEiP19318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74549; AAC74549; b1467.
BAA15104; BAA15104; BAA15104.
GeneIDi946034.
KEGGiecj:JW1462.
eco:b1467.
PATRICi32118226. VBIEscCol129921_1533.

Organism-specific databases

EchoBASEiEB0641.
EcoGeneiEG10647. narY.

Phylogenomic databases

eggNOGiENOG4108IUE. Bacteria.
COG1140. LUCA.
HOGENOMiHOG000237353.
InParanoidiP19318.
KOiK00371.
OMAiEPMKVSW.
PhylomeDBiP19318.

Enzyme and pathway databases

BioCyciEcoCyc:NARY-MONOMER.
ECOL316407:JW1462-MONOMER.
MetaCyc:NARY-MONOMER.

Miscellaneous databases

PROiP19318.

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 nameiNARY_ECOLI
AccessioniPrimary (citable) accession number: P19318
Secondary accession number(s): P78267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.