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P19318

- NARY_ECOLI

UniProt

P19318 - NARY_ECOLI

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Protein

Respiratory nitrate reductase 2 beta chain

Gene

narY

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi19 – 191Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi22 – 221Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi26 – 261Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi183 – 1831Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi186 – 1861Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi191 – 1911Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi195 – 1951Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi216 – 2161Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi222 – 2221Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi226 – 2261Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi243 – 2431Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi246 – 2461Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi258 – 2581Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi262 – 2621Iron-sulfur 1 (4Fe-4S)By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. anaerobic respiration Source: EcoCyc
  2. cellular response to DNA damage stimulus Source: EcoliWiki
  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: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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10647. narY.

Subcellular locationi

GO - Cellular componenti

  1. nitrate reductase complex Source: InterPro
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Respiratory nitrate reductase 2 beta chainPRO_0000096734Add
BLAST

Proteomic databases

PaxDbiP19318.
PRIDEiP19318.

Expressioni

Gene expression databases

GenevestigatoriP19318.

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

DIPiDIP-10323N.
IntActiP19318. 14 interactions.
MINTiMINT-1251788.
STRINGi511145.b1467.

Structurei

3D structure databases

ProteinModelPortaliP19318.
SMRiP19318. Positions 1-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 35294Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini174 – 205324Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini207 – 236304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1140.
HOGENOMiHOG000237353.
InParanoidiP19318.
KOiK00371.
OMAiKRMDKIV.
OrthoDBiEOG6X3W4C.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3262QR → HG in CAA34965. (PubMed:2233673)Curated

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.
YP_489732.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74549; AAC74549; b1467.
BAA15104; BAA15104; BAA15104.
GeneIDi12933900.
946034.
KEGGiecj:Y75_p1443.
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 .
PIRi F64899.
RefSeqi NP_415984.1. NC_000913.3.
YP_489732.1. NC_007779.1.

3D structure databases

ProteinModelPortali P19318.
SMRi P19318. Positions 1-505.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10323N.
IntActi P19318. 14 interactions.
MINTi MINT-1251788.
STRINGi 511145.b1467.

Protein family/group databases

TCDBi 5.A.3.1.2. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Proteomic databases

PaxDbi P19318.
PRIDEi P19318.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74549 ; AAC74549 ; b1467 .
BAA15104 ; BAA15104 ; BAA15104 .
GeneIDi 12933900.
946034.
KEGGi ecj:Y75_p1443.
eco:b1467.
PATRICi 32118226. VBIEscCol129921_1533.

Organism-specific databases

EchoBASEi EB0641.
EcoGenei EG10647. narY.

Phylogenomic databases

eggNOGi COG1140.
HOGENOMi HOG000237353.
InParanoidi P19318.
KOi K00371.
OMAi KRMDKIV.
OrthoDBi EOG6X3W4C.
PhylomeDBi P19318.

Enzyme and pathway databases

BioCyci EcoCyc:NARY-MONOMER.
ECOL316407:JW1462-MONOMER.
MetaCyc:NARY-MONOMER.

Miscellaneous databases

PROi P19318.

Gene expression databases

Genevestigatori P19318.

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 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], PROTEIN SEQUENCE OF 1-18.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.

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 26, 2014
This is version 131 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

External Data

Dasty 3