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P19318

- NARY_ECOLI

UniProt

P19318 - NARY_ECOLI

Protein

Respiratory nitrate reductase 2 beta chain

Gene

narY

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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

    Binds 3 4Fe-4S clusters per subunit.By similarity
    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
    6. protein binding Source: IntAct

    GO - Biological processi

    1. anaerobic respiration Source: EcoCyc
    2. cellular response to DNA damage stimulus Source: EcoliWiki
    3. nitrate assimilation Source: UniProtKB-KW

    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-SubCell

    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.
    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.
    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

    MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TGREGMEYAW FNNVETKPGI    50
    GYPKNWEDQE EWQGGWVRDV NGKIRPRLGN KMGVITKIFA NPVVPQIDDY 100
    YEPFTFDYEH LHSAPEGKHI PTARPRSLID GKRMDKVIWG PNWEELLGGE 150
    FEKRARDRNF EAMQKEMYGQ FENTFMMYLP RLCEHCLNPS CVATCPSGAI 200
    YKREEDGIVL IDQDKCRGWR LCISGCPYKK IYFNWKSGKS EKCIFCYPRI 250
    ESGQPTVCSE TCVGRIRYLG VLLYDADRIE EAASTEREVD LYERQCEVFL 300
    DPHDPSVIEE ALKQGIPQNV IDAAQRSPVY KMAMDWKLAL PLHPEYRTLP 350
    MVWYVPPLSP IQSYADAGGL PKSEGVLPAI ESLRIPVQYL ANMLSAGDTG 400
    PVLRALKRMM AMRHYMRSQT VEGVTDTRAI DEVGLSVAQV EEMYRYLAIA 450
    NYEDRFVIPT SHREMAGDAF AERNGCGFTF GDGCHGSDSK FNLFNSSRID 500
    AINITEVRDK AEGE 514
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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.
    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

    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: October 1, 2014
    This is version 129 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