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P11349

- NARH_ECOLI

UniProt

P11349 - NARH_ECOLI

Protein

Respiratory nitrate reductase 1 beta chain

Gene

narH

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 149 (01 Oct 2014)
      Sequence version 3 (01 Feb 1996)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

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

    1
    512
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11349.

    Family & Domainsi

    Domains and Repeats

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti398 – 41720DTKPV…RHYKR → EYQTGTARTETYAGDASLQT in AAA24195. (PubMed:2832376)CuratedAdd
    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

    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: October 1, 2014
    This is version 149 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