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P33937

- NAPA_ECOLI

UniProt

P33937 - NAPA_ECOLI

Protein

Periplasmic nitrate reductase

Gene

napA

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 142 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism By similarity.By similarity

    Catalytic activityi

    Nitrite + acceptor = nitrate + reduced acceptor.

    Cofactori

    Binds 1 4Fe-4S cluster.By similarity
    Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi46 – 461Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi49 – 491Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi53 – 531Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi81 – 811Iron-sulfur (4Fe-4S)By similarity

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: EcoCyc
    2. electron carrier activity Source: UniProtKB-HAMAP
    3. iron ion binding Source: UniProtKB-HAMAP
    4. molybdenum ion binding Source: EcoCyc
    5. nitrate reductase activity Source: CACAO
    6. oxidoreductase activity, acting on NAD(P)H Source: RefGenome
    7. protein binding Source: IntAct

    GO - Biological processi

    1. anaerobic respiration Source: EcoliWiki
    2. cellular respiration Source: RefGenome
    3. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
    4. nitrate assimilation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Nitrate assimilation, Transport

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

    Enzyme and pathway databases

    BioCyciEcoCyc:NAPA-MONOMER.
    ECOL316407:JW2194-MONOMER.
    MetaCyc:NAPA-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Periplasmic nitrate reductase (EC:1.7.99.4)
    Gene namesi
    Name:napA
    Synonyms:yojC, yojD, yojE
    Ordered Locus Names:b2206, JW2194
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12067. napA.

    Subcellular locationi

    Periplasm 1 Publication

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: CACAO
    2. periplasmic space Source: EcoCyc

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3636Tat-type signal1 PublicationAdd
    BLAST
    Chaini37 – 828792Periplasmic nitrate reductasePRO_0000019170Add
    BLAST

    Post-translational modificationi

    Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

    Proteomic databases

    PaxDbiP33937.
    PRIDEiP33937.

    Expressioni

    Gene expression databases

    GenevestigatoriP33937.

    Interactioni

    Subunit structurei

    Interacts with NapB.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    napDP0A9I58EBI-554952,EBI-554985

    Protein-protein interaction databases

    DIPiDIP-10304N.
    IntActiP33937. 12 interactions.
    MINTiMINT-1243254.
    STRINGi511145.b2206.

    Structurei

    Secondary structure

    1
    828
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 2116
    Beta strandi26 – 294
    Beta strandi40 – 456
    Beta strandi47 – 493
    Beta strandi54 – 607
    Beta strandi63 – 697
    Turni74 – 785
    Helixi82 – 854
    Helixi86 – 894
    Beta strandi101 – 1099
    Beta strandi114 – 1174
    Helixi120 – 13718
    Helixi140 – 1423
    Beta strandi143 – 1475
    Helixi153 – 16412
    Turni165 – 1673
    Beta strandi172 – 1743
    Helixi175 – 1773
    Turni178 – 1803
    Helixi181 – 19010
    Helixi200 – 2056
    Beta strandi207 – 2137
    Helixi216 – 2194
    Helixi221 – 23212
    Beta strandi238 – 2469
    Helixi248 – 2525
    Beta strandi254 – 2585
    Turni261 – 2633
    Helixi264 – 27714
    Helixi283 – 2897
    Beta strandi290 – 2956
    Helixi308 – 3114
    Beta strandi321 – 3233
    Helixi326 – 3349
    Helixi338 – 3458
    Helixi349 – 36012
    Beta strandi366 – 3716
    Helixi372 – 3754
    Helixi380 – 39415
    Beta strandi402 – 4065
    Turni411 – 4166
    Helixi417 – 4204
    Helixi436 – 44611
    Helixi461 – 4699
    Beta strandi475 – 4806
    Helixi483 – 4864
    Turni490 – 4934
    Helixi494 – 4996
    Beta strandi504 – 5118
    Helixi514 – 5174
    Beta strandi519 – 5257
    Helixi528 – 5303
    Beta strandi533 – 5364
    Beta strandi540 – 5456
    Helixi558 – 5658
    Helixi566 – 5683
    Helixi571 – 5744
    Helixi577 – 5804
    Helixi584 – 5863
    Helixi591 – 5955
    Turni599 – 6024
    Helixi606 – 6083
    Helixi616 – 6216
    Helixi625 – 63713
    Turni638 – 6414
    Helixi647 – 6504
    Beta strandi656 – 6583
    Beta strandi667 – 6715
    Turni672 – 6743
    Beta strandi694 – 6985
    Beta strandi710 – 7123
    Beta strandi714 – 7196
    Helixi731 – 7333
    Helixi735 – 7384
    Beta strandi745 – 7473
    Helixi750 – 7545
    Turni755 – 7573
    Beta strandi763 – 7686
    Beta strandi771 – 78212
    Beta strandi789 – 7935
    Helixi801 – 8033
    Turni811 – 8133
    Beta strandi821 – 8266

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NYAX-ray2.50A/F37-828[»]
    2PQ4NMR-B1-35[»]
    ProteinModelPortaliP33937.
    SMRiP33937. Positions 1-35, 37-827.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33937.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 95574Fe-4S Mo/W bis-MGD-typeAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0243.
    HOGENOMiHOG000031441.
    KOiK02567.
    OMAiHPKTRVA.
    OrthoDBiEOG6CVV7G.
    PhylomeDBiP33937.

    Family and domain databases

    HAMAPiMF_01630. Nitrate_reduct.
    InterProiIPR009010. Asp_de-COase-like_dom.
    IPR006657. MoPterin_dinucl-bd_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR027467. MopterinOxRdtase_cofactor_BS.
    IPR010051. Periplasm_NO3_reductase_lsu.
    IPR006311. TAT_signal.
    IPR019546. TAT_signal_bac_arc.
    [Graphical view]
    PfamiPF04879. Molybdop_Fe4S4. 1 hit.
    PF00384. Molybdopterin. 1 hit.
    PF01568. Molydop_binding. 1 hit.
    [Graphical view]
    SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
    [Graphical view]
    SUPFAMiSSF50692. SSF50692. 1 hit.
    TIGRFAMsiTIGR01706. NAPA. 1 hit.
    TIGR01409. TAT_signal_seq. 1 hit.
    PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P33937-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG    50
    TGCGVLVGTQ QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP 100
    LLRMKNGKYD KEGEFTPITW DQAFDVMEEK FKTALKEKGP ESIGMFGSGQ 150
    WTIWEGYAAS KLFKAGFRSN NIDPNARHCM ASAVVGFMRT FGMDEPMGCY 200
    DDIEQADAFV LWGANMAEMH PILWSRITNR RLSNQNVTVA VLSTYQHRSF 250
    ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG 300
    YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD 350
    QLEQLAQLYA DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP 400
    GCGPFSLTGQ PSACGTAREV GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS 450
    GTIPAKIGLH AVAQDRALKD GKLNVYWTMC TNNMQAGPNI NEERMPGWRD 500
    PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER RTQFWRQQVQ 550
    APGEAKSDLW QLVQFSRRFK TEEVWPEDLL AKKPELRGKT LYEVLYATPE 600
    VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY 650
    HKARGLRWPV VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP 700
    FEPAAEAPDE EYDLWLSTGR VLEHWHTGSM TRRVPELHRA FPEAVLFIHP 750
    LDAKARDLRR GDKVKVVSRR GEVISIVETR GRNRPPQGLV YMPFFDAAQL 800
    VNKLTLDATD PLSKETDFKK CAVKLEKV 828
    Length:828
    Mass (Da):93,042
    Last modified:November 1, 1997 - v3
    Checksum:iCE2D7AB000FEAFCA
    GO

    Sequence cautioni

    The sequence AAA16399.1 differs from that shown. Reason: Frameshift at positions 19 and 27.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981T → R in AAA16399. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00008 Genomic DNA. Translation: AAA16399.1. Frameshift.
    U00096 Genomic DNA. Translation: AAC75266.1.
    AP009048 Genomic DNA. Translation: BAA15989.2.
    PIRiD64990.
    RefSeqiNP_416710.1. NC_000913.3.
    YP_490444.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75266; AAC75266; b2206.
    BAA15989; BAA15989; BAA15989.
    GeneIDi12933227.
    947093.
    KEGGiecj:Y75_p2167.
    eco:b2206.
    PATRICi32119771. VBIEscCol129921_2295.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00008 Genomic DNA. Translation: AAA16399.1 . Frameshift.
    U00096 Genomic DNA. Translation: AAC75266.1 .
    AP009048 Genomic DNA. Translation: BAA15989.2 .
    PIRi D64990.
    RefSeqi NP_416710.1. NC_000913.3.
    YP_490444.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NYA X-ray 2.50 A/F 37-828 [» ]
    2PQ4 NMR - B 1-35 [» ]
    ProteinModelPortali P33937.
    SMRi P33937. Positions 1-35, 37-827.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10304N.
    IntActi P33937. 12 interactions.
    MINTi MINT-1243254.
    STRINGi 511145.b2206.

    Proteomic databases

    PaxDbi P33937.
    PRIDEi P33937.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75266 ; AAC75266 ; b2206 .
    BAA15989 ; BAA15989 ; BAA15989 .
    GeneIDi 12933227.
    947093.
    KEGGi ecj:Y75_p2167.
    eco:b2206.
    PATRICi 32119771. VBIEscCol129921_2295.

    Organism-specific databases

    EchoBASEi EB1994.
    EcoGenei EG12067. napA.

    Phylogenomic databases

    eggNOGi COG0243.
    HOGENOMi HOG000031441.
    KOi K02567.
    OMAi HPKTRVA.
    OrthoDBi EOG6CVV7G.
    PhylomeDBi P33937.

    Enzyme and pathway databases

    BioCyci EcoCyc:NAPA-MONOMER.
    ECOL316407:JW2194-MONOMER.
    MetaCyc:NAPA-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P33937.
    PROi P33937.

    Gene expression databases

    Genevestigatori P33937.

    Family and domain databases

    HAMAPi MF_01630. Nitrate_reduct.
    InterProi IPR009010. Asp_de-COase-like_dom.
    IPR006657. MoPterin_dinucl-bd_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR027467. MopterinOxRdtase_cofactor_BS.
    IPR010051. Periplasm_NO3_reductase_lsu.
    IPR006311. TAT_signal.
    IPR019546. TAT_signal_bac_arc.
    [Graphical view ]
    Pfami PF04879. Molybdop_Fe4S4. 1 hit.
    PF00384. Molybdopterin. 1 hit.
    PF01568. Molydop_binding. 1 hit.
    [Graphical view ]
    SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50692. SSF50692. 1 hit.
    TIGRFAMsi TIGR01706. NAPA. 1 hit.
    TIGR01409. TAT_signal_seq. 1 hit.
    PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Automated multiplex sequencing of the E.coli genome."
      Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
      Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / BHB2600.
    2. Robison K.
      Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    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.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-757.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site."
      Thomas G., Potter L., Cole J.A.
      FEMS Microbiol. Lett. 174:167-171(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 37-43, SUBCELLULAR LOCATION.
    7. "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides."
      Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G.
      J. Biol. Chem. 282:8309-8316(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPORT VIA THE TAT-SYSTEM.

    Entry informationi

    Entry nameiNAPA_ECOLI
    AccessioniPrimary (citable) accession number: P33937
    Secondary accession number(s): P78087
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 142 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