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P39185

- NAPA_CUPNH

UniProt

P39185 - NAPA_CUPNH

Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (27 Sep 2004)
      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.

    Catalytic activityi

    Nitrite + acceptor = nitrate + reduced acceptor.UniRule annotation

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi48 – 481Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi51 – 511Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi55 – 551Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi83 – 831Iron-sulfur (4Fe-4S)UniRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
    2. electron carrier activity Source: UniProtKB-HAMAP
    3. iron ion binding Source: UniProtKB-HAMAP
    4. molybdenum ion binding Source: InterPro
    5. nitrate reductase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
    2. 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

    BioCyciCNEC381666:GJUJ-6487-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Periplasmic nitrate reductaseUniRule annotation (EC:1.7.99.4UniRule annotation)
    Gene namesi
    Name:napAUniRule annotation
    Ordered Locus Names:PHG211
    Encoded oniPlasmid megaplasmid pHG10 Publication
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Plasmid megaplasmid pHG1

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Tat-type signal1 PublicationUniRule annotationAdd
    BLAST
    Chaini30 – 831802Periplasmic nitrate reductasePRO_0000019168Add
    BLAST

    Post-translational modificationi

    Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

    Expressioni

    Inductioni

    Expressed independently of nitrate induction and anaerobiosis.

    Interactioni

    Subunit structurei

    Interacts with NapB.UniRule annotation

    Protein-protein interaction databases

    STRINGi381666.PHG211.

    Structurei

    Secondary structure

    1
    831
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 478
    Beta strandi56 – 627
    Beta strandi65 – 717
    Turni76 – 805
    Helixi84 – 874
    Helixi88 – 914
    Beta strandi103 – 1075
    Beta strandi115 – 1195
    Helixi122 – 13918
    Helixi142 – 1443
    Beta strandi145 – 1495
    Helixi155 – 16612
    Turni167 – 1693
    Beta strandi174 – 1763
    Helixi177 – 1804
    Helixi183 – 19311
    Helixi202 – 2065
    Beta strandi209 – 2157
    Helixi218 – 2214
    Helixi223 – 23513
    Beta strandi240 – 2489
    Helixi250 – 2534
    Beta strandi256 – 2605
    Turni263 – 2653
    Helixi266 – 27914
    Helixi285 – 2917
    Beta strandi292 – 2976
    Helixi310 – 3145
    Beta strandi324 – 3274
    Helixi329 – 3379
    Helixi341 – 3488
    Helixi352 – 36312
    Beta strandi369 – 3746
    Helixi375 – 3784
    Helixi383 – 39715
    Beta strandi405 – 4095
    Turni414 – 4196
    Helixi420 – 4234
    Helixi439 – 44810
    Helixi464 – 4729
    Beta strandi478 – 4836
    Helixi486 – 4894
    Turni493 – 4964
    Helixi497 – 5026
    Beta strandi507 – 5148
    Helixi517 – 5204
    Beta strandi523 – 5297
    Helixi531 – 5333
    Beta strandi536 – 5394
    Beta strandi543 – 5486
    Helixi561 – 5699
    Helixi574 – 5774
    Helixi580 – 5834
    Helixi587 – 5893
    Helixi594 – 5985
    Beta strandi600 – 6034
    Helixi609 – 6113
    Helixi619 – 6246
    Helixi628 – 64013
    Turni641 – 6444
    Helixi650 – 6556
    Beta strandi659 – 6624
    Beta strandi670 – 6745
    Turni675 – 6773
    Beta strandi697 – 7015
    Beta strandi713 – 7153
    Beta strandi717 – 7226
    Helixi734 – 7363
    Helixi738 – 7436
    Beta strandi748 – 7514
    Helixi753 – 7586
    Beta strandi766 – 7705
    Beta strandi775 – 78511
    Beta strandi792 – 7976
    Helixi804 – 8063
    Turni814 – 8163
    Beta strandi824 – 8307

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ML1X-ray1.60A30-831[»]
    3O5AX-ray1.72A30-831[»]
    ProteinModelPortaliP39185.
    SMRiP39185. Positions 41-828.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 97574Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.UniRule annotation
    Contains 1 4Fe-4S Mo/W bis-MGD-type domain.UniRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0243.
    HOGENOMiHOG000031441.
    KOiK02567.
    OMAiHAMANVI.
    OrthoDBiEOG6CVV7G.

    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.

    P39185-1 [UniParc]FASTAAdd to Basket

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    MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF    50
    CGTGCGVTVA VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT 100
    RPLMRMKNGK YDKNGDFAPV TWDQAFDEME RQFKRVLKEK GPTAVGMFGS 150
    GQWTVWEGYA AAKLYKAGFR SNNIDPNARH CMASAAAGFM RTFGMDEPMG 200
    CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR VVVLSTFTHR 250
    CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD 300
    IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV 350
    PKAKLDQLAE LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI 400
    ATPGNSPFSL TGQPSACGTA REVGTFSHRL PADMVVTNPK HREEAERIWK 450
    LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW VQVNNNMQAA ANLMEEGLPG 500
    YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN AERRTQFWHQ 550
    LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR 600
    NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF 650
    DAYHEARGLR WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF 700
    ALPYEPPAES PDKEYPYWLV TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF 750
    MHPEDAKALG LRRGVEVEVV SRRGRMRSRI ETRGRDAPPR GLVFVPWFDA 800
    SQLINKVTLD ATCPISLQTD FKKCAVKIVK V 831
    Length:831
    Mass (Da):93,346
    Last modified:September 27, 2004 - v2
    Checksum:i34CE1CDE6677C42F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1516GMFGSG → ACSAPA in CAA50507. (PubMed:8376334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71385 Genomic DNA. Translation: CAA50507.1.
    AY305378 Genomic DNA. Translation: AAP85963.1.
    PIRiA48489.
    RefSeqiNP_942849.1. NC_005241.1.
    WP_011154126.1. NC_005241.1.

    Genome annotation databases

    EnsemblBacteriaiAAP85963; AAP85963; PHG211.
    GeneIDi2656653.
    KEGGireh:PHG211.
    PATRICi35228976. VBIRalEut6770_0159.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71385 Genomic DNA. Translation: CAA50507.1 .
    AY305378 Genomic DNA. Translation: AAP85963.1 .
    PIRi A48489.
    RefSeqi NP_942849.1. NC_005241.1.
    WP_011154126.1. NC_005241.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ML1 X-ray 1.60 A 30-831 [» ]
    3O5A X-ray 1.72 A 30-831 [» ]
    ProteinModelPortali P39185.
    SMRi P39185. Positions 41-828.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.PHG211.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP85963 ; AAP85963 ; PHG211 .
    GeneIDi 2656653.
    KEGGi reh:PHG211.
    PATRICi 35228976. VBIRalEut6770_0159.

    Phylogenomic databases

    eggNOGi COG0243.
    HOGENOMi HOG000031441.
    KOi K02567.
    OMAi HAMANVI.
    OrthoDBi EOG6CVV7G.

    Enzyme and pathway databases

    BioCyci CNEC381666:GJUJ-6487-MONOMER.

    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. "Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16."
      Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S., Friedrich B.
      J. Bacteriol. 175:5867-5876(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-50.
    2. "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."
      Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.
      J. Mol. Biol. 332:369-383(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

    Entry informationi

    Entry nameiNAPA_CUPNH
    AccessioniPrimary (citable) accession number: P39185
    Secondary accession number(s): Q7WXC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3