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Q56350

- NAPA_PARPN

UniProt

Q56350 - NAPA_PARPN

Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Paracoccus pantotrophus (Thiosphaera pantotropha)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Periplasmic nitrate reductaseUniRule annotation (EC:1.7.99.4UniRule annotation)
    Gene namesi
    Name:napAUniRule annotation
    OrganismiParacoccus pantotrophus (Thiosphaera pantotropha)
    Taxonomic identifieri82367 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

    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 – 3131Tat-type signalUniRule annotationAdd
    BLAST
    Chaini32 – 831800Periplasmic nitrate reductasePRO_0000019172Add
    BLAST

    Post-translational modificationi

    Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

    Interactioni

    Subunit structurei

    Interacts with NapB.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ56350.
    SMRiQ56350. 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

    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.

    Q56350-1 [UniParc]FASTAAdd to Basket

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    MTISRRDLLK AQAAGIAAMA ANIPLSSQAP AVPGGVESLQ ITWSKAPCRF    50
    CGTGCGVMVG VKEGRVVATH GDLLAEVNRG LNCVKGYFLS KIMYGADRLT 100
    QPLLRKKDGV YAKDGEFTPV SWEEAFDTMA AQAKRVLRDK GPTALGMFGS 150
    GQWTIFEGYA ATKLMRAGFR SNNLDPNARH CMASAAYAFM RTFGMDEPMG 200
    CYDDFEAADA FVLWGSNMAE MHPILWTRVA DRRLGHPHVK VAVLSTFTHR 250
    SSDLADIPIV FKPGTDLAIL NYIANHIIQT GRVNRDFVDR HTTFVAGATG 300
    IGYGLRDDDP REMAARTAED PAATTPSTFE EFAELVSEYT LDKVSELSGV 350
    EPAFLEQLAE LYADPDRKVM SLWTMGFNQH VRGVWANQMV YNLHLLTGKI 400
    SEPGNSPFSL TGQASACGTA RQVGTFRHRL PSDMTVTNPE RRQDAEEIWR 450
    IPHGVIPEQP GLHAVAQDRA LHDGTLNFYW IQVNNNLQAS PNNDGEAWPG 500
    YRNPDNFIVV SDAYPTVTAL AADLILPAAM WVEKEGAYGN AERRTHVWHQ 550
    LVEAPGEARS DLWQMMEFST RFTTDEVWPE EILAANPNYR GQSLFDVLFR 600
    NGSVDRFDLS ELNPVTPTAE SNAFGFYVQK GLFEEYAPFG RGHGHDLAPY 650
    DTYHEVRGLR WPVVDGKETL WRYREGLDPY VEPGAGVQFY GNPDGKARII 700
    AVPYEPPAEP PDEEYNIWLV TGRVLEHWHS GSMTMRVPEL YRAFPGARCF 750
    MNPEDARDMG FNQGAEVRIV SRRGEIRSRV ETRGRNRMPR GVVFVPWFDA 800
    SQLINKVTLD ATDPISKQTD FKKCAVKILP V 831
    Length:831
    Mass (Da):92,618
    Last modified:November 1, 1996 - v1
    Checksum:iED78963BD2DA2144
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281T → D AA sequence (PubMed:7639719)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z36773 Genomic DNA. Translation: CAA85346.1.
    PIRiS50163.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z36773 Genomic DNA. Translation: CAA85346.1 .
    PIRi S50163.

    3D structure databases

    ProteinModelPortali Q56350.
    SMRi Q56350. Positions 41-828.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha."
      Berks B.C., Richardson D.J., Reilly A., Willis A.C., Ferguson S.J.
      Biochem. J. 309:983-992(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 35512 / DSM 2944 / LMD 82.5 / NCCB 82005.
    2. "Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha."
      Berks B.C., Richardson D.J., Robinson C., Reilly A., Aplin R.T., Ferguson S.J.
      Eur. J. Biochem. 220:117-124(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: M-6.
    3. "Characterization of the paramagnetic iron-containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase."
      Breton J., Berks B.C., Reilly A., Thomson A.J., Ferguson S.J., Richardson D.J.
      FEBS Lett. 345:76-80(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 642-655 AND 699-715.
      Strain: M-6.

    Entry informationi

    Entry nameiNAPA_PARPN
    AccessioniPrimary (citable) accession number: Q56350
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3