Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3HS05

- NAPA_PSEST

UniProt

Q3HS05 - NAPA_PSEST

Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Pseudomonas stutzeri (Pseudomonas perfectomarina)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.UniRule annotation

    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.UniRule annotation

    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
    OrganismiPseudomonas stutzeri (Pseudomonas perfectomarina)
    Taxonomic identifieri316 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    Periplasm UniRule annotation

    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 signalUniRule annotationAdd
    BLAST
    Chaini30 – 834805Periplasmic nitrate reductasePRO_0000045996Add
    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

    ProteinModelPortaliQ3HS05.
    SMRiQ3HS05. Positions 41-829.
    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.
    [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.
    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.

    Q3HS05-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLTRRQFAK ANAAAIAATV AGMPIASTAS NLVTEADATN LKWDKAPCRF    50
    CGTGCGVMVA TRENRVVATH GDVKADVNRG INCVKGYFLS KIMYGTDRLT 100
    QPLLRMKDGK FDKQGEFQPV TWDQAFDIME EKYKAALKAG GPEAIGMFGS 150
    GQWTIWEGYA ANKLMKAGFR SNNIDPNARH CMASAAFGFM RTFGMDEPMG 200
    CYEDIEAADA FVLWGSNMAE MHPVLWTRLT DRRLSAPHVK VAVMSTFEHR 250
    SFELADIPMI FNPQTDLVIL NYIANHIIQS GAVNKEFIDK HTRFAKGATN 300
    IGYGLRPTDP LELKAENAAV ANTWTDIGYE DYVEFLKPYT LEHAAKESGV 350
    PAERLKALAE LYADPKVKVM SFWTMGFNQH TRGVWANNMI YNIHLLTGKI 400
    SEPGNSPFSL TGQPSACGTA REVGTFSHRL PADMAVTNPK HRAITEKIWK 450
    LPEGTIQEKP GFHAVDQSRK LKDGVLKVYW TQVTNNMQAG PNVMQEILPG 500
    WRNPETFVIV SDVYPTVSAQ AADLILPSAM WVEKEGAYGN AERRTQFWHQ 550
    LVTAPGEARS DLWQLVEFSK RFRVDEVWPA ELLSKAPEFK DKTLFDVLFK 600
    NGQVDRFSND EIAEGYANYE AEAFGFYLQK GLFEEYAEFG RGHAHDLAAF 650
    DVYHRERGLR WPVVDEKETQ WRYREGYDPY VEAGSGVQFY GNADKKAIIF 700
    ALPYEVPAEV PDEEYPFWLS TGRVLEHWHT GSMTQRVDEL HKAVPDALVY 750
    MHPEDARKLN VRRGSVVKIV SRRGEMQGRV ETRGRNKPPM GLVYVPFFDA 800
    NKLINKVTLD ATDPISKQTD FKKCAVKIEV VSIA 834
    Length:834
    Mass (Da):93,752
    Last modified:November 8, 2005 - v1
    Checksum:i7621B1EF0FDE3B4D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ200356 Genomic DNA. Translation: ABA42173.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ200356 Genomic DNA. Translation: ABA42173.1 .

    3D structure databases

    ProteinModelPortali Q3HS05.
    SMRi Q3HS05. Positions 41-829.
    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.
    [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.
    PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nitrate reduction in Pseudomonas stutzeri A15 and its contribution to rice and wheat rhizosphere fitness."
      Rediers H., Vanderleyden J., De Mot R.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A15.

    Entry informationi

    Entry nameiNAPA_PSEST
    AccessioniPrimary (citable) accession number: Q3HS05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3