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)

A8LLY9

- NAPA_DINSH

UniProt

A8LLY9 - NAPA_DINSH

Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (04 Dec 2007)
      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 bindingi49 – 491Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi52 – 521Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi56 – 561Iron-sulfur (4Fe-4S)UniRule annotation
    Metal bindingi84 – 841Iron-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

    BioCyciDSHI398580:GKEL-3204-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:Dshi_3165
    OrganismiDinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
    Taxonomic identifieri398580 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter
    ProteomesiUP000006833: Chromosome

    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 – 3535Tat-type signalUniRule annotationAdd
    BLAST
    Chaini36 – 831796Periplasmic nitrate reductasePRO_0000335805Add
    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

    Protein-protein interaction databases

    STRINGi398580.Dshi_3165.

    Structurei

    3D structure databases

    ProteinModelPortaliA8LLY9.
    SMRiA8LLY9. Positions 41-830.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 98574Fe-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.
    OMAiCACKVER.
    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.
    [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.

    A8LLY9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTISDSRRTF LKASAAAATA SAAGIPLANG TAAEAQAIST GIRWDKAACR    50
    FCGTGCSVLV GTKEGRVVAT QGDPDAPVNR GLNCIKGYFL SKIMYGEDRL 100
    TMPLLRKTNG VYDKNGTFEP VSWDEAFDVM AQKWKEALAK KGPTSVGMFG 150
    SGQWTVWEGY AAAKLMKAGF RSNNIDPNAR HCMASAVVGF MRTFGIDEPM 200
    GCYDDFEHAD TFVLWGSNMA EMHPILWSRL TDTRLTKPGS EVHVLSTYEH 250
    RSFELADNGM VFAPQTDLAI LNYIANYIIS TGRVNEDFMS KHVNITKTAT 300
    DIGYGLRDEH ALQQEAENPN SGKLEPISFD EYAASVAEYT VDKVSELSGV 350
    PAAQLEKLAE QYADPNRKVM SLWTMGFNQH TRGSWVNSLM YNVHLLVGKI 400
    SEPGNSPFSL TGQPSACGTA REVGTFAHRL PADMVVMNDA HRALTEKKWN 450
    LPEGTIPAKP GFHAVLQHRK LKDGDLNAYW VQCNNNMQAA PNMNEEGYPG 500
    YRNPENFITV SDPYPTVTTM SADLILPTAM WVEKEGAYGN AERRTQFWRQ 550
    QVKAPGEAKS DLWQLMEFSK RFTIEEVWGE ELLAKMPEHR GKTMYDVLFA 600
    NGKVDKYPLS ETAEGFDNDE SEHFGYYVQK GLFEEYAGFG RGKAHDLASF 650
    ETYHQSRGLR WPVVDGQETL YRFREGYDPY VPEGEGVRFY GHSDGKAKII 700
    YAPYEPAPEV PDAEFDLWLC TGRVLEHWHS GSMTRRVPEL HRAYPAAVVY 750
    MHPEDAKARG LRRGQEINIS TRRGDMLSRV ETRGRNKVPQ GLVFVPWFDE 800
    GQLINQLTLD ATCPLSKETD FKKCACKVER A 831
    Length:831
    Mass (Da):92,890
    Last modified:December 4, 2007 - v1
    Checksum:i0D8369C67278F4D9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000830 Genomic DNA. Translation: ABV94898.1.
    RefSeqiWP_012179825.1. NC_009952.1.
    YP_001534499.1. NC_009952.1.

    Genome annotation databases

    EnsemblBacteriaiABV94898; ABV94898; Dshi_3165.
    GeneIDi5712221.
    KEGGidsh:Dshi_3165.
    PATRICi21819127. VBIDinShi9476_3294.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000830 Genomic DNA. Translation: ABV94898.1 .
    RefSeqi WP_012179825.1. NC_009952.1.
    YP_001534499.1. NC_009952.1.

    3D structure databases

    ProteinModelPortali A8LLY9.
    SMRi A8LLY9. Positions 41-830.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 398580.Dshi_3165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV94898 ; ABV94898 ; Dshi_3165 .
    GeneIDi 5712221.
    KEGGi dsh:Dshi_3165.
    PATRICi 21819127. VBIDinShi9476_3294.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DSHI398580:GKEL-3204-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.
    [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 16493 / NCIMB 14021 / DFL 12.

    Entry informationi

    Entry nameiNAPA_DINSH
    AccessioniPrimary (citable) accession number: A8LLY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 52 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3