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P26829

- DHNA_BACYN

UniProt

P26829 - DHNA_BACYN

Protein

NADH dehydrogenase

Gene

ahpF

Organism
Bacillus sp. (strain YN-1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

    Catalytic activityi

    NADH + acceptor = NAD+ + reduced acceptor.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi210 – 24132FADBy similarityAdd
    BLAST
    Nucleotide bindingi349 – 37931NADBy similarityAdd
    BLAST
    Nucleotide bindingi469 – 47911FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. alkyl hydroperoxide reductase activity Source: InterPro
    2. electron carrier activity Source: InterPro
    3. flavin adenine dinucleotide binding Source: InterPro
    4. NAD binding Source: InterPro
    5. NADH dehydrogenase activity Source: UniProtKB-EC
    6. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. response to reactive oxygen species Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, NAD, Ubiquinone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH dehydrogenase (EC:1.6.99.3)
    Alternative name(s):
    Alkyl hydroperoxide reductase
    Gene namesi
    Name:ahpF
    Synonyms:ndh
    OrganismiBacillus sp. (strain YN-1)
    Taxonomic identifieri72581 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519NADH dehydrogenasePRO_0000166788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi337 ↔ 340Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP26829.
    SMRiP26829. Positions 209-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – ?183183Membrane-bindingAdd
    BLAST
    Regioni?184 – 519336CatalyticAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Family and domain databases

    Gene3Di3.40.30.10. 2 hits.
    InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR002109. Glutaredoxin.
    IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR000103. Pyridine_nuc-diS_OxRdtase_2.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF13192. Thioredoxin_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000238. AhpF. 1 hit.
    PRINTSiPR00368. FADPNR.
    PR00469. PNDRDTASEII.
    SUPFAMiSSF52833. SSF52833. 2 hits.
    TIGRFAMsiTIGR03140. AhpF. 1 hit.
    PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
    PS00573. PYRIDINE_REDOX_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P26829-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLEPQIKSQ LNQYLQLMEG DVLLKVSAGN DKVSEDMLSL VDELASMSSR    50
    ITVEKTNLER TPSFSVNRPG EDTGIVFAGI PLGHEFTSLV LALLQVSGRA 100
    PKAEQNVIDQ IKNIEGEYHF ESYISLSCQN CPDVVQALNL MSVLNPGISH 150
    TMIDGAAFKD EVESKDIMAV PTVYLNGESF TSGRMTVEEI LAQLGSGPDA 200
    SELADKDPFD VLVVGGGPAG ASSAIYAARK GIRTGIVADR FGGQIMDTLS 250
    IENFISQKYT EGPKLAASLE EHVKEYDIDV MKLQRAKRLE KKDLIEIELE 300
    NGAVLKSKSV ILSTGARWRN VGVPGEQEFK NKGVAYCPHC DGPLFEGKDV 350
    AVIGGGNSGV EAAIDLAGIV NHVTVLEFMP ELKADEVLQE RLNSLPNVTV 400
    IKNAQTKEIT GDDKVNGISY MDRDTEEVHH IELAGVFVQI GLVPNTDWLD 450
    GTLERNRFGE IVVDSHGATN VPGVFAAGDC TNSAYKQIII SMGSGATAAL 500
    GAFDYLIRNT TPAESAAAK 519
    Length:519
    Mass (Da):55,830
    Last modified:August 1, 1992 - v1
    Checksum:i054FA461B5A156C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10701 Genomic DNA. Translation: BAA01545.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10701 Genomic DNA. Translation: BAA01545.1 .

    3D structure databases

    ProteinModelPortali P26829.
    SMRi P26829. Positions 209-511.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.30.10. 2 hits.
    InterProi IPR012081. Alkyl_hydroperoxide_Rdtase_suF.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR002109. Glutaredoxin.
    IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR000103. Pyridine_nuc-diS_OxRdtase_2.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF13192. Thioredoxin_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000238. AhpF. 1 hit.
    PRINTSi PR00368. FADPNR.
    PR00469. PNDRDTASEII.
    SUPFAMi SSF52833. SSF52833. 2 hits.
    TIGRFAMsi TIGR03140. AhpF. 1 hit.
    PROSITEi PS51354. GLUTAREDOXIN_2. 1 hit.
    PS00573. PYRIDINE_REDOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1."
      Xu X., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T.
      J. Biochem. 109:678-683(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Tryptic digestion of NADH dehydrogenase from alkalophilic Bacillus."
      Xu X., Kanaya S., Koyama N., Sekiguchi T., Nosoh Y., Ohashi S., Tsuda K.
      J. Biochem. 105:626-632(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiDHNA_BACYN
    AccessioniPrimary (citable) accession number: P26829
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 101 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