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P42974

- DHNA_BACSU

UniProt

P42974 - DHNA_BACSU

Protein

NADH dehydrogenase

Gene

ahpF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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 By similarity.By similarity

    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

    Enzyme and pathway databases

    BioCyciBSUB:BSU40100-MONOMER.

    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
    Ordered Locus Names:BSU40100
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU40100. [Micado]

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity

    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 – 509509NADH dehydrogenasePRO_0000166789Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP42974.

    PTM databases

    PhosSiteiP0803268.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiP42974. 1 interaction.
    MINTiMINT-8364972.
    STRINGi224308.BSU40100.

    Structurei

    3D structure databases

    ProteinModelPortaliP42974.
    SMRiP42974. Positions 2-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – ?183183Membrane-bindingAdd
    BLAST
    Regioni?184 – 509326CatalyticAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG3634.
    HOGENOMiHOG000169462.
    KOiK03387.
    OMAiDQGPRFA.
    OrthoDBiEOG65XN2W.
    PhylomeDBiP42974.

    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.

    P42974-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLDANIKAQ LNQYMQLIEN DIVLKVSAGE DDTSKDMLAL VDELASMSSK    50
    ISVEKAELNR TPSFSVNRVG EDTGVTFAGI PLGHEFTSLV LALLQVSGRP 100
    PKVDQKVIDQ VKKISGEYHF ESYISLTCHN CPDVVQALNM MSVLNPNITH 150
    TMIDGAAYKA EVESKNIMAV PTVYLNGESF GSGRMTLEEI LAKMGSGTDA 200
    SEFADKEPFD VLVVGGGPAG ASAAIYTARK GIRTGVVAER FGGQVLDTMS 250
    IENFISVKAT EGPKLAASLE EHVKEYDIDV MNLQRAKRLE KKDLFELELE 300
    NGAVLKSKTV ILSTGARWRN VNVPGEQEFK NKGVAYCPHC DGPLFEGKDV 350
    AVIGGGNSGI EAAIDLAGIV NHVTVLEFAP ELKADEVLQK RLYSLPNVTV 400
    VKNAQTKEIT GDQSVNGITY VDRETGEEKH VELQGVFVQI GLVPNTEWLE 450
    GTVERNRMGE IIVDKHGATS VPGLFAAGDC TDSAYNQIII SMGSGATAAL 500
    GAFDYLIRN 509
    Length:509
    Mass (Da):54,874
    Last modified:October 1, 1996 - v2
    Checksum:i487FFF089CA3A079
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291G → E AA sequence (PubMed:8180695)Curated
    Sequence conflicti227 – 2271T → D(PubMed:8125345)Curated
    Sequence conflicti393 – 3931Y → I(PubMed:8125345)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78193 Genomic DNA. Translation: BAA11269.1.
    AL009126 Genomic DNA. Translation: CAB16047.1.
    L19710 Genomic DNA. No translation available.
    PIRiG69583.
    RefSeqiNP_391890.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB16047; CAB16047; BSU40100.
    GeneIDi937717.
    KEGGibsu:BSU40100.
    PATRICi18980090. VBIBacSub10457_4207.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78193 Genomic DNA. Translation: BAA11269.1 .
    AL009126 Genomic DNA. Translation: CAB16047.1 .
    L19710 Genomic DNA. No translation available.
    PIRi G69583.
    RefSeqi NP_391890.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P42974.
    SMRi P42974. Positions 2-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P42974. 1 interaction.
    MINTi MINT-8364972.
    STRINGi 224308.BSU40100.

    PTM databases

    PhosSitei P0803268.

    Proteomic databases

    PaxDbi P42974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB16047 ; CAB16047 ; BSU40100 .
    GeneIDi 937717.
    KEGGi bsu:BSU40100.
    PATRICi 18980090. VBIBacSub10457_4207.

    Organism-specific databases

    GenoListi BSU40100. [Micado ]

    Phylogenomic databases

    eggNOGi COG3634.
    HOGENOMi HOG000169462.
    KOi K03387.
    OMAi DQGPRFA.
    OrthoDBi EOG65XN2W.
    PhylomeDBi P42974.

    Enzyme and pathway databases

    BioCyci BSUB:BSU40100-MONOMER.

    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. "Sequence analysis of the 36-kb region between gntZ and trnY genes of Bacillus subtilis genome."
      Kasahara Y., Nakai S., Ogasawara N.
      DNA Res. 4:155-159(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "A Bacillus subtilis bglA gene encoding phospho-beta-glucosidase is inducible and closely linked to a NADH dehydrogenase-encoding gene."
      Zhang J., Aronson A.I.
      Gene 140:85-90(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-509.
      Strain: 168 / JH642.
    4. "Isolation and characterization of a hydrogen peroxide resistant mutant of Bacillus subtilis."
      Hartford O.M., Dowds B.C.A.
      Microbiology 140:297-304(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-29.
      Strain: 168 / YB886 / BG214.

    Entry informationi

    Entry nameiDHNA_BACSU
    AccessioniPrimary (citable) accession number: P42974
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 122 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3