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P42974

- DHNA_BACSU

UniProt

P42974 - DHNA_BACSU

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Protein
NADH dehydrogenase
Gene
ahpF, ndh, BSU40100
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone 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 – 24132FAD By similarity
Add
BLAST
Nucleotide bindingi349 – 37931NAD By similarity
Add
BLAST
Nucleotide bindingi469 – 47911FAD By similarity
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509NADH dehydrogenase
PRO_0000166789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi337 ↔ 340Redox-active By 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – ?183183Membrane-binding
Add
BLAST
Regioni?184 – 509326Catalytic
Add
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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291G → E AA sequence 1 Publication
Sequence conflicti227 – 2271T → D1 Publication
Sequence conflicti393 – 3931Y → I1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 121 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

Similar proteinsi