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Protein

NADH dehydrogenase

Gene

ahpF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

NADH + acceptor = NAD+ + reduced acceptor.

Cofactori

FADBy similarityNote: 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

GO - Biological processi

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 Componenti: Chromosome

Organism-specific databases

GenoListiBSU40100. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP42974. 1 interaction.
MINTiMINT-8364972.
STRINGi224308.Bsubs1_010100021626.

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.
InParanoidiP42974.
KOiK03387.
OMAiNTTWLEG.
OrthoDBiEOG65XN2W.
PhylomeDBiP42974.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
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.
PRINTSiPR00469. 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

        10         20         30         40         50
MVLDANIKAQ LNQYMQLIEN DIVLKVSAGE DDTSKDMLAL VDELASMSSK
60 70 80 90 100
ISVEKAELNR TPSFSVNRVG EDTGVTFAGI PLGHEFTSLV LALLQVSGRP
110 120 130 140 150
PKVDQKVIDQ VKKISGEYHF ESYISLTCHN CPDVVQALNM MSVLNPNITH
160 170 180 190 200
TMIDGAAYKA EVESKNIMAV PTVYLNGESF GSGRMTLEEI LAKMGSGTDA
210 220 230 240 250
SEFADKEPFD VLVVGGGPAG ASAAIYTARK GIRTGVVAER FGGQVLDTMS
260 270 280 290 300
IENFISVKAT EGPKLAASLE EHVKEYDIDV MNLQRAKRLE KKDLFELELE
310 320 330 340 350
NGAVLKSKTV ILSTGARWRN VNVPGEQEFK NKGVAYCPHC DGPLFEGKDV
360 370 380 390 400
AVIGGGNSGI EAAIDLAGIV NHVTVLEFAP ELKADEVLQK RLYSLPNVTV
410 420 430 440 450
VKNAQTKEIT GDQSVNGITY VDRETGEEKH VELQGVFVQI GLVPNTEWLE
460 470 480 490 500
GTVERNRMGE IIVDKHGATS VPGLFAAGDC TDSAYNQIII SMGSGATAAL

GAFDYLIRN
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:
EMBLi
GenBanki
DDBJi
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.
WP_003243077.1. NZ_JNCM01000034.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_003243077.1. NZ_JNCM01000034.1.

3D structure databases

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

Protein-protein interaction databases

IntActiP42974. 1 interaction.
MINTiMINT-8364972.
STRINGi224308.Bsubs1_010100021626.

Proteomic databases

PaxDbiP42974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU40100. [Micado]

Phylogenomic databases

eggNOGiCOG3634.
HOGENOMiHOG000169462.
InParanoidiP42974.
KOiK03387.
OMAiNTTWLEG.
OrthoDBiEOG65XN2W.
PhylomeDBiP42974.

Enzyme and pathway databases

BioCyciBSUB:BSU40100-MONOMER.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
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.
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR03140. AhpF. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: June 24, 2015
This is version 129 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.