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P26829

- DHNA_BACYN

UniProt

P26829 - DHNA_BACYN

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Protein
NADH dehydrogenase
Gene
ahpF, ndh
Organism
Bacillus sp. (strain YN-1)
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.

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519NADH dehydrogenase
PRO_0000166788Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP26829.
SMRiP26829. Positions 209-511.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – ?183183Membrane-binding
Add
BLAST
Regioni?184 – 519336Catalytic
Add
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 16, 2013
This is version 100 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

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