Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P26829

- DHNA_BACYN

UniProt

P26829 - DHNA_BACYN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NADH dehydrogenase

Gene

ahpF

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 – 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
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-KW
Complete GO annotation...

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

        10         20         30         40         50
MVLEPQIKSQ LNQYLQLMEG DVLLKVSAGN DKVSEDMLSL VDELASMSSR
60 70 80 90 100
ITVEKTNLER TPSFSVNRPG EDTGIVFAGI PLGHEFTSLV LALLQVSGRA
110 120 130 140 150
PKAEQNVIDQ IKNIEGEYHF ESYISLSCQN CPDVVQALNL MSVLNPGISH
160 170 180 190 200
TMIDGAAFKD EVESKDIMAV PTVYLNGESF TSGRMTVEEI LAQLGSGPDA
210 220 230 240 250
SELADKDPFD VLVVGGGPAG ASSAIYAARK GIRTGIVADR FGGQIMDTLS
260 270 280 290 300
IENFISQKYT EGPKLAASLE EHVKEYDIDV MKLQRAKRLE KKDLIEIELE
310 320 330 340 350
NGAVLKSKSV ILSTGARWRN VGVPGEQEFK NKGVAYCPHC DGPLFEGKDV
360 370 380 390 400
AVIGGGNSGV EAAIDLAGIV NHVTVLEFMP ELKADEVLQE RLNSLPNVTV
410 420 430 440 450
IKNAQTKEIT GDDKVNGISY MDRDTEEVHH IELAGVFVQI GLVPNTDWLD
460 470 480 490 500
GTLERNRFGE IVVDSHGATN VPGVFAAGDC TNSAYKQIII SMGSGATAAL
510
GAFDYLIRNT TPAESAAAK
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 29, 2014
This is version 102 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