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O67334 (NUOB_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-quinone oxidoreductase subunit B

EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I subunit B
NDH-1 subunit B
Gene names
Name:nuoB
Ordered Locus Names:aq_1312
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity. HAMAP MF_01356

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP MF_01356

Cofactor

Binds 1 4Fe-4S cluster By similarity. HAMAP MF_01356

Subunit structure

NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex By similarity.

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_01356.

Sequence similarities

Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179NADH-quinone oxidoreductase subunit B HAMAP MF_01356
PRO_0000118764

Sites

Metal binding351Iron-sulfur (4Fe-4S) Potential
Metal binding361Iron-sulfur (4Fe-4S) Potential
Metal binding1001Iron-sulfur (4Fe-4S) Potential
Metal binding1291Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
O67334 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 239D68B6AF828B77

FASTA17919,880
        10         20         30         40         50         60 
MVAINSNGFV TTTVEELLRW GRRNSLWPVT IGLACCAIEM MHTAASRFDL DRLGVIFRAS 

        70         80         90        100        110        120 
PRQADVLIVA GTVVNKVAPM LKLIWDQMPD PKWCISMGGC ASAGGPFPTY STLQGVDRII 

       130        140        150        160        170 
PVDVYIPGCP PTPQGLIYGI LQLQRKIKEQ GITKYDKLFA DFNREIEKEG IFVPRELKV 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07297.1.
PIRC70413.
RefSeqNP_213898.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67334.
SMRO67334. Positions 6-156.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192772.
GenomeReviewsGene locus aq_1312 in contig AE000657_GR.
KEGGaae:aq_1312.
NMPDRfig|224324.1.peg.913.
PATRIC20959810. VBIAquAeo85532_1022.

Phylogenomic databases

HOGENOMHBG553221.
OMAHYDNERF.
PhylomeDBO67334.
ProtClustDBPRK06411.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1312-MONOMER.

Family and domain databases

HAMAPMF_01356. NDH1_NuoB.
[Tree]
InterProIPR006137. NADH_UbQ_OxRdtase-like_20kDa.
IPR006138. NADH_UQ_OxRdtase_20Kd_su.
IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB.
[Graphical view]
Gene3DG3DSA:3.40.50.700. G3DSA:3.40.50.700. 1 hit.
KOK00331.
PANTHERPTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit.
PfamPF01058. Oxidored_q6. 1 hit.
[Graphical view]
TIGRFAMsTIGR01957. NuoB_fam. 1 hit.
PROSITEPS01150. COMPLEX1_20K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOB_AQUAE
AccessionPrimary (citable) accession number: O67334
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families