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Q8K9Y6 (NUOB_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BUsg_148
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length223 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 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex By similarity.

Subcellular location

Cell 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 membrane
Membrane
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete 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 – 223223NADH-quinone oxidoreductase subunit B HAMAP MF_01356
PRO_0000118770

Sites

Metal binding661Iron-sulfur (4Fe-4S) Potential
Metal binding671Iron-sulfur (4Fe-4S) Potential
Metal binding1321Iron-sulfur (4Fe-4S) Potential
Metal binding1611Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8K9Y6 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 9883840771B302BF

FASTA22325,497
        10         20         30         40         50         60 
MNYTLTRAER KSQRHYPNET TQSTIDPIEG YLKKNILMGK VTKLLHKIVN WGRKNSLWPY 

        70         80         90        100        110        120 
NFGLSCCYVE MVTAFTSVHD VARFGSEVLR ASPRQADVMV IAGTPFIKMA PVIQRLYDQM 

       130        140        150        160        170        180 
LEPKWVISMG ACANSGGMYD IYSVVQGVDK FLPVDIYIPG CPPRPEAYIH ALTLLQKTIN 

       190        200        210        220 
EERRPLSWVV GEQGIYRKKM LSEKIQNRKK RISVVNLPTS EKI 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67716.1.
RefSeqNP_660505.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9Y6.
SMRQ8K9Y6. Positions 42-182.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000000311; EBBUCP00000000311; EBBUCG00000000311.
GeneID1005965.
GenomeReviewsGene locus BUsg_148 in contig AE013218_GR.
KEGGbas:BUsg148.
PATRIC21247077. VBIBucAph100086_0152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008096.
HOGENOMHBG553221.
OMAPRPEAYI.
ProtClustDBPRK06411.

Enzyme and pathway databases

BioCycBAPH198804:BUSG148-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_BUCAP
AccessionPrimary (citable) accession number: Q8K9Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

SIMILARITY comments

Index of protein domains and families