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Q83BQ6 (NUOB_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:CBU_1447
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length161 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-Rule MF_01356

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01356

Cofactor

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

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161NADH-quinone oxidoreductase subunit B HAMAP-Rule MF_01356
PRO_0000358395

Sites

Metal binding361Iron-sulfur (4Fe-4S) Potential
Metal binding371Iron-sulfur (4Fe-4S) Potential
Metal binding1021Iron-sulfur (4Fe-4S) Potential
Metal binding1321Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
Q83BQ6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4720682912477297

FASTA16118,160
        10         20         30         40         50         60 
MQQLLTKEGF LLTSLDDLMR WARSGSLWPM TFGLACCAVE MMQCASSRYD LDRFGAGLFR 

        70         80         90        100        110        120 
PSPRQSDVMI VAGTLCNKMA PALRKVYDQM AEPRWVISMG SCANGGGYYH YAYSVVRGCD 

       130        140        150        160 
RIVPVDVYVP GCPPTAEALF YGIMQLRNKI RYRNIFDRKD A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO90944.1.
RefSeqNP_820430.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83BQ6.
SMRQ83BQ6. Positions 7-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_1447.

Proteomic databases

PRIDEQ83BQ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90944; AAO90944; CBU_1447.
GeneID1209354.
KEGGcbu:CBU_1447.
PATRIC17931649. VBICoxBur82552_1447.

Phylogenomic databases

eggNOGCOG0377.
HOGENOMHOG000228249.
KOK00331.
OMASSIKYAK.
OrthoDBEOG62K20C.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1435-MONOMER.

Family and domain databases

Gene3D3.40.50.700. 1 hit.
HAMAPMF_01356. NDH1_NuoB.
InterProIPR006137. NADH_UbQ_OxRdtase-like_20kDa.
IPR006138. NADH_UQ_OxRdtase_20Kd_su.
[Graphical view]
PfamPF01058. Oxidored_q6. 1 hit.
[Graphical view]
TIGRFAMsTIGR01957. nuoB_fam. 1 hit.
PROSITEPS01150. COMPLEX1_20K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOB_COXBU
AccessionPrimary (citable) accession number: Q83BQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 75 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names