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Q98KQ6 (NUOB_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:mll1371
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length193 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.

Sequence caution

The sequence BAB48758.1 differs from that shown. Reason: Erroneous initiation.

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
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 – 193193NADH-quinone oxidoreductase subunit B HAMAP MF_01356
PRO_0000358465

Sites

Metal binding721Iron-sulfur (4Fe-4S) Potential
Metal binding731Iron-sulfur (4Fe-4S) Potential
Metal binding1371Iron-sulfur (4Fe-4S) Potential
Metal binding1671Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
Q98KQ6 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 6A290226CD4D12F4

FASTA19321,103
        10         20         30         40         50         60 
MGLNDSSGTL VAPKPKGIID PNTGRPVGED DPFFLEINNE LADKGFLVTS TEALITWARS 

        70         80         90        100        110        120 
GSLMFMTFGL ACCAVEMIHT SMPRYDSERF GVAPRASPRQ SDIMIVAGTL TNKMAPALRK 

       130        140        150        160        170        180 
VYDQMPEPRY VISMGSCANG GGYYHYSYSV VRGCDRIVPV DIYVPGCPPS AEALLYGILL 

       190 
LQKKIRRTGT IER 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB48758.1. Different initiation.
RefSeqNP_102972.1. NC_002678.2.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1225635.
GenomeReviewsGene locus mll1371 in contig BA000012_GR.
KEGGmlo:mll1371.
NMPDRfig|266835.1.peg.1077.
PATRIC22476384. VBIMesLot2464_1103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG553221.
ProtClustDBPRK06411.

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_RHILO
AccessionPrimary (citable) accession number: Q98KQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: January 25, 2012
This is version 56 of the entry and version 2 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