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P0AFD0 (NUOB_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:SF2363, S2498
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length220 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. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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 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
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 – 220220NADH-quinone oxidoreductase subunit B HAMAP MF_01356
PRO_0000118768

Sites

Metal binding631Iron-sulfur (4Fe-4S) Potential
Metal binding641Iron-sulfur (4Fe-4S) Potential
Metal binding1291Iron-sulfur (4Fe-4S) Potential
Metal binding1581Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
P0AFD0 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: EBD6268505993880

FASTA22025,056
        10         20         30         40         50         60 
MDYTLTRIDP NGENDRYPLQ KQEIVTDPLE QEVNKNVFMG KLNDMVNWGR KNSIWPYNFG 

        70         80         90        100        110        120 
LSCCYVEMVT SFTAVHDVAR FGAEVLRASP RQADLMVVAG TCFTKMAPVI QRLYDQMLEP 

       130        140        150        160        170        180 
KWVISMGACA NSGGMYDIYS VVQGVDKFIP VDVYIPGCPP RPEAYMQALM LLQESIGKER 

       190        200        210        220 
RPLSWVVGDQ GVYRANMQSE RERKRGERIA VTNLRTPDEI

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005674 Genomic DNA. Translation: AAN43876.1.
AE014073 Genomic DNA. Translation: AAP17694.1.
RefSeqNP_708169.1. NC_004337.2.
NP_837884.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AFD0.
SMRP0AFD0. Positions 34-181.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000087470; EBESCP00000084292; EBESCG00000086515.
EBESCT00000093243; EBESCP00000089879; EBESCG00000092287.
GeneID1027233.
1078089.
GenomeReviewsGene locus SF2363 in contig AE005674_GR.
Gene locus S2498 in contig AE014073_GR.
KEGGsfl:SF2363.
sfx:S2498.
PATRIC18706589. VBIShiFle31049_2770.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009829.
HOGENOMHBG553221.
OMAPRPEAYI.
ProtClustDBPRK06411.

Enzyme and pathway databases

BioCycSFLE198214:AAN43876.1-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_SHIFL
AccessionPrimary (citable) accession number: P0AFD0
Secondary accession number(s): P33598 expand/collapse secondary AC list , P78090, P78186, P78187
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 25, 2012
This is version 50 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

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