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Reviewed, UniProtKB/Swiss-Prot A7GV51 (NUOA_BACCN)

Last modified November 3, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADH-quinone oxidoreductase subunit A
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit A
    NDH-1 subunit A
    NUO1
Gene names
Name: nuoA
Ordered Locus Names: Bcer98_3819
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 a menaquinone. 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.

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP MF_01394

Subunit structure

NDH-1 is composed of 14 different subunits. Subunits nuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the complex I subunit 3 family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
   LigandNAD
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: HAMAP

photosynthesis, light reaction

Inferred from electronic annotation. Source: HAMAP

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: InterPro

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122NADH-quinone oxidoreductase subunit A HAMAP MF_01394
PRO_0000362623

Regions

Transmembrane10 – 3021 Potential
Transmembrane66 – 8621 Potential
Transmembrane91 – 11121 Potential

Sequences

Sequence LengthMass (Da)Tools
A7GV51-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: CFBA6DE95F9E8B0F

FASTA12214,133
        10         20         30         40         50         60 
MENVYENSYM IVGIFLLLGI LLPVVALTLG KLLRPHKPSE AKNTTYESGI EPYHDANVRF 

        70         80         90        100        110        120 
HARYYIFALL FVIFDVETLF LYPWAVAYDK LGLFALIEML IFVAMLLIGL AYAWKKKVLQ 


WL 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000764 Genomic DNA. Translation: ABS24009.1.
RefSeqYP_001377004.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7GV51.

Genome annotation databases

GeneID5345984.
GenomeReviewsGene locus Bcer98_3819 in contig CP000764_GR.
KEGGbcy:Bcer98_3819.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAGERELTY.

Family and domain databases

HAMAPMF_01394.
[Tree]
InterProIPR000440. NADH_UbQ/plastoQ_OxRdtase_su3.
[Graphical view]
PANTHERPTHR11058. Oxidored_q4. 1 hit.
PfamPF00507. Oxidored_q4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOA_BACCN
AccessionPrimary (citable) accession number: A7GV51
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents