Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6FE71 (NUOA_ACIAD)

Last modified November 3, 2009. Version 39. 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: ACIAD0730
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length183 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 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.

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 inner membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the complex I subunit 3 family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   LigandNAD
Ubiquinone
   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 – 183183NADH-quinone oxidoreductase subunit A HAMAP MF_01394
PRO_0000362616

Regions

Transmembrane11 – 3121 Potential
Transmembrane63 – 8321 Potential
Transmembrane98 – 11821 Potential

Sequences

Sequence LengthMass (Da)Tools
Q6FE71-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 2EFC97F90A3B8D7A

FASTA18320,052
        10         20         30         40         50         60 
MSAITPYDWA IIAFVIGVTF LCVFMLTVPL LLGGKSWGRA KQEQFESGVV SAGGARIRLS 

        70         80         90        100        110        120 
AKFYLVAIFF VVFDLEALYL YAWATSVREV GWMGFTTMVI FVVDLLIALI YVFATGALTW 

       130        140        150        160        170        180 
SPSDRRKAAG IKPKIGSPNM NIAEITRFNS IEELVIDPTG HIPAQSSGRM KSKTSTAPSS 


KQE 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR543861 Genomic DNA. Translation: CAG67637.1.
RefSeqYP_045459.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FE71.

Genome annotation databases

GeneID2879580.
GenomeReviewsGene locus ACIAD0730 in contig CR543861_GR.
KEGGaci:ACIAD0730.
NMPDRfig|62977.3.peg.473.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6FE71.
OMAALYLYAY.

Enzyme and pathway databases

BioCycASP62977:ACIAD0730-MON.

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_ACIAD
AccessionPrimary (citable) accession number: Q6FE71
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 19, 2004
Last modified: November 3, 2009
This is version 39 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