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Reviewed, UniProtKB/Swiss-Prot A1TLL6 (NUOA_ACIAC)

Last modified November 3, 2009. Version 25. 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: Aave_1263
OrganismAcidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length119 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 – 119119NADH-quinone oxidoreductase subunit A HAMAP MF_01394
PRO_0000362610

Regions

Transmembrane9 – 2921 Potential
Transmembrane63 – 8321 Potential
Transmembrane88 – 10821 Potential

Sequences

Sequence LengthMass (Da)Tools
A1TLL6-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F74C9D91A2A2E0C0

FASTA11913,351
        10         20         30         40         50         60 
MNLDQYLPVL LFILVGIGVG VVPLVLGYVL GPNRPDAAKN SPYECGFEAF EDARMKFDVR 

        70         80         90        100        110 
YYLVAILFIL FDLEIAFLFP WAVALHEVGM TGFVAVIVFL AILVVGFAYE WKKGALDWE 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000512 Genomic DNA. Translation: ABM31854.1.
RefSeqYP_969628.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1TLL6.

Genome annotation databases

GeneID4665551.
GenomeReviewsGene locus Aave_1263 in contig CP000512_GR.
KEGGaav:Aave_1263.
NMPDRfig|397945.5.peg.1107.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIGFAYEW.

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_ACIAC
AccessionPrimary (citable) accession number: A1TLL6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 25 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