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Reviewed, UniProtKB/Swiss-Prot Q39QA7 (NUOA2_GEOMG)

Last modified January 19, 2010. Version 33. 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 2
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit A 2
    NDH-1 subunit A 2
    NUO1 2
Gene names
Name: nuoA2
Ordered Locus Names: Gmet_3355
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length118 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_01394

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. HAMAP MF_01394

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_01394.

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 – 118118NADH-quinone oxidoreductase subunit A 2 HAMAP MF_01394
PRO_0000362692

Regions

Transmembrane5 – 2521 Potential
Transmembrane60 – 8021 Potential
Transmembrane87 – 10721 Potential

Sequences

Sequence LengthMass (Da)Tools
Q39QA7-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 6192FD0FAF14F785

FASTA11813,316
        10         20         30         40         50         60 
MLGAYLPILV LVAIAVIFGL CSLVFSSLIG QKKPSVVKLA PYECGCEPVG SARERFSVKF 

        70         80         90        100        110 
YIIAMLFILF DIEAVFLYPW SVLFKRLGMF GVMEMGVFIV ILFVGYIYVW KKGALEWE 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB33567.1.
RefSeqYP_386292.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ39QA7.

Genome annotation databases

GeneID3739099.
GenomeReviewsGene locus Gmet_3355 in contig CP000148_GR.
KEGGgme:Gmet_3355.
NMPDRfig|269799.3.peg.3330.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0838.
HOGENOMHBG605540.
OMACEPVGSA.
PhylomeDBQ39QA7.

Enzyme and pathway databases

BioCycGMET269799:GMET_3355-MONOMER.

Family and domain databases

HAMAPMF_01394. NDH1_NuoA.
[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 nameNUOA2_GEOMG
AccessionPrimary (citable) accession number: Q39QA7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: November 22, 2005
Last modified: January 19, 2010
This is version 33 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