Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q2IL11 (NUOA_ANADE)

Last modified January 19, 2010. Version 34. 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: Adeh_2570
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length129 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 – 129129NADH-quinone oxidoreductase subunit A HAMAP MF_01394
PRO_5000108234

Regions

Transmembrane9 – 2921 Potential
Transmembrane68 – 8821 Potential
Transmembrane97 – 11721 Potential

Sequences

Sequence LengthMass (Da)Tools
Q2IL11-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 5AFE869BD55CABCE

FASTA12914,210
        10         20         30         40         50         60 
MLTPLQIYFP IGVVLLVAVV LAFTMLGLAN VLGPRRPSLV KQTPFECGSE PIGSARERFG 

        70         80         90        100        110        120 
VKFYVVALLF IVFDIEAIFL YPWAVLLLPD GQGYPGLGWP GFISMGIFVF TLVAGLVYVW 


KKGVLDWAD 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC82340.1.
RefSeqYP_465777.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IL11.

Genome annotation databases

GeneID3890054.
GenomeReviewsGene locus Adeh_2570 in contig CP000251_GR.
KEGGade:Adeh_2570.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0838.
HOGENOMHBG605540.
OMACEPVGSA.
PhylomeDBQ2IL11.

Enzyme and pathway databases

BioCycADEH290397:ADEH_2570-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 nameNUOA_ANADE
AccessionPrimary (citable) accession number: Q2IL11
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: March 7, 2006
Last modified: January 19, 2010
This is version 34 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