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UniProtKB/Swiss-Prot entry Q89AU4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NUOCD_BUCBP
Primary accession number Q89AU4
Secondary accession numbers None
Integrated into Swiss-Prot on November 14, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit C/D
Synonyms EC 1.6.99.5
NADH dehydrogenase I subunit C/D
NDH-1 subunit C/D
Gene name
Name: nuoCD
OrderedLocusNames: bbp_145
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE016826; AAO26879.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_777774.1; -.
3D structure databases
ModBase Q89AU4.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_145-MON; -.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0008137; Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0048038; Molecular function: quinone binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006120; Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR014029; NADH-UbQ_OxRdtase_49kDa_CS.
IPR010219; NADH_DH_1_dsu.
IPR010218; NADH_DH_csu.
IPR001268; NADH_DHase_Ub_30kDa_su.
IPR001135; NADH_UbQ_OxRdtase_49kDa.
Graphical view of domain structure.
Pfam PF00329; Complex1_30kDa; 1.
PF00346; Complex1_49kDa; 1.
Pfam graphical view of domain structure.
ProDom PD001581; Complex1_30K; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01961; NuoC_fam; 1.
TIGR01962; NuoD; 1.
PROSITE PS00542; COMPLEX1_30K; FALSE_NEG.
PS00535; COMPLEX1_49K; 1.
BLOCKS Q89AU4.
ProtoNet Q89AU4.
Genome annotation databases
GeneID 1058218; -.
GenomeReviews AE016826_GR; bbp_145.
KEGG bab:bbp145; -.
Phylogenomic databases
HOGENOM Q89AU4; -.
Genome annotation databases
CMR Q89AU4; bbp_145.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Multifunctional enzyme; NAD; Oxidoreductase; Quinone.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   597  597     NADH-quinone oxidoreductase subunit C/D. PRO_0000118683
REGION   1   188  188     NADH dehydrogenase I subunit C. 
REGION   211   597  387     NADH dehydrogenase I subunit D. 
Sequence information
Length: 597 AA [This is the length of the unprocessed precursor] Molecular weight: 69110 Da [This is the MW of the unprocessed precursor] CRC64: 480D38EFDEE505FA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKEIKRDDV NVIEKDFGNN NSIILKLFKK FGEDSFFIQT TVTDIIVLWI DGSLLLALAK 

        70         80         90        100        110        120 
FLLTINNPYN MLFDLYGIDE RMRLYKHNLP LSHFSVVYHF ISINRNSDII LKIALLEEKL 

       130        140        150        160        170        180 
SLPTLTKLYP NANWYEREIW DMFGISFENH PNLIRILMPK TWVGHPLRKD HPARATEFDP 

       190        200        210        220        230        240 
YVLNKYKEDI EMEALKFKPE EWGMKKNKQS KYMFLNLGPN HPSAHGAFRI ILQLDGEEIV 

       250        260        270        280        290        300 
DCVPDIGYHH RGAEKMGERQ TWHNYIPYTD RVEYLGGCIN EMPYVLAVER LAGIEVSQRI 

       310        320        330        340        350        360 
EVIRIMLSEL FRINSHLLFI STFIQDVGAM TPVFLAFTDR QKIYDLIELI TGSRMHPAWF 

       370        380        390        400        410        420 
RIGGLAHDLP KGWNALLKEF LLWMPKRLLK YINVALKNSI LISRSKGIAE YNKHDALLWG 

       430        440        450        460        470        480 
VTGAGLRATG INFDVRKKRP YSGYQNFDFE VPIGAGISDC YSRVMLKLEE IWQSLAILKQ 

       490        500        510        520        530        540 
CLENMPEGPF KMDHPNTTPP HKVRTLQHIE TMISHFLKVS WGPVLSSNES FKMVEATKGI 

       550        560        570        580        590 
NSYYLISDGN TMSYRTRIRT PSFPHLQQIP SVIRGNLISD LIAYLGSIDF VMSDVDR 

Q89AU4 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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