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UniProtKB/Swiss-Prot entry P0A1Y7


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

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Entry information
Entry name NUOCD_SALTI
Primary accession number P0A1Y7
Secondary accession number P33902
Integrated into Swiss-Prot on March 1, 2005
Sequence was last modified on July 22, 2008 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 25)
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: nuoC
Synonyms: nuoCD, nuoD
OrderedLocusNames: STY2556, t0538
From
Salmonella typhi [TaxID: 601] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CT18;
DOI=10.1038/35101607; PubMed=11677608 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18.";
Nature 413:848-852(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700931 / Ty2;
DOI=10.1128/JB.185.7.2330-2337.2003; PubMed=12644504 [NCBI, ExPASy, EBI, Israel, Japan]
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18.";
J. Bacteriol. 185:2330-2337(2003).
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.
  • SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits nuoB, CD, E, F, and G constitute the peripheral sector of the complex (By similarity).
  • SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
  • SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa subunit family.
  • SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa subunit family.
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
AL627274; CAD07558.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014613; AAO68244.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_456868.1; -.
NP_804395.1; -.
3D structure databases
ModBase P0A1Y7.
Enzyme and pathway databases
BioCyc SENT209261:T0538-MON; -.
SENT220341:STY2556-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
HAMAP MF_01359; -; 1.
PBIL [Tree]
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.
Genome annotation databases
GeneID 1069525; -.
1248881; -.
GenomeReviews AE014613_GR; t0538.
AL513382_GR; STY2556.
KEGG stt:t0538; -.
sty:STY2556; -.
Phylogenomic databases
HOGENOM P0A1Y7; -.
Genome annotation databases
CMR P0A1Y7; STY2556.
Other
ProtoNet P0A1Y7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell inner membrane; Cell membrane; Complete proteome; Membrane; Multifunctional enzyme; NAD; Oxidoreductase; Quinone; Transport; Ubiquinone.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   596  595     NADH-quinone oxidoreductase subunit C/D. PRO_0000118679
REGION   2   186  185     NADH dehydrogenase I chain C (By similarity). 
REGION   210   596  387     NADH dehydrogenase I chain D (By similarity). 
Sequence information
Length: 596 AA [This is the length of the unprocessed precursor] Molecular weight: 68402 Da [This is the MW of the unprocessed precursor] CRC64: 362B1FBD9A864F46 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTDLTAQDAA WSTRDHLDDP VIGELRNRFG PDAFTVQATR TGIPVVWVKR EQLLEVGDFL 

        70         80         90        100        110        120 
KKLPKPYVML FDLHGMDERL RTHRDGLPAA DFSVFYHLIS IERNRDIMLK VALSENDLRV 

       130        140        150        160        170        180 
PTFTKLFPNA NWYERETWEM FGIDIEGHPH LTRIMMPQTW EGHPLRKDYP ARATEFDPFE 

       190        200        210        220        230        240 
LTKAKQDLEM EALTFKPEDW GMKRGTDNED FMFLNLGPNH PSAHGAFRII LQLDGEEIVD 

       250        260        270        280        290        300 
CVPDIGYHHR GAEKMGERQS WHSYIPYTDR IEYLGGCVNE MPYVLAVEKL AGITVPDRVN 

       310        320        330        340        350        360 
VIRVMLSELF RINSHLLYIS TFIQDVGAMT PVFFAFTDRQ KIYDLVEAIT GFRMHPAWFR 

       370        380        390        400        410        420 
IGGVAHDLPR GWDRLLREFL EWMPKRLDSY EKAALRNTIL KGRSQGVAAY GAKEALEWGT 

       430        440        450        460        470        480 
TGAGLRATGI DFDVRKWRPY SGYENFDFEV PVGGGVSDCY TRVMLKVEEL RQSLRILQQC 

       490        500        510        520        530        540 
LDNMPEGPFK ADHPLTTPPP KERTLQHIET LITHFLQVSW GPVMPAQESF QMVEATKGIN 

       550        560        570        580        590 
SYYLTSDGST MSYRTRVRTP SFAHLQQIPS AIRGSLVSDL IVYLGSIDFV MSDVDR 

P0A1Y7 in FASTA format

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