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UniProtKB/Swiss-Prot entry P0AFC7


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

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Entry information
Entry name NUOB_ECOLI
Primary accession number P0AFC7
Secondary accession numbers P33598 P78090 P78186 P78187
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on December 20, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 25)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit B
Synonyms EC 1.6.99.5
NADH dehydrogenase I subunit B
NDH-1 subunit B
NUO2
Gene name
Name: nuoB
OrderedLocusNames: b2287, JW5875
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / AN387;
DOI=10.1006/jmbi.1993.1488; PubMed=7690854 [NCBI, ExPASy, EBI, Israel, Japan]
Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
"The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I.";
J. Mol. Biol. 233:109-122(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[6]
PROTEIN SEQUENCE OF 1-6.
PubMed=7607227 [NCBI, ExPASy, EBI, Israel, Japan]
Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.;
"Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli.";
Eur. J. Biochem. 230:538-548(1995).
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.
  • CATALYTIC ACTIVITY: NADH + quinone = NAD+ + quinol.
  • COFACTOR: Binds 1 4Fe-4S cluster (Potential).
  • SUBUNIT: Composed of 13 different subunits.
  • SIMILARITY: Belongs to the complex I 20 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
X68301; CAA48361.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75347.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16121.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E65000; E65000.
RefSeq AP_002885.1; -.
NP_416790.1; -.
3D structure databases
ModBase P0AFC7.
Enzyme and pathway databases
BioCyc EcoCyc:NUOB-MON; -.
2D gel databases
SWISS-2DPAGE P0AFC7; -.
Organism-specific databases
EchoBASE EB2008; -.
EcoGene EG12083; nuoB.
Family and domain databases
InterPro IPR006138; NADH_DHase_20kDa_su.
IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
IPR006137; OxRdtase_q6.
Graphical view of domain structure.
PANTHER PTHR11995:SF2; NADH_DH_20kDa; 1.
PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1.
Pfam PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01957; nuoB_fam; 1.
PROSITE PS01150; COMPLEX1_20K; 1.
BLOCKS P0AFC7.
Genome annotation databases
GeneID 946738; -.
GenomeReviews U00096_GR; b2287.
AP009048_GR; JW5875.
KEGG ecj:JW5875; -.
eco:b2287; -.
Phylogenomic databases
HOGENOM P0AFC7; -.
Genome annotation databases
CMR P0AFC7; b2287.
Other
ProtoNet P0AFC7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Quinone; Ubiquinone.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   220  220     NADH-quinone oxidoreductase subunit B. PRO_0000118765
METAL   63    63        Iron-sulfur (4Fe-4S) (Potential). 
METAL   64    64        Iron-sulfur (4Fe-4S) (Potential). 
METAL   129   129        Iron-sulfur (4Fe-4S) (Potential). 
METAL   158   158        Iron-sulfur (4Fe-4S) (Potential). 
CONFLICT   71    71        S -> L (in Ref. 1; CAA48361). 
Sequence information
Length: 220 AA [This is the length of the unprocessed precursor] Molecular weight: 25056 Da [This is the MW of the unprocessed precursor] CRC64: EBD6268505993880 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDYTLTRIDP NGENDRYPLQ KQEIVTDPLE QEVNKNVFMG KLNDMVNWGR KNSIWPYNFG 

        70         80         90        100        110        120 
LSCCYVEMVT SFTAVHDVAR FGAEVLRASP RQADLMVVAG TCFTKMAPVI QRLYDQMLEP 

       130        140        150        160        170        180 
KWVISMGACA NSGGMYDIYS VVQGVDKFIP VDVYIPGCPP RPEAYMQALM LLQESIGKER 

       190        200        210        220 
RPLSWVVGDQ GVYRANMQSE RERKRGERIA VTNLRTPDEI 

P0AFC7 in FASTA format

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