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UniProtKB/Swiss-Prot entry P0AFC9


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

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Entry information
Entry name NUOB_ECO57
Primary accession number P0AFC9
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    December 16, 2008 (Entry version 22)
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: Z3546, ECs3171
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
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.
  • COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
  • 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: 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
AE005174; AAG57416.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB36594.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C91025; C91025.
RefSeq NP_288861.1; -.
NP_311198.1; -.
3D structure databases
ModBase P0AFC9.
Enzyme and pathway databases
BioCyc ECOL83334:ECS3171-MON; -.
Ontologies
GO
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
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_01356; -; 1.
PBIL [Tree]
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.
Genome annotation databases
GeneID 916879; -.
958339; -.
GenomeReviews AE005174_GR; Z3546.
BA000007_GR; ECs3171.
KEGG ece:Z3546; -.
ecs:ECs3171; -.
Phylogenomic databases
HOGENOM P0AFC9; -.
Other
LinkHub P0AFC9; -.
Genome annotation databases
CMR P0AFC9; Z3546.
Other
ProtoNet P0AFC9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; Transport; Ubiquinone.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   220  220     NADH-quinone oxidoreductase subunit B. PRO_0000118766
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). 
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 

P0AFC9 in FASTA format

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