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UniProtKB/Swiss-Prot entry O68853


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

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Entry information
Entry name NUOB1_RHIME
Primary accession number O68853
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 54)
Name and origin of the protein
Protein name NADH-quinone oxidoreductase subunit B 1
Synonyms EC 1.6.99.5
NADH dehydrogenase I subunit B 1
NDH-1 subunit B 1
Gene name
Name: nuoB1
Synonyms: nuoB
OrderedLocusNames: R01265
ORFNames: SMc01913
From
Rhizobium meliloti (Sinorhizobium meliloti) [TaxID: 382] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=RCR2011 / SU47;
Schmidt R., Uhde C., Nagel A., Puehler A., Selbitschka W.;
"Sinorhizobium meliloti mutant strain SP10 which is impaired in stationary phase survival shows a reduction in the energy charge due to its defect in the energy-conserving NADH dehydrogenase.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=41;
Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E.;
"Rhizobium meliloti carries two sets of nuo genes.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294398; PubMed=11481430 [NCBI, ExPASy, EBI, Israel, Japan]
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021.";
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(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 (Potential).
  • 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
AF055637; AAC12755.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ245398; CAB51621.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591688; CAC45844.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_385371.1; -.
3D structure databases
ModBase O68853.
Enzyme and pathway databases
BioCyc SMEL266834:SMC01913-MON; -.
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 O68853.
Genome annotation databases
GeneID 1232913; -.
GenomeReviews AL591688_GR; R01265.
KEGG sme:SMc01913; -.
NMPDR fig|266834.1.peg.2559; -.
Phylogenomic databases
HOGENOM O68853; -.
Genome annotation databases
CMR O68853; R01265.
Other
ProtoNet O68853.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Quinone; Ubiquinone.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   192  192     NADH-quinone oxidoreductase subunit B 1. PRO_0000118775
METAL   71    71        Iron-sulfur (4Fe-4S) (Potential). 
METAL   72    72        Iron-sulfur (4Fe-4S) (Potential). 
METAL   136   136        Iron-sulfur (4Fe-4S) (Potential). 
METAL   166   166        Iron-sulfur (4Fe-4S) (Potential). 
CONFLICT   1    33        MELASGTTLVAPQPKGILDPATGKPIGSNDAFF -> MTLSV (in Ref. 1). 
CONFLICT   65    68        MTFG -> NELSV (in Ref. 1; AAC12755). 
Sequence information
Length: 192 AA [This is the length of the unprocessed precursor] Molecular weight: 21002 Da [This is the MW of the unprocessed precursor] CRC64: 5C73D67955AC062D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELASGTTLV APQPKGILDP ATGKPIGSND AFFGEINNEL ADKGFLVTST DELINWARTG 

        70         80         90        100        110        120 
SLMWMTFGLA CCAVEMMQMS MPRYDAERFG FAPRASPRQS DVMIVAGTLT NKMAPALRKV 

       130        140        150        160        170        180 
YDQMPEPRYV ISMGSCANGG GYYHYSYSVV RGCDRVVPVD IYVPGCPPTA EALLYGVLLL 

       190 
QKKIRRTGTI ER 

O68853 in FASTA format

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