P0AFC7 (NUOB_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 55.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: NADH-quinone oxidoreductase subunit B EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit B NDH-1 subunit B NUO2 | ||||
| Gene names |
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| Organism | Escherichia coli (strain K12) | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 220 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (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 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. HAMAP MF_01356 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP MF_01356 |
| Cofactor | Binds 1 4Fe-4S cluster By similarity. HAMAP MF_01356 |
| Subunit structure | NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex. |
| Subcellular location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side HAMAP MF_01356. |
| Sequence similarities | Belongs to the complex I 20 kDa subunit family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 220 | 220 | NADH-quinone oxidoreductase subunit B HAMAP MF_01356 | PRO_0000118765 | |||||
Sites | |||||||||
| Metal binding | 63 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 64 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 129 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 158 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 71 | 1 | S → L in CAA48361. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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." Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. J. Mol. Biol. 233:109-122(1993) [PubMed: 7690854] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / AN387. |
| [2] | "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." 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. Horiuchi T.DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2. |
| [6] | "Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli." Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T. Eur. J. Biochem. 230:538-548(1995) [PubMed: 7607227] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-6. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X68301 Genomic DNA. Translation: CAA48361.1. U00096 Genomic DNA. Translation: AAC75347.1. AP009048 Genomic DNA. Translation: BAA16121.2. |
| PIR | E65000. |
| RefSeq | NP_416790.1. NC_000913.2. |
3D structure databases | |
| ProteinModelPortal | P0AFC7. |
| SMR | P0AFC7. Positions 34-181. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P0AFC7. 1 interaction. |
Protein family/group databases | |
| TCDB | 3.D.1.1.1. H+ or Na+-translocating NADH dehydrogenase (NDH) family. |
2D gel databases | |
| SWISS-2DPAGE | P0AFC7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000002390; EBESCP00000002390; EBESCG00000001951. EBESCT00000002391; EBESCP00000002391; EBESCG00000001951. EBESCT00000016093; EBESCP00000015384; EBESCG00000015153. |
| GeneID | 946738. |
| GenomeReviews | Gene locus JW5875 in contig AP009048_GR. Gene locus b2287 in contig U00096_GR. |
| KEGG | ecj:JW5875. eco:b2287. |
| PATRIC | 32119941. VBIEscCol129921_2380. |
Organism-specific databases | |
| EchoBASE | EB2008. |
| EcoGene | EG12083. nuoB. |
Phylogenomic databases | |
| eggNOG | COG0377. |
| GeneTree | EBGT00050000009829. |
| HOGENOM | HBG553221. |
| OMA | PRPEAYI. |
| PhylomeDB | P0AFC7. |
| ProtClustDB | PRK06411. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:NUOB-MONOMER. MetaCyc:NUOB-MONOMER. |
Gene expression databases | |
| Genevestigator | P0AFC7. |
Family and domain databases | |
| HAMAP | MF_01356. NDH1_NuoB. [Tree] |
| InterPro | IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UQ_OxRdtase_20Kd_su. IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB. [Graphical view] |
| Gene3D | G3DSA:3.40.50.700. G3DSA:3.40.50.700. 1 hit. |
| KO | K00331. |
| PANTHER | PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit. |
| Pfam | PF01058. Oxidored_q6. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01957. NuoB_fam. 1 hit. |
| PROSITE | PS01150. COMPLEX1_20K. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0AFC7 Secondary accession number(s): P33598 P78187 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

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