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ECOLI:NUOB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) nuoB (ECO:0000255 with HAMAP-Rule:MF_01356)
Protein Name(s) NADH-quinone oxidoreductase subunit B (ECO:0000255 with HAMAP-Rule:MF_01356)

NADH dehydrogenase I subunit B (ECO:0000255 with HAMAP-Rule:MF_01356) NDH-1 subunit B (ECO:0000255 with HAMAP-Rule:MF_01356) NUO2

External Links
UniProt P0AFC7
EMBL X68301
U00096
AP009048
PIR E65000
RefSeq NP_416790.1
YP_490527.1
ProteinModelPortal P0AFC7
SMR P0AFC7
IntAct P0AFC7
STRING 511145.b2287
TCDB 3.D.1.1.1
SWISS-2DPAGE P0AFC7
PaxDb P0AFC7
PRIDE P0AFC7
EnsemblBacteria AAC75347
BAA16121
GeneID 12933981
946738
KEGG ecj:Y75_p2251
eco:b2287
PATRIC 32119941
EchoBASE EB2008
EcoGene EG12083
eggNOG COG0377
HOGENOM HOG000228249
InParanoid P0AFC7
KO K00331
OMA PRPEAYI
OrthoDB EOG62K20C
PhylomeDB P0AFC7
BioCyc EcoCyc:NUOB-MONOMER
ECOL316407:JW5875-MONOMER
MetaCyc:NUOB-MONOMER
PRO PR:P0AFC7
Proteomes UP000000318
UP000000625
Genevestigator P0AFC7
GO GO:0016020
GO:0030964
GO:0005886
GO:0045272
GO:0051539
GO:0005506
GO:0008137
GO:0048038
GO:0009060
GO:0015990
Gene3D 3.40.50.700
HAMAP MF_01356
InterPro IPR006137
IPR006138
Pfam PF01058
TIGRFAMs TIGR01957
PROSITE PS01150

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0016020

membrane

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0045272

plasma membrane respiratory chain complex I

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12083
PANTHER:PTN000242188

C

Seeded From UniProt

complete

involved_in

GO:0015990

electron transport coupled proton transport

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12083
PANTHER:PTN000242188

P

Seeded From UniProt

complete

involved_in

GO:0009060

aerobic respiration

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12083
PANTHER:PTN000242188

P

Seeded From UniProt

complete

enables

GO:0008137

NADH dehydrogenase (ubiquinone) activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12083
PANTHER:PTN000242188

F

Seeded From UniProt

complete

contributes_to

GO:0003954

NADH dehydrogenase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12083
PANTHER:PTN000242188
UniProtKB:O75251

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:12975362[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0030964

NADH dehydrogenase complex

PMID:7607227[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:7607227[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

NOT|part_of

GO:0005737

cytoplasm

PMID:7607227[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:12975362[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0045272

plasma membrane respiratory chain complex I

PMID:22063474[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0045272

plasma membrane respiratory chain complex I

PMID:11997136[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0015990

electron transport coupled proton transport

PMID:16807239[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009060

aerobic respiration

PMID:9495756[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008137

NADH dehydrogenase (ubiquinone) activity

PMID:9495756[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008137

NADH dehydrogenase (ubiquinone) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006138

F

Seeded From UniProt

complete

enables

GO:0048038

quinone binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006138

F

Seeded From UniProt

complete

enables

GO:0051536

iron-sulfur cluster binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006137

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006138

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006137
InterPro:IPR006138

P

Seeded From UniProt

complete

enables

GO:0050136

NADH dehydrogenase (quinone) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101894

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101894

P

Seeded From UniProt

complete

enables

GO:0005506

iron ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101894

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101894

C

Seeded From UniProt

complete

enables

GO:0051536

iron-sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0411

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0048038

quinone binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0874

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0004

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 2.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ 3.0 3.1 Flemming, D et al. (2003) Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB. J. Biol. Chem. 278 47602-9 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Leif, H et al. (1995) Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230 538-48 PubMed GONUTS page
  5. ↑ Erhardt, H et al. (2012) Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli. Biochim. Biophys. Acta 1817 863-71 PubMed GONUTS page
  6. ↑ David, P et al. (2002) Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues. Biochim. Biophys. Acta 1553 268-78 PubMed GONUTS page
  7. ↑ Flemming, D et al. (2006) Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 281 24781-9 PubMed GONUTS page
  8. ↑ 8.0 8.1 Falk-Krzesinski, HJ & Wolfe, AJ (1998) Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli. J. Bacteriol. 180 1174-84 PubMed GONUTS page
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