Q83BQ6 (NUOB_COXBU) Reviewed, UniProtKB/Swiss-Prot

Names 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

Gene names

Name:	nuoB
Ordered Locus Names:	CBU_1447

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. HAMAP-Rule MF_01356
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01356
Cofactor	Binds 1 4Fe-4S cluster By similarity. HAMAP-Rule MF_01356
Subunit structure	NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, 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 HAMAP-Rule MF_01356.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: HAMAP quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 161	161	NADH-quinone oxidoreductase subunit B HAMAP-Rule MF_01356		PRO_0000358395
Sites
	Metal binding	36	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	37	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	102	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	132	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q83BQ6 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4720682912477297	FASTA	161	18,160
	10 20 30 40 50 60 MQQLLTKEGF LLTSLDDLMR WARSGSLWPM TFGLACCAVE MMQCASSRYD LDRFGAGLFR 70 80 90 100 110 120 PSPRQSDVMI VAGTLCNKMA PALRKVYDQM AEPRWVISMG SCANGGGYYH YAYSVVRGCD 130 140 150 160 RIVPVDVYVP GCPPTAEALF YGIMQLRNKI RYRNIFDRKD A

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO90944.1.
RefSeq	NP_820430.1. NC_002971.3.
3D structure databases
ProteinModelPortal	Q83BQ6.
SMR	Q83BQ6. Positions 7-158.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_1447.
Proteomic databases
PRIDE	Q83BQ6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO90944; AAO90944; CBU_1447.
GeneID	1209354.
KEGG	cbu:CBU_1447.
PATRIC	17931649. VBICoxBur82552_1447.
Phylogenomic databases
eggNOG	COG0377.
HOGENOM	HOG000228249.
KO	K00331.
OMA	INYTRTG.
ProtClustDB	PRK06411.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-1435-MONOMER.
Family and domain databases
Gene3D	3.40.50.700. 1 hit.
HAMAP	MF_01356. NDH1_NuoB.
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UQ_OxRdtase_20Kd_su. IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB. [Graphical view]
PANTHER	PTHR11995. PTHR11995. 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_COXBU

Accession

Primary (citable) accession number: Q83BQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	June 1, 2003
Last modified:	May 29, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program