Q8YGK1 (NUOB_BRUME) 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:	BMEI1157

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella melitensis › Brucella melitensis bv. 1

Protein attributes

Sequence length	193 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.
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.
Sequence caution	The sequence AAL52338.1 differs from that shown. Reason: Erroneous initiation.

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
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 – 193	193	NADH-quinone oxidoreductase subunit B HAMAP-Rule MF_01356		PRO_0000358359
Sites
	Metal binding	72	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	73	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	137	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	167	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8YGK1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 07E2DF39F0E5DF32	FASTA	193	21,032
	10 20 30 40 50 60 MGLTGTNTTL VAPQPKGILD PRTGKPVGSD DAFFNDLNGE LSDKGFIVTS ADALITWART 70 80 90 100 110 120 GSLMWMTFGL ACCAVEMMHI SMPRYDAERF GIAPRASPRQ SDVMIVAGTL TNKMAPALRK 130 140 150 160 170 180 VYDQMPEPRY VISMGSCANG GGYYHYSYSV VRGCDRVVPV DIYVPGCPPT AEALLYGILL 190 LQKKIRRTGT IER

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008917 Genomic DNA. Translation: AAL52338.1. Different initiation.
PIR	AG3396.
RefSeq	NP_540074.1. NC_003317.1.
3D structure databases
ProteinModelPortal	Q8YGK1.
ModBase	Search...
Protein-protein interaction databases
STRING	224914.BMEI1157.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL52338; AAL52338; BMEI1157.
GeneID	1196868.
KEGG	bme:BMEI1157.
PATRIC	17797704. VBIBruMel146950_0667.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000228249.
KO	K00331.
ProtClustDB	PRK06411.
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_BRUME

Accession

Primary (citable) accession number: Q8YGK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program