Reviewed, UniProtKB/Swiss-Prot Q8K9Y6 (NUOB_BUCAP)

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:	BUsg_148

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP MF_01356
Cofactor	Binds 1 4Fe-4S cluster By similarity.
Subunit structure	NDH-1 is composed of 13 different subunits. Subunits nuoB, CD, E, F, and G constitute the peripheral sector of the complex By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
Biological process	Transport
Cellular component	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	oxidation reduction Inferred from electronic annotation. Source: HAMAP 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 – 223	223	NADH-quinone oxidoreductase subunit B HAMAP MF_01356		PRO_0000118770
Sites
	Metal binding	66	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	67	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	132	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	161	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8K9Y6-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 9883840771B302BF	FASTA	223	25,497
	10 20 30 40 50 60 MNYTLTRAER KSQRHYPNET TQSTIDPIEG YLKKNILMGK VTKLLHKIVN WGRKNSLWPY 70 80 90 100 110 120 NFGLSCCYVE MVTAFTSVHD VARFGSEVLR ASPRQADVMV IAGTPFIKMA PVIQRLYDQM 130 140 150 160 170 180 LEPKWVISMG ACANSGGMYD IYSVVQGVDK FLPVDIYIPG CPPRPEAYIH ALTLLQKTIN 190 200 210 220 EERRPLSWVV GEQGIYRKKM LSEKIQNRKK RISVVNLPTS EKI

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67716.1.
RefSeq	NP_660505.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1005965.
GenomeReviews	Gene locus BUsg_148 in contig AE013218_GR.
KEGG	bas:BUsg148.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8K9Y6.
OMA	Q8K9Y6. IAGTPFI.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG148-MON.
Family and domain databases
HAMAP	MF_01356. [Tree]
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UbQ_OxRdtase_su-20kDa. IPR014406. NiFe_hyd_3_ssu/Q_oxred_NuoB. [Graphical view]
PANTHER	PTHR11995:SF2. NADH_DH_20kDa. 1 hit. 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_BUCAP

Accession

Primary (citable) accession number: Q8K9Y6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)