Reviewed, UniProtKB/Swiss-Prot Q89AU5 (NUOB_BUCBP)

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:	bbp_144

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	222 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 – 222	222	NADH-quinone oxidoreductase subunit B HAMAP MF_01356		PRO_0000118771
Sites
	Metal binding	67	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	68	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	133	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	162	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q89AU5-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: ED00C35665AD2BDB	FASTA	222	25,606
	10 20 30 40 50 60 MKYTLTRVNI SDDDQNYPRE KKIQVSDPTK KYIQKNVFMG TLSKVLHNLV NWGRKNSLWP 70 80 90 100 110 120 YNFGLSCCYV EMVTSFTSVH DISRFGSEVL RASPRQADFM VIAGTPFIKM VPIIQRLYDQ 130 140 150 160 170 180 MLEPKWVISM GSCANSGGMY DIYSVVQGVD KFLPVDVYIP GCPPRPEAYI HGLMLLQKSI 190 200 210 220 SKERRPLSWI IGEQGIYKAN FNSEKKNLRK MRNLVKYSQD KN

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26878.1.
RefSeq	NP_777773.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1058400.
GenomeReviews	Gene locus bbp_144 in contig AE016826_GR.
KEGG	bab:bbp144.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89AU5.
OMA	Q89AU5. IAGTPFI.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_144-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_BUCBP

Accession

Primary (citable) accession number: Q89AU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 40 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)