Reviewed, UniProtKB/Swiss-Prot A1B497 (NQO6_PARDP)

Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit 6
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I, subunit 6
    NDH-1, subunit 6

Gene names

Name:	nqo6
Ordered Locus Names:	Pden_2249

Organism

Paracoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]

Taxonomic identifier

318586 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	175 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. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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 Potential.
Subunit structure	NDH-1 is composed of at least 14 different subunits, nqo1 to nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers By similarity.
Subcellular location	Cell inner 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 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	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	internal side of 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 – 175	175	NADH-quinone oxidoreductase subunit 6 HAMAP MF_01356		PRO_0000358441
Sites
	Metal binding	54	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	55	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	119	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	149	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	A1B497-1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 8233131871D66E8B	FASTA	175	19,505
	10 20 30 40 50 60 MMTGLNTAGA DRDLATAELN RELQDKGFLL TTTEDIINWA RNGSLHWMTF GLACCAVEMM 70 80 90 100 110 120 QTSMPRYDLE RFGTAPRASP RQSDLMIVAG TLTNKMAPAL RKVYDQMPEP RYVISMGSCA 130 140 150 160 170 NGGGYYHYSY SVVRGCDRIV PVDIYVPGCP PTAEALLYGI LQLQRRIRRT GTLVR

References

[1]

"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000489 Genomic DNA. Translation: ABL70341.1.
RefSeq	YP_916037.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A1B497.
Genome annotation databases
GeneID	4579303.
GenomeReviews	Gene locus Pden_2249 in contig CP000489_GR.
KEGG	pde:Pden_2249.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	EMMATNA.
Family and domain databases
HAMAP	MF_01356. [Tree]
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UbQ_OxRdtase_20kDa_su. 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

NQO6_PARDP

Accession

Primary (citable) accession number: A1B497

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 24 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)