Q9PGI5 (NUOK_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-quinone oxidoreductase subunit K
EC=1.6.99.5

Alternative name(s):
NADH dehydrogenase I subunit K
NDH-1 subunit K

Gene names

Name:	nuoK
Ordered Locus Names:	XF_0315

Organism

Xylella fastidiosa [Complete proteome] [HAMAP]

Taxonomic identifier

2371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length	101 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. 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. HAMAP MF_01456
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP MF_01456
Subunit structure	NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_01456.
Sequence similarities	Belongs to the complex I subunit 4L family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC 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 – 101	101	NADH-quinone oxidoreductase subunit K HAMAP MF_01456		PRO_0000390280
Regions
	Transmembrane	4 – 24	21	Helical; Potential
	Transmembrane	30 – 50	21	Helical; Potential
	Transmembrane	62 – 82	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9PGI5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 0FDA8608FED538B6	FASTA	101	10,813
	10 20 30 40 50 60 MISLGHLLVL GAALFCISLA GIFLNRKNVI VLLMSIELML LAVNVNFIAF SRQLGDTAGQ 70 80 90 100 LFVFFILTVA AAEAAIGLAI LVTLFRTRHT INVAEVDALK G

References

[1]

"The genome sequence of the plant pathogen Xylella fastidiosa." Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C. Nature 406:151-159(2000) [PubMed: 10910347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9a5c.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003849 Genomic DNA. Translation: AAF83126.1.
PIR	E82822.
RefSeq	NP_297606.1. NC_002488.3.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1125843.
GenomeReviews	Gene locus XF_0315 in contig AE003849_GR.
KEGG	xfa:XF0315.
NMPDR	fig|160492.1.peg.313.
PATRIC	24130593. VBIXylFas578_0343.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG673066.
OMA	AVNINLM.
ProtClustDB	PRK05715.
Enzyme and pathway databases
BioCyc	XFAS160492:XF0315-MONOMER.
Family and domain databases
HAMAP	MF_01456. NDH1_NuoK. [Tree]
InterPro	IPR001133. NADH_UbQ_OxRdtase_chain4L/K. [Graphical view]
KO	K00340.
PANTHER	PTHR11434. Oxidored_4L. 1 hit.
Pfam	PF00420. Oxidored_q2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOK_XYLFA

Accession

Primary (citable) accession number: Q9PGI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program