Q8K9Y3 (NUOF_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	nuoF
Ordered Locus Names:	BUsg_151

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	447 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.
Catalytic activity	NADH + quinone = NAD+ + quinol.
Cofactor	Binds 1 4Fe-4S cluster Probable. FMN Probable.
Subunit structure	Composed of 13 different subunits. Subunits NuoCD, E, F, and G constitute the peripheral sector of the complex By similarity.
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

Ontologies

Keywords
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 447	447	NADH-quinone oxidoreductase subunit F		PRO_0000118572
Regions
	Nucleotide binding	61 – 70	10	NAD By similarity
	Nucleotide binding	174 – 221	48	FMN By similarity
Sites
	Metal binding	352	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	355	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	358	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	399	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8K9Y3 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D11DE0940D67AB51	FASTA	447	49,865
	10 20 30 40 50 60 MNNIIPTEET HPLTWRLRND RETVWIEEYC KKNGYFSLKK ALKTMCPEDV VHLIKESGLK 70 80 90 100 110 120 GRGGAGFSTG LKWSLMSKDN SSKIRYLLCN ADEMEPGTYK DRFLMENIPH QLIEGMLLSA 130 140 150 160 170 180 FALNVSRGYI FLRGEYIKAE YILKKSIQEA INFGFIGSNI LNSGFNFELF LHTGAGRYIC 190 200 210 220 230 240 GEETALINSL EGRRANPRAK PPFPAVFGLW GKPTCVNNVE TLSNVPSIVL HGVNWYKKLS 250 260 270 280 290 300 KSTDTTGTKL MGFSGKVNNP GVWELPFGTT AREILEDYAR GMKSGLFLKS WQPGGAGTDF 310 320 330 340 350 360 LIEKHLDLPM DFTSIAKAGS RLGTAIAMAV DNKTNMISLV CNIEKFFSRE SCGLCTPCRE 370 380 390 400 410 420 GLPWIVKILE SLEKKEGHKN DVKNLERLCL DLSPGKTFCA HAPGAVEPLQ SAIKYFRLEF 430 440 EAGISIKKLK KCSNILGIQS NEFTSKV

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67719.1.
RefSeq	NP_660508.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9Y3.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg151.
Proteomic databases
PRIDE	Q8K9Y3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67719; AAM67719; BUsg_151.
GeneID	1005968.
KEGG	bas:BUsg151.
PATRIC	21247083. VBIBucAph100086_0155.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1894.
KO	K00335.
OMA	NMVSLTR.
ProtClustDB	CLSK315384.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-161-MONOMER.
Family and domain databases
InterPro	IPR001949. NADH-UbQ_OxRdtase_51kDa_CS. IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR011537. NADH-UbQ_OxRdtase_suF. IPR011538. NADH_UbQ_OxRdtase_51kDa_su. IPR019554. Soluble_ligand-bd. [Graphical view]
Pfam	PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. PF10531. SLBB. 1 hit. [Graphical view]
SMART	SM00928. NADH_4Fe-4S. 1 hit. [Graphical view]
TIGRFAMs	TIGR01959. nuoF_fam. 1 hit.
PROSITE	PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOF_BUCAP

Accession

Primary (citable) accession number: Q8K9Y3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program