Reviewed, UniProtKB/Swiss-Prot O07948 (NUOF_RHOCA)

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

Organism

Rhodobacter capsulatus (Rhodopseudomonas capsulata)

Taxonomic identifier

1061 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	431 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.
Catalytic activity	NADH + quinone = NAD+ + quinol.
Cofactor	Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential.
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

Ontologies

Keywords
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro iron 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 – 431	431	NADH-quinone oxidoreductase subunit F		PRO_0000118578
Regions
	Nucleotide binding	54 – 63	10	NAD By similarity
	Nucleotide binding	167 – 214	48	FMN By similarity
Sites
	Metal binding	346	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	349	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	352	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	392	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	O07948-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 08AFA168C18BF8B4	FASTA	431	47,133
	10 20 30 40 50 60 MLNDHDRIFT NIYGMHDRSL KGAMARGHWD GTAAILGNGR DWIIEQVKAS GLRGRGGAGF 70 80 90 100 110 120 PTGLKWSFMP KQSDGRPSFL VINADESEPG TCKDREIMRH DPHTLIEGAL IAGFAMGARA 130 140 150 160 170 180 AYIYIRGEYV REKEALQAAI DECYEAGLIG KNACRSDYDF DVYLHHGAGA YICGEETALL 190 200 210 220 230 240 ESLEGKKGMP RMKPPFPAGS GLYGCPTTVN NVESIAVVPT ILRRGGAWFA GIGRPNNTGV 250 260 270 280 290 300 KLFAMSGHVN TPCVVEEAMS ISMKELIEKH GGGVRGGWKN LKAVIPGGAS CPVIPAHLCE 310 320 330 340 350 360 DAIMDYDGMR EKQSSFGTAC LIVMDQQTDI IKAIARLSKF FKHESCGQCT PCREGTSWMW 370 380 390 400 410 420 RVMERLVTGE AEVEEIDMLF SVTKQVEGHT ICALGDAAAW PIQGLIRHYR EEIEDRIKAR 430 KTGRMGAMAA E

References

[1]	"Immuno-purification of a dimeric subcomplex of the respiratory NADH-CoQ reductase of Rhodobacter capsulatus equivalent to the FP fraction of the mitochondrial complex I." Duborjal H., Dupuis A., Chapel A., Kieffer S., Lunardi J., Issartel J.P. FEBS Lett. 405:345-350(1997) [PubMed: 9108316] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33303 / B10.
[2]	"The NADH-binding fragment of the NADH:ubiquinone oxidoreductase from Rhodobacter capsulatus: proteins and gene structure." Herter S.M., Schiltz E., Drews G. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y10142 Genomic DNA. Translation: CAA71232.1. Y09884 Genomic DNA. Translation: CAA71013.1. AF029365 Genomic DNA. Translation: AAC24991.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.6.99.5. 567.
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]
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_RHOCA

Accession

Primary (citable) accession number: O07948

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 46 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)