Reviewed, UniProtKB/Swiss-Prot Q89AU2 (NUOF_BUCBP)

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:	bbp_147

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	444 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.
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)
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 – 444	444	NADH-quinone oxidoreductase subunit F		PRO_0000118573
Regions
	Nucleotide binding	62 – 71	10	NAD By similarity
	Nucleotide binding	177 – 224	48	FMN By similarity
Sites
	Metal binding	354	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	357	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	360	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	401	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q89AU2-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: C3AD7DF2D8583EA9	FASTA	444	49,916
	10 20 30 40 50 60 MKKLLSRTSE THPLTWRLNA QQDTVWIKEY KRKNGYRAFE KVVNHMTSED VIDLIKQSGL 70 80 90 100 110 120 KGRGGAGFLT GLKWSLMPPL NDEYGYTRYL LCNADEMEPG TYKDRFLMEK VPHQLLEGIL 130 140 150 160 170 180 ISAFALSVTK SYIFLRGEYV NTERILKQSI IEATNYGYLG KNVCGSNLTF EIFIHTGAGR 190 200 210 220 230 240 YICGEETALI NSLEGRRANP RFKPPFPAYV GLWGKPTCVN NVETLSNVPA IFLNGVKWYK 250 260 270 280 290 300 GLSKSLDTGT KMMGFSGSVK FPGIWELPFG ITAREIFERY AGGMKNNKKL KVWQPGGAST 310 320 330 340 350 360 SFLIDKHLDV PMDFVNIKKV GSRLGTALAM AVDDSVSIVS LVRNIEEFFS RESCGFCTPC 370 380 390 400 410 420 RDGLPWIVKI LKVLEQKIGV PEDIEILEQL CEQLGPGRTF CAHAPGAIEP LKSALKYFRL 430 440 EFELCVNSNS TIKCKYIHSS ISEY

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: AAO26881.1.
RefSeq	NP_777776.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1058163.
GenomeReviews	Gene locus bbp_147 in contig AE016826_GR.
KEGG	bab:bbp147.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89AU2.
OMA	Q89AU2. LPHLLIE.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_147-MON.
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_BUCBP

Accession

Primary (citable) accession number: Q89AU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 41 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)