Na(+)-translocating NADH-quinone reductase subunit F - Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395)

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A5F5Y4 (NQRF_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 55. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Na(+)-translocating NADH-quinone reductase subunit F
Short name=Na(+)-NQR subunit F
Short name=Na(+)-translocating NQR subunit F
EC=1.6.5.-

Alternative name(s):
NQR complex subunit F
NQR-1 subunit F

Gene names

Name:	nqrF
Ordered Locus Names:	VC0395_A1879, VC395_2406

Organism

Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP]

Taxonomic identifier

345073 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na⁺ ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway By similarity. HAMAP-Rule MF_00430
Catalytic activity	NADH + ubiquinone + Na⁺(In) = NAD⁺ + ubiquinol + Na⁺(Out). HAMAP-Rule MF_00430
Cofactor	Binds 1 2Fe-2S cluster By similarity. HAMAP-Rule MF_00430 FAD By similarity. HAMAP-Rule MF_00430
Subunit structure	Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and NqrF By similarity.
Subcellular location	Cell inner membrane Potential HAMAP-Rule MF_00430.
Sequence similarities	Belongs to the NqrF family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Ion transport Sodium transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD Sodium Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	sodium ion transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	Gram-negative-bacterium-type cell wall Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 408

408

Na(+)-translocating NADH-quinone reductase subunit F HAMAP-Rule MF_00430

PRO_1000080595

Regions

Transmembrane

4 – 24

Helical; Potential

Domain

33 – 127

2Fe-2S ferredoxin-type

Domain

130 – 270

141

FAD-binding FR-type

Sites

Metal binding

Iron-sulfur (2Fe-2S) By similarity

Metal binding

Iron-sulfur (2Fe-2S) By similarity

Metal binding

Iron-sulfur (2Fe-2S) By similarity

Metal binding

111

Iron-sulfur (2Fe-2S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A5F5Y4 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: F5665E9623CAAD7B
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FASTA

408

45,067

        10         20         30         40         50         60 
MSTIIFGVVM FTLIILALVL VILFAKSKLV PTGDITISIN GDPEKAIVTQ PGGKLLTALA 

        70         80         90        100        110        120 
GAGVFVSSAC GGGGSCGQCR VKIKSGGGDI LPTELDHISK GEAREGERLA CQVAVKADMD 

       130        140        150        160        170        180 
LELPEEIFGV KKWECTVISN DNKATFIKEL KLAIPDGESV PFRAGGYIQI EAPAHHVKYA 

       190        200        210        220        230        240 
DFDVPEKYRG DWDKFNLFRY ESKVDEPIIR AYSMANYPEE FGIIMLNVRI ATPPPNNPNV 

       250        260        270        280        290        300 
PPGQMSSYIW SLKAGDKCTI SGPFGEFFAK DTDAEMVFIG GGAGMAPMRS HIFDQLKRLK 

       310        320        330        340        350        360 
SKRKMSYWYG ARSKREMFYV EDFDGLAAEN DNFVWHCALS DPQPEDNWTG YTGFIHNVLY 

       370        380        390        400 
ENYLKDHEAP EDCEYYMCGP PMMNAAVINM LKNLGVEEEN ILLDDFGG

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References

[1]	Heidelberg J. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395.
[2]	"A recalibrated molecular clock and independent origins for the cholera pandemic clones." Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L. PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000627 Genomic DNA. Translation: ABQ21559.1. CP001235 Genomic DNA. Translation: ACP10396.1.
RefSeq	YP_001217803.1. NC_009457.1. YP_002820632.1. NC_012582.1.
3D structure databases
ProteinModelPortal	A5F5Y4.
SMR	A5F5Y4. Positions 129-407.
ModBase	Search...
Protein-protein interaction databases
STRING	345073.VC0395_A1879.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABQ21559; ABQ21559; VC0395_A1879. ACP10396; ACP10396; VC395_2406.
GeneID	5136909. 7776183.
KEGG	vco:VC0395_A1879. vcr:VC395_2406.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2871.
HOGENOM	HOG000263661.
KO	K00351.
OMA	ANYPEEK.
ProtClustDB	PRK05464.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
HAMAP	MF_00430. NqrF.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR012675. Beta-grasp_dom. IPR017927. Fd_Rdtase_FAD-bd. IPR010205. NADH_Q_Rdtase_suF. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
TIGRFAMs	TIGR01941. nqrF. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NQRF_VIBC3

Accession

Primary (citable) accession number: A5F5Y4
Secondary accession number(s): C3M414

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 12, 2007
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents