A0A069SGW3 · A0A069SGW3_PHOVU
- ProteinNa(+)-translocating NADH-quinone reductase subunit B
- GenenqrB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids402 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic activity
- a ubiquinone + H+ + n Na+(in) + NADH = a ubiquinol + n Na+(out) + NAD+
a ubiquinone RHEA-COMP:9565 + CHEBI:15378 + n Na+ (in)CHEBI:29101+ CHEBI:57945 = a ubiquinol RHEA-COMP:9566 + n Na+ (out)CHEBI:29101+ CHEBI:57540
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | FMN binding | |
Molecular Function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor | |
Biological Process | respiratory electron transport chain | |
Biological Process | sodium ion transport | |
Biological Process | transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNa(+)-translocating NADH-quinone reductase subunit B
- EC number
- Short namesNa(+)-NQR subunit B ; Na(+)-translocating NQR subunit B
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Phocaeicola
Accessions
- Primary accessionA0A069SGW3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 57-74 | Helical | ||||
Sequence: IMSMVVIALIPALLFGMY | ||||||
Transmembrane | 94-119 | Helical | ||||
Sequence: FIYGFLAVLPKIIVSYVVGLGIEFVV | ||||||
Transmembrane | 131-162 | Helical | ||||
Sequence: FLVSGLLIPMIVPVECPLWILAVATAFSVIFA | ||||||
Transmembrane | 252-275 | Helical | ||||
Sequence: LIPGSIGETSVIAIALGAIILLWT | ||||||
Transmembrane | 282-300 | Helical | ||||
Sequence: TMFSVFAGGIVMGLIFNVF | ||||||
Transmembrane | 312-330 | Helical | ||||
Sequence: WYEHIVLGGFCFGAVFMAT | ||||||
Transmembrane | 342-360 | Helical | ||||
Sequence: KFIYGFLIGVMAIVIRVLN | ||||||
Transmembrane | 366-386 | Helical | ||||
Sequence: GMMLAILLMNIFAPLIDYCIV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 220 | FMN phosphoryl threonine | ||||
Sequence: T |
Keywords
- PTM
Interaction
Subunit
Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and NqrF.
Structure
Sequence
- Sequence statusComplete
- Length402
- Mass (Da)43,551
- Last updated2014-10-01 v1
- Checksum52EACD93692D58DD
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JNHM01000028 EMBL· GenBank· DDBJ | KDS53684.1 EMBL· GenBank· DDBJ | Genomic DNA |