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Reviewed, UniProtKB/Swiss-Prot Q4QSC6 (NQO8_RHOMR)

Last modified November 4, 2008. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADH-quinone oxidoreductase subunit 8
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit 8
    NDH-1 subunit 8
Gene names
Name: nqo8
OrganismRhodothermus marinus (Rhodothermus obamensis)
Taxonomic identifier29549 [NCBI]
Taxonomic lineageBacteriaBacteroidetesSphingobacteriaSphingobacterialesRhodothermaceaeRhodothermus

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 menaquinone. 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.

Subunit structure

NDH-1 is composed of 14 different subunits. Subunits NQO7-14 constitute the membrane sector of the complex By similarity.

Subcellular location

Cell inner membrane; Multi-pass membrane proteinPotential.

Sequence similarities

Belongs to the complex I subunit 1 family.

Ontologies

Keywords

   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   LigandNAD
   Molecular functionOxidoreductase
   PTMQuinone

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: HAMAP

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNADH dehydrogenase (quinone) activity

Inferred from electronic annotation. Source: EC

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341NADH-quinone oxidoreductase subunit 8
PRO_0000240051

Regions

Transmembrane9 – 2921 Potential
Transmembrane75 – 9521 Potential
Transmembrane108 – 12821 Potential
Transmembrane154 – 17421 Potential
Transmembrane180 – 20021 Potential
Transmembrane244 – 26421 Potential
Transmembrane278 – 29821 Potential
Transmembrane321 – 34121 Potential

Sequences

Sequence LengthMass (Da)Tools
Q4QSC6-1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 546A00803E4605A9

FASTA34137,374
        10         20         30         40         50         60 
MDLPLYWTAL IAFLIINAML LTASVLVYAE RKISGFIQHR LGPNRVGPAG FLQPFADVVK 

        70         80         90        100        110        120 
LLFKEDIIPA QANRFIHALA PTIMVTIAMT VPALIPFARG VVIADIDVGV LAILALTSIS 

       130        140        150        160        170        180 
VYGITLAGWS SNSKYSLLGG LRSSAQMISY ELAMGTAVLS VILQAGSLNV SAIVEAQRDG 

       190        200        210        220        230        240 
WAILGWHVFT NPIGALIFIV TAFAETNRLP FDLPEAEQEL VGGYHTEYSG MKFGMFFLAE 

       250        260        270        280        290        300 
YVNLFVASFV IATLFFGGYL VPFEPLLLKA FPALEGSVLL GLLQFLSLLA KTCFFAFLYI 

       310        320        330        340 
WVRWTFPRFK YNQLMTLGWK YLLPIGLANV ILIALGVALF S 

« Hide

References

[1]"A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes."
Melo A.M.P., Lobo S.A.L., Sousa F.L., Fernandes A.S., Pereira M.M., Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.
Biochim. Biophys. Acta 1709:95-103(2005) [PubMed: 16023073] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PRQ-62B.

Cross-references

Sequence databases

AY972098 Genomic DNA. Translation: AAY42992.1.

3D structure databases

ModBaseSearch...

Family and domain databases

HAMAPMF_01350.
[Tree]
InterProIPR001694. Resp_NADH_DHase_1.
[Graphical view]
PANTHERPTHR11432. Resp_NADH_DH_1. 1 hit.
PfamPF00146. NADHdh. 1 hit.
[Graphical view]
PROSITEPS00667. COMPLEX1_ND1_1. False negative.
PS00668. COMPLEX1_ND1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNQO8_RHOMR
AccessionPrimary (citable) accession number: Q4QSC6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: July 19, 2005
Last modified: November 4, 2008
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents