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A2CCP6 (NDHK_PROM3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD(P)H-quinone oxidoreductase subunit K

EC=1.6.5.-
Alternative name(s):
NAD(P)H dehydrogenase I subunit K
NDH-1 subunit K
Short name=NDH-K
Gene names
Name:ndhK
Ordered Locus Names:P9303_25251
OrganismProchlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]
Taxonomic identifier59922 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration By similarity. HAMAP-Rule MF_01356

Catalytic activity

NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP-Rule MF_01356

Cofactor

Binds 1 4Fe-4S cluster By similarity. HAMAP-Rule MF_01356

Subunit structure

NDH-1 can be composed of about 15 different subunits; different subcomplexes with different compositions have been identified which probably have different functions By similarity.

Subcellular location

Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP-Rule MF_01356.

Sequence similarities

Belongs to the complex I 20 kDa subunit family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
Thylakoid
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
NADP
Plastoquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processphotosynthesis, light reaction

Inferred from electronic annotation. Source: UniProtKB-HAMAP

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentthylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250NAD(P)H-quinone oxidoreductase subunit K HAMAP-Rule MF_01356
PRO_0000358453

Sites

Metal binding601Iron-sulfur (4Fe-4S) Potential
Metal binding611Iron-sulfur (4Fe-4S) Potential
Metal binding1251Iron-sulfur (4Fe-4S) Potential
Metal binding1561Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
A2CCP6 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 37A2BD06379B2017

FASTA25026,879
        10         20         30         40         50         60 
MSVTPSIDAV RDLRAASCGP VGAPSVTSEL SENIILTSLD DLHNWARLSS LWPLLYGTAC 

        70         80         90        100        110        120 
CFIEFAALIG SRFDFDRFGL VPRSSPRQAD LLIVAGTVTM KMAPALVRLY EQMPEPKYVI 

       130        140        150        160        170        180 
AMGACTITGG MFSADSTTAV RGVDKLIPVD LYLPGCPPRP EAIFDAVIKL RKKVGDESVS 

       190        200        210        220        230        240 
ERIKIAQTHR YFTVPHQMKR VEPIVTGAYL SADTQKAALS PGAGLPMAAE LNTSEIDASP 

       250 
ASQPSSTYES 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9303.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000554 Genomic DNA. Translation: ABM79256.1.
RefSeqYP_001018521.1. NC_008820.1.

3D structure databases

ProteinModelPortalA2CCP6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59922.P9303_25251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM79256; ABM79256; P9303_25251.
GeneID4778323.
KEGGpmf:P9303_25251.
PATRIC23002609. VBIProMar17757_2590.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0377.
HOGENOMHOG000228249.
KOK05582.
OMAKKVGNES.
OrthoDBEOG62K20C.

Enzyme and pathway databases

BioCycPMAR59922:GH54-2631-MONOMER.

Family and domain databases

Gene3D3.40.50.700. 1 hit.
HAMAPMF_01356. NDH1_NuoB.
InterProIPR006137. NADH_UbQ_OxRdtase-like_20kDa.
IPR006138. NADH_UQ_OxRdtase_20Kd_su.
[Graphical view]
PfamPF01058. Oxidored_q6. 1 hit.
[Graphical view]
TIGRFAMsTIGR01957. nuoB_fam. 1 hit.
PROSITEPS01150. COMPLEX1_20K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDHK_PROM3
AccessionPrimary (citable) accession number: A2CCP6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: February 20, 2007
Last modified: May 14, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families