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Reviewed, UniProtKB/Swiss-Prot A9LYA4 (NDHJ_ACOAM)

Last modified June 16, 2009. Version 10. 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:
    NAD(P)H-quinone oxidoreductase subunit J, chloroplastic
    EC=1.6.5.-
Alternative name(s):
    NAD(P)H dehydrogenase subunit J
    NADH-plastoquinone oxidoreductase subunit J
Gene names
Name: ndhJ
Encoded onPlastid; Chloroplast
OrganismAcorus americanus (Sweetflag)
Taxonomic identifier263995 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAcoraceaeAcorus

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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 By similarity.

Catalytic activity

NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01357

Subunit structure

NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus By similarity.

Subcellular location

Plastidchloroplast thylakoid membrane; Peripheral membrane protein; Stromal side By similarity.

Sequence similarities

Belongs to the complex I 30 kDa subunit family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   LigandNAD
NADP
Plastoquinone
   Molecular functionOxidoreductase
   PTMQuinone
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: HAMAP

photosynthesis, light reaction

Inferred from electronic annotation. Source: HAMAP

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADH dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: InterPro

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158NAD(P)H-quinone oxidoreductase subunit J, chloroplastic HAMAP MF_01357
PRO_0000358235

Sequences

Sequence LengthMass (Da)Tools
A9LYA4-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0CD496051F160BEA

FASTA15818,674
        10         20         30         40         50         60 
MQGRLSAWLV KHELVHRSLG FDYQGIEILQ IKPEDWDSIA VISYVYGYNY LRSQCAYDVA 

        70         80         90        100        110        120 
PGGFLASVYH LTRIQYGVDQ PEEVCIKVFA PRRNPKIPSV FWIWRSADFQ ERESYDMLGI 

       130        140        150 
SYENHPRLKR ILMPESWIGW PLRKDYIAPN FYEIQDAH 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of 81 genes from 64 plastid genomes resolves relationships in angiosperms and identifies genome-scale evolutionary patterns."
Jansen R.K., Cai Z., Raubeson L.A., Daniell H., dePamphilis C.W., Leebens-Mack J., Muller K.F., Guisinger-Bellian M., Haberle R.C., Hansen A.K., Chumley T.W., Lee S.B., Peery R., McNeal J.R., Kuehl J.V., Boore J.L.
Proc. Natl. Acad. Sci. U.S.A. 104:19369-19374(2007) [PubMed: 18048330] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete chloroplast genome of Acorus americanus."
Peery R.M., Chumley T.W., Kuehl J.V., Boore J.L., Raubeson L.A.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EU016719 Genomic DNA. Translation: ABU85160.1.
EU273602 Genomic DNA. Translation: ABX38747.1.
RefSeqYP_001586185.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5777800.

Family and domain databases

HAMAPMF_01357.
[Tree]
InterProIPR001268. NADH_UbQ_OxRdtase_30kDa_su.
[Graphical view]
PfamPF00329. Complex1_30kDa. 1 hit.
[Graphical view]
ProDomPD001581. Complex1_30K. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00542. COMPLEX1_30K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDHJ_ACOAM
AccessionPrimary (citable) accession number: A9LYA4
Secondary accession number(s): A9QAR7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: February 5, 2008
Last modified: June 16, 2009
This is version 10 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