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Reviewed, UniProtKB/Swiss-Prot Q85BB2 (NDHJ_ANTFO)

Last modified June 16, 2009. Version 31. 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
OrganismAnthoceros formosae (Hornwort)
Taxonomic identifier48387 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaAnthocerotophytaAnthocerotopsidaAnthocerotidaeAnthocerotalesAnthocerotaceaeAnthoceros

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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.

RNA editing

Edited at positions 20, 59, 64, 72, 82 and 110. Ref.1 Ref.2

Ontologies

Keywords
   Biological processTransport
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   Coding sequence diversityRNA editing
   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 – 169169NAD(P)H-quinone oxidoreductase subunit J, chloroplastic HAMAP MF_01357
PRO_0000118651

Sequences

Sequence LengthMass (Da)Tools
Q85BB2-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 815388D996068709

FASTA16919,742
        10         20         30         40         50         60 
MLETFTNDTN EIQGRLSAWL IKHRLAHRPL GFDYQGVETL QVRSEDWLSI AVALYAYGFN 

        70         80         90        100        110        120 
YLRSQCVYDV APGGLLASVY HLTKVQSNAD QPEEVCIKIF VSRKNPKIPS VFWVWKGADF 

       130        140        150        160 
QERESYDMLG ISYESHPRLK RILMPDSWIG WPLRKDYIVP NFYELQDAY 

« Hide

References

« Hide 'large scale' references
[1]"The complete nucleotide sequence of the hornwort (Anthoceros formosae) chloroplast genome: insight into the earliest land plants."
Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.
Nucleic Acids Res. 31:716-721(2003) [PubMed: 12527781] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], RNA EDITING.
Tissue: Thallus.
[2]"RNA editing in hornwort chloroplasts makes more than half the genes functional."
Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.
Nucleic Acids Res. 31:2417-2423(2003) [PubMed: 12711687] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA EDITING.
Tissue: Thallus.

Cross-references

Sequence databases

AB086179 Genomic DNA. Translation: BAC55352.1.
AB087444 mRNA. Translation: BAC55445.1.
AB087445 mRNA. Translation: BAC55446.1.
RefSeqNP_777416.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2553503.

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_ANTFO
AccessionPrimary (citable) accession number: Q85BB2
Secondary accession number(s): Q85UU3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2003
Last modified: June 16, 2009
This is version 31 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