R4ZGW2 · R4ZGW2_PICAB

Function

function

Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.

Pathway

Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site22[4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner
Binding site47[4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner
Binding site107[4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Function4 iron, 4 sulfur cluster binding
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on iron-sulfur proteins as donors
Molecular Functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
Biological Processlight-independent chlorophyll biosynthetic process
Biological Processphotosynthesis, dark reaction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Light-independent protochlorophyllide reductase subunit N
  • EC number
  • Short names
    DPOR subunit N
    ; LI-POR subunit N

Gene names

    • Name
      chlN
    • ORF names
      PACH01_0108

Encoded on

  • Chloroplast

Organism names

Accessions

  • Primary accession
    R4ZGW2

Subcellular Location

Keywords

Interaction

Subunit

Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain22-439Nitrogenase/oxidoreductase component 1

Sequence similarities

Belongs to the BchN/ChlN family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    468
  • Mass (Da)
    53,286
  • Last updated
    2013-07-24 v1
  • Checksum
    5DD24F5793E68E23
MSAKIDETITFECETGNYHTFCPISCVSWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAHLNDYEELKTLCIRIRKDRDPSVIIWIGTCTTEIIKMDLEGMAPKLEYEIGIPILVARANGLDYAFTQGEDTVLAVMAHRCPEQEFPIGESKETITKTKLFPFPLLKEKKLVEYANHPPLVIFGSLPSNLVSQLDTELRRQFIKVSGWLPAQRYADLPSLGDGVYVCGVNPFLGRTATTLIRRKKCELIVAPFPIGPDGTRAWIERICPVFGIETQSLEEREERIWESLKDYLDLVRGKSVFFMGDNLLEISLARFLIRCGMIVYEIGIPYMDKRYQAAELALLKDTCIKMCIPIPRIVEKPDNSNQIRRMRELQPDLAITGMAHANPLGARGIDTKWSVEFTFAQIHGFASARDVLELVTRPLRRNENLDNLDRTTLVRKNNEFYTSTPR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HF937082
EMBL· GenBank· DDBJ
CCW23147.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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