Q19V92 · CHLB_CHLAT

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, active site.

TypeIDPosition(s)Description
Binding site36[4Fe-4S] cluster (UniProtKB | ChEBI); ligand shared with heterodimeric partner
Active site296Proton donor
Binding site431-432substrate

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 B
  • EC number
  • Short names
    DPOR subunit B
    ; LI-POR subunit B

Gene names

    • Name
      chlB

Encoded on

  • Chloroplast

Organism names

Accessions

  • Primary accession
    Q19V92

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003240471-510Light-independent protochlorophyllide reductase subunit B

Interaction

Subunit

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

Structure

Family & Domains

Sequence similarities

Belongs to the ChlB/BchB/BchZ family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    510
  • Mass (Da)
    57,474
  • Last updated
    2007-02-20 v2
  • Checksum
    37BA8884272F5630
MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIVDRHVLARGSQNKVVENITRKDKEERPDLIVLTPTCTSSILQEDLQNFVDRASMDSESDVILADVNHYRVNELQAADRTLEQVVRFYIEKSKKQGDLNLTKTEKPSANILGIFTLGFHNQHDCRELKRLLQELGIEINEVIPEGGSVNNLKNLPRAWFNLVPYREVGLMTAIYLEKEFGMPYVSTTPMGVVDTATCIREIEKILNSFDKDVVVDFESYIDKQTRFVSQAAWFSRSIDCQNLTGKKAVVFGDATHAASMTKILAREMGINVACAGTYCKHDADWFKEQVQGYCDEVLITDDHTEVGDLIARIEPSAIFGTQMERHIGKRLNIPCGVISAPVHIQNFPLGYRPFLGYEGTNQIADLVYNSFTLGMEDHLLEIFGGHDTKEVITKSLSTEEGLTWTSDAQAELSKIPGFVRGKIKRNTEKFARENNISEINIEVMYAAKESLNA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ422812
EMBL· GenBank· DDBJ
ABD62177.2
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp