P74132 · HEMN_SYNY3

Function

function

Involved in the heme and chlorophyll biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.

Catalytic activity

Cofactor

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

Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site60S-adenosyl-L-methionine 1 (UniProtKB | ChEBI)
Binding site66[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site70[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site72S-adenosyl-L-methionine 2 (UniProtKB | ChEBI)
Binding site73[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site117S-adenosyl-L-methionine 1 (UniProtKB | ChEBI)
Binding site118-119S-adenosyl-L-methionine 2 (UniProtKB | ChEBI)
Binding site150S-adenosyl-L-methionine 1 (UniProtKB | ChEBI)
Binding site177S-adenosyl-L-methionine 2 (UniProtKB | ChEBI)
Binding site189S-adenosyl-L-methionine 2 (UniProtKB | ChEBI)
Binding site214S-adenosyl-L-methionine 2 (UniProtKB | ChEBI)
Binding site248S-adenosyl-L-methionine 2 (UniProtKB | ChEBI)
Binding site334S-adenosyl-L-methionine 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functioncoproporphyrinogen dehydrogenase activity
Molecular Functioncoproporphyrinogen oxidase activity
Molecular Functionmetal ion binding
Biological Processchlorophyll biosynthetic process
Biological Processporphyrin-containing compound biosynthetic process
Biological Processprotoporphyrinogen IX biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Oxygen-independent coproporphyrinogen III oxidase
  • EC number
  • Short names
    CPO
  • Alternative names
    • Coproporphyrinogen III dehydrogenase (CPDH)

Gene names

    • Name
      hemN
    • Ordered locus names
      sll1876

Organism names

Accessions

  • Primary accession
    P74132

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene grow significantly slower than that of the wild-type under microoxic conditions, while they grow normally under aerobic conditions. Coproporphyrin-III is accumulated at a low but significant level in the mutant growing under microoxic conditions.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001099541-466Oxygen-independent coproporphyrinogen III oxidase

Proteomic databases

Expression

Induction

Induced under microoxic conditions.

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain51-285Radical SAM core

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    466
  • Mass (Da)
    53,161
  • Last updated
    1997-02-01 v1
  • Checksum
    D49735A905A5C572
MTTTFPTVEFSAELLNKYNQGIPRYTSYPPATELNKEFDPSDFQTAINLGNYKKTPLSLYCHIPFCAKACYFCGCNTIITQHKPAVDPYLKAVAKQIALVAPLVDQQRPVQQLHWGGGTPNYLTLEQAEFLFNTITDAFPLAENAEISIEINPCYVDKDYIFALRQLGFNRISFGIQDFNSQVQQAVNRIQPEAMLFQVMDWIRQANFDSVNVDLIYGLPHQNLATFRETLRKTAQLNPDRIAVFNFAYVPWLKPVQKKMPESALPPAEEKLKIMQATIADLTEQGYVFIGMDHFAKPDDELAIAQRRGELHRNFQGYTTQPESDLLGFGITSISMLQDVYAQNHKTLKAFYNALDREVMPIEKGFKLSQDDLIRRTVIKELMCQFKLSAQELESKYNLGFDCDFNDYFAKELSALDVLEADGLLRRLGDGLEVTPRGRILIRNIAAVFDTYLQNKSKQQMFSRAI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000022
EMBL· GenBank· DDBJ
BAA18218.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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