A0A0H3I8A0 · A0A0H3I8A0_PECPM

Function

function

Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.

Catalytic activity

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.
Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site22-23NAD+ (UniProtKB | ChEBI)
Binding site43-44NAD+ (UniProtKB | ChEBI)
Binding site231S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site254Proton acceptor
Active site276Proton donor
Binding site307-309S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site312S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site337-338S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site389S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site418S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionNAD binding
Molecular Functionprecorrin-2 dehydrogenase activity
Molecular Functionsirohydrochlorin ferrochelatase activity
Molecular Functionuroporphyrin-III C-methyltransferase activity
Biological Processcobalamin biosynthetic process
Biological Processmethylation
Biological Processsiroheme biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Siroheme synthase

Including 3 domains:

  • Recommended name
    Uroporphyrinogen-III C-methyltransferase
  • EC number
  • Short names
    Urogen III methylase
  • Alternative names
    • SUMT
    • Uroporphyrinogen III methylase
      (UROM
      )
  • Recommended name
    Precorrin-2 dehydrogenase
  • EC number
  • Recommended name
    Sirohydrochlorin ferrochelatase
  • EC number

Gene names

    • Name
      cobA
    • Synonyms
      cysG
    • ORF names
      C5E00_12360
    • Ordered locus names
      W5S_3660

Organism names

  • Taxonomic identifier
  • Strains
    • SCC3193
    • IFB5626
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Pectobacteriaceae > Pectobacterium

Accessions

  • Primary accession
    A0A0H3I8A0

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue128Phosphoserine

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-203Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain119-145Siroheme synthase central
Domain150-207Sirohaem synthase dimerisation
Region222-480Uroporphyrinogen-III C-methyltransferase
Domain224-433Tetrapyrrole methylase

Sequence similarities

Belongs to the precorrin methyltransferase family.
In the C-terminal section; belongs to the precorrin methyltransferase family.
In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    480
  • Mass (Da)
    51,702
  • Last updated
    2015-09-16 v1
  • Checksum
    076CFE0B4D804677
MNYLPIFADLRQRPVLVVGGGEVATRKIDLLQRAGAEVKIVAQALAEPLAAQHQAGQVEWLAHAFTPELLSGVFLVIAATDDAELNAAVFDAANQRHLLVNVVDDQPKCSFIFPSIVDRSPLVVAISSGGQAPVLARLLREKLESLLPASLGTMADIAGGWRNRIKTRLHSMSDRRRFWERLFVGRFASLVSAGQLEQAEDELQQQLVNQQDEQQLPASARGEVALVGAGPGDAGLLTLRGLQVMQQADVVLYDHLVSADVLDLVRRDAERICVGKRASAHSLPQDGINQLLVKLAQEGKRVVRLKGGDPFIFGRGGEELQAVAQAGISFQVVPGVTAAAGVTAYAGIPLTHRDYAQSVIFITGHCRPDGDALDWSTLARGRQTLAIYMGTMKAAEISQQLIAHGRSAQTPVAVIGRGTRHDQQVQIGTLQELEHLARQAPTPALLVIGEVVDLHHQIAWFGQTTPTVPQDSRPAVVNLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003415
EMBL· GenBank· DDBJ
AFI91723.1
EMBL· GenBank· DDBJ
Genomic DNA
PSZG01000001
EMBL· GenBank· DDBJ
RKO77520.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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