A0A9D6JL83 · A0A9D6JL83_9GAMM

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

Type
IDPosition(s)Description
Binding site22-23NAD+ (UniProtKB | ChEBI)
Binding site43-44NAD+ (UniProtKB | ChEBI)
Binding site227S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site250Proton acceptor
Active site272Proton donor
Binding site303-305S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site308S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site333-334S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site385S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site414S-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

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
      HYZ31_08785

Organism names

Accessions

  • Primary accession
    A0A9D6JL83

Proteomes

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-203Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain119-144Siroheme synthase central
Domain150-207Sirohaem synthase dimerisation
Region218-474Uroporphyrinogen-III C-methyltransferase
Domain220-429Tetrapyrrole 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    474
  • Mass (Da)
    51,369
  • Last updated
    2023-05-03 v1
  • Checksum
    EC6B5DF12A55D47E
MDFLPIFVNIRQQPCLVVGGGEVAARKVSLLLKAGAAVTVVSPRLSHELADMLKAGAISHAARDFADADIKQPVLVIAATDNRMVNQHVSELARARGIPVNVVDSPELCSFIMPSIVDRSPMQIAISTGGASPVLARMIRTKLEGCIPAGYGRLAALVDGFREKVKARFTDVNQRRMFWESVLEGSVAERVFAGHEDEAAAELDKAIAAGDARGEFKGEVYLVGAGPGDPDLLTFRALRLMQAADVVVYDRLVAPAIMELVRRDAELIYVGKERDNHTMRQENINQLLVRLAQEGKRVLRLKGGDPFIFGRGGEEIETLAENGVAFQVVPGITAAAGCAAYSGIPLTHRDYSQACVFVTGHLKDGSIDLNWKALAQPNQTVVFYMGLHGAPELCKNMIAHGLPPSTPVALVQKGTTPEHKTIIATLETLVETVRKNDLKPPTLIIVGEVVKLHEKLDWFDPHKPQGRAVKAGQW

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACPVK010000308
EMBL· GenBank· DDBJ
MBI3187939.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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