A0A3V8D4W4 · A0A3V8D4W4_SALET

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

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 site225S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site248Proton acceptor
Active site270Proton donor
Binding site301-303S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site306S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site331-332S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site382S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site411S-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
      BG172_17010
      , CB215_06835
      , CR347_19145
      , E0S65_06195
      , G0D41_23400
      , G0D54_04570
      , G4I76_002475
      , G4I81_004043
      , G4P10_000389
      , G4P17_003696
      , G4P47_003052
      , GNB84_002636
      , GND62_002190

Organism names

Accessions

  • Primary accession
    A0A3V8D4W4

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue128Phosphoserine

Keywords

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-204Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain119-145Siroheme synthase central
Domain150-207Sirohaem synthase dimerisation
Region216-457Uroporphyrinogen-III C-methyltransferase
Domain218-426Tetrapyrrole 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
    457
  • Mass (Da)
    50,128
  • Last updated
    2019-05-08 v1
  • Checksum
    5B2A57B48D62A3AF
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFTVWANEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSEAAESRRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAVNATTEHLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCHAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQEKLIAFGMQADMPVALVENGTSVKQRVVHGVLTQLGELAQQVESPALIIVGRVVGLRDKLNWFSNH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAIOLQ010000003
EMBL· GenBank· DDBJ
ECG4536295.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKJZK010000005
EMBL· GenBank· DDBJ
ECS5603235.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKROK010000005
EMBL· GenBank· DDBJ
ECU9523551.1
EMBL· GenBank· DDBJ
Genomic DNA
AAMICF010000004
EMBL· GenBank· DDBJ
EDH5773465.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAMJC010000002
EMBL· GenBank· DDBJ
HAC6864488.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAMJS010000018
EMBL· GenBank· DDBJ
HAC6950056.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAREJ010000005
EMBL· GenBank· DDBJ
HAE2084125.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASLT010000005
EMBL· GenBank· DDBJ
HAE6050722.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASMX010000049
EMBL· GenBank· DDBJ
HAE6183269.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASVX010000005
EMBL· GenBank· DDBJ
HAE7247668.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASXX010000002
EMBL· GenBank· DDBJ
HAE7516042.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASYM010000016
EMBL· GenBank· DDBJ
HAE7550757.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASZT010000003
EMBL· GenBank· DDBJ
HAE7704072.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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