A0A4U0YAK9 · A0A4U0YAK9_9GAMM

  • Protein
    Siroheme synthase
  • Gene
    cobA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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.

TypeIDPosition(s)Description
Binding site22-23NAD+ (UniProtKB | ChEBI)
Binding site43-44NAD+ (UniProtKB | ChEBI)
Binding site226S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site249Proton acceptor
Active site271Proton donor
Binding site302-304S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site307S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site332-333S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site384S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site413S-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
      FAZ79_08940

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SB14A
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Thioalkalibacteraceae > Guyparkeria

Accessions

  • Primary accession
    A0A4U0YAK9

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-203Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain120-144Siroheme synthase central
Domain151-205Sirohaem synthase dimerisation
Region217-483Uroporphyrinogen-III C-methyltransferase
Domain219-428Tetrapyrrole 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
    483
  • Mass (Da)
    51,664
  • Last updated
    2019-07-31 v1
  • Checksum
    87688A2F81140F23
MDQLPIFMNLRGKPCLVVGGGAVAARKADLMRAAGARVTVVSPMITGETRRMVDDGRLTWQEAVFDPAMVVGNRLVIAATDEPQVNHSVFDACEARGIPVNVADEPDLCSFILPGIVDRSPVTIALSTGGRSPVLARLMRARLETLIPAGFGRLADLLGRYRQRAKDRILGLETRKRFWEDVIDGPIGNLVLAGKDREAEDKLAGLLDDREAPTDTGEVYLIGAGPGDPDLLTFRALRLLQKADVVVYDRLVAPAIVDLARREAERIYVGKRAGNHSCSQGDISGLLRDLAAEGKRVARLKGGDPFIFGRGGEEIDVLARAGLPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHRRGERLDLDWQHLASGQDTLVFYMGLGNAREICAQLIAHGMPADRGAGLVEHGTTSRQQVHVGTLATLPDRIAAAQSPALLIIGDVVGLHSRLAWFEGSASADPSFLSGSIEQSDPLSVRSAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SWAW01000023
EMBL· GenBank· DDBJ
TKA88732.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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