A0A066ZYM1 · A0A066ZYM1_HYDMR

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 site234S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site257Proton acceptor
Active site279Proton donor
Binding site310-312S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site315S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site340-341S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site392S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site421S-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
      cysG
    • ORF names
      EI16_03910

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MH-110
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Thiotrichales > Piscirickettsiaceae > Hydrogenovibrio

Accessions

  • Primary accession
    A0A066ZYM1

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-209Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain127-151Siroheme synthase central
Domain157-213Sirohaem synthase dimerisation
Region225-484Uroporphyrinogen-III C-methyltransferase
Domain227-436Tetrapyrrole 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
    484
  • Mass (Da)
    52,445
  • Last updated
    2014-09-03 v1
  • Checksum
    DB4658D4EE804930
MDYLPIFMNIKQQACLIVGGGVVAARKADLFIQSGAQVMVIAPALKSEMQSFLNQNKVTWHQGVFSPKVMADVFGEQLPKLVISATDNQAVNIAVYEYCQAAGIPVNVADQTEYCDFILPAIVDRAPMTIAISTGGRSPVLARVMKAKLETMIPHGFGRLTDLVGRYRDKVKAAISSIDGRKAFWESLLDGLFIDKAVHGLDGEAEALLEKKLEQADNFEEAAVGEVYVIGAGPGDPELMTFKAQRLLQQADVVLYDRLVSPEIVDMARREAERVYVGKKSKHHAVPQEDICRMLVEYAKQGKKVARLKGGDPYIFGRGGEEVEILAKAGVAYQVVPGITAAAGCAAYADFPLTHREFSQSVALVTGHQQEGGNAIDYGRLAHSGDTMVFYMGIKNAPKIQAGLIAHGMNPGTPAAIIERGTRADQKVTVSSLGKLTETIAKQAIKPPALLVVGEVVKVRERIQNAKRFVQQAEQSPPLHRVAV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JMIU01000001
EMBL· GenBank· DDBJ
KDN95456.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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