A0A1S2ADF6 · A0A1S2ADF6_9ENTR

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 site205S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site228Proton acceptor
Active site250Proton donor
Binding site281-283S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site286S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site311-312S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site363S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site392S-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
    • Synonyms
      cobA
    • ORF names
      ABF77_19580
      , B9059_003575

Organism names

  • Taxonomic identifier
  • Strains
    • GN02692
    • CRK0054
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Enterobacter > Enterobacter cloacae complex

Accessions

  • Primary accession
    A0A1S2ADF6

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue109Phosphoserine

Keywords

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-184Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain100-126Siroheme synthase central
Domain131-188Sirohaem synthase dimerisation
Region196-452Uroporphyrinogen-III C-methyltransferase
Domain198-408Tetrapyrrole 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
    452
  • Mass (Da)
    48,951
  • Last updated
    2017-04-12 v1
  • MD5 Checksum
    5F4D0A43B7E8DBF166C091E28DCB47C2
MDYLPLFAAIKEKPVLVVGTGEIADRKIAFLQRAGAQVQVVEETDFDESQIDSVVLVIAATDDRELNQRISDAAQARYRLVNVVDDQPLCSFIFPSIVDRSPLLVAISSGGTAPVLARVLREKIEALLPTSLGRMAEKASYWRNHLKTRLTSVTERRRFWERVFRGRFASLMHAGNETAAQKILEDELDNPGSTGGEIILVGAGPGDAGLLTLRGLQVLQDADVVFYDHLVTDGVRELIRRDAEQICVGKRAGEHSVPQHDTNQMLIDAAKAGKTVVRLKGGDPFIFGRGGEELQAAAEAGVPFQVVPGITAASAVTAYAGIPLTHRDYAQSVTFVTGHYKADSTPFDWSHLAQSRQTLAIYMGTMKAADISEQLIQHGREATTPVAVISRGTRVDQHVAVGTLQDLATLAKDAPMPALIVVGEVVQLHSTLAWFQHTTDTEGFGSSVVNLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LEDI01000106
EMBL· GenBank· DDBJ
KLP91782.1
EMBL· GenBank· DDBJ
Genomic DNA
NEYZ02000017
EMBL· GenBank· DDBJ
RNT47470.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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