A0A4Q2ECR2 · A0A4Q2ECR2_ENTCL

  • 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 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
      cobA
    • Synonyms
      cysG
    • ORF names
      DM877_03825

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • GEO_4_Eff_A
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Enterobacter > Enterobacter cloacae complex

Accessions

  • Primary accession
    A0A4Q2ECR2

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue109Phosphoserine

Keywords

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    452
  • Mass (Da)
    48,893
  • Last updated
    2019-07-31 v1
  • Checksum
    0222AF5EBAF37FDB
MDYLPLFAAIKDKPVLVVGTGEIADRKIVFLQRAGAQVRVVAGADFDESQIDSVVLVIAATDDRELNRRISDAAQARYRLVNVVDDQSLCSFIFPSIVDRSPLLVAISSGGTAPVLARVLREKIEALLPTSLGRMAEKASYWRNHLKTRLTSVTERRRFWERVFRGRFASLMHAGNETAAQKILEDELDNPGSTGGEIILVGAGPGDAGLLTLRGLQVLQDADVVFYDHLVTDGIRELIRRDAEQICVGKRAGEHSVPQHDTNQMLVDAAKAGKTVVRLKGGDPFIFGRGGEELQAAAEAGVPFQVVPGITAASAVTAYAGIPLTHRDYAQSVTFVTGHYKADSTPFDWSHLAQSRQTLAIYMGTMKAADISEQLIQHGREAKTPVAVISRGTRVDQHVAIGTLDDLATLAKDAPMPALIVVGEVVQLHSTLAWFQHTTDTEGFGSSVINLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QJSL01000003
EMBL· GenBank· DDBJ
RXW30152.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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