A0AAD0AE24 · A0AAD0AE24_MOROS

  • 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.

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)
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

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
      YHS_05930

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • YHS
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Moraxella

Accessions

  • Primary accession
    A0AAD0AE24

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue128Phosphoserine

Keywords

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-206Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain119-144Siroheme synthase central
Domain151-201Sirohaem synthase dimerisation
Region225-466Uroporphyrinogen-III C-methyltransferase
Domain226-436Tetrapyrrole 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
    466
  • Mass (Da)
    50,689
  • Last updated
    2024-05-29 v1
  • Checksum
    7DD354BDB9E756BC
MNTLPLFFKLENRPVLVVGGGEVALRKADLLDKAGATITFVAPSYEPRLTAQFSDSRHQLINDVYQQKYLDKQTIVIACTDDETVNAQIFHDCEARFIPVNVVDNPPLCTFIFPAIVDRNPITIAVSSAGKAPVLARLLRAKIETVVPPQYGELAGLAGKFRDKVKAALPNVTARRKFWEQAFEGQVAESVFEGNSNSLSKAESQLETLLQQHANNQPTDKAQLGKVYIVGAGAGDPDLLTFKALRLMQQADVVFYDNLVSAQILDLCRRDATKIYVGKKASDHAVRQEKINELLVEQAQQGKRVLRLKGGDPYVFGRGGEEAEQLVAAGIDFEVVPGITAATAAASCAGIPLTHRAYAHSVKFVTASLKTDTINEDFASWLDDSQTVVFYMGLKQLDKLTSGLIDAGKNPSTPIAIVSNASLPHQQVLTGTLETIVAKQAEANLPAPAILIMGNVVKLHHRLNKR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP024176
EMBL· GenBank· DDBJ
ATQ83401.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp