A0AA91FHX3 · A0AA91FHX3_MOROS

  • Protein
    Siroheme synthase
  • Gene
    cysG
  • 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)
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
      cysG
    • ORF names
      A9299_04320

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CCUG 67237
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Moraxella

Accessions

  • Primary accession
    A0AA91FHX3

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
Domain151-200Sirohaem synthase dimerisation
Region225-467Uroporphyrinogen-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
    467
  • Mass (Da)
    50,800
  • Last updated
    2024-03-27 v1
  • Checksum
    6604F99C335924C5
MNTLPLFFKLENRPVLVVGGGEVALRKADLLDKAGATITFVAPSYEPRLTAQFSDSRHQLINDVYQQKYLDKQTIVIACTDDETVNAQIFHDCEARFIPVNVVDNPPLCTFIFPAIVDRNPITIAVSSAGKAPVLARLLRANIETVVPPQYGELAGLAGKFRDKVKAALPNVTARRKFWEQAFEGQVAESVFEGNSNSLSKAEAQLEILLQQHANNQPTNKAQLGKVYIVGAGAGDPDLLTFKALRLMQQADVVFYDNLVSAQILDLCRRDATKIYVGKKASDHAVRQEKINELLVEQAQQGQRVLRLKGGDPYVFGRGGEEAEALVAAGIEFEVVPGITAATAAASCAGMPLTHRAYAHSVKFVTASLKTDTINEDFASWLDDNQTVVFYMGLKQLDKLTSGLINAGKNPSTPIAIVSNASLPHQQVLTGTLETIVAKQREANLPAPAILIMGNVVKLHHRLNKLS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LZMT01000034
EMBL· GenBank· DDBJ
OBX62424.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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