A0A653QMR0 · A0A653QMR0_9GAMM

  • 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

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 site224S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site247Proton acceptor
Active site269Proton donor
Binding site300-302S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site305S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site330-331S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site382S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site411S-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
      HU668_17490
      , PANT111_140158

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • Pantoea sp. 111
    • IF5SW-B1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Pantoea

Accessions

  • Primary accession
    A0A653QMR0

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue128Phosphoserine

Keywords

Structure

3D structure databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-203Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain119-144Siroheme synthase central
Domain150-207Sirohaem synthase dimerisation
Region215-471Uroporphyrinogen-III C-methyltransferase
Domain217-426Tetrapyrrole 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
    471
  • Mass (Da)
    50,953
  • Last updated
    2020-04-22 v1
  • Checksum
    86CD5057CF6039B3
MDYLPLFADLSGRPVLVVGGGDIAARKIELLRRARARVQIAARELCPELQALLETQQLEWLATAFDPAQLDGVFLVIAATDDNALNAAVFEAANARQKLVNVVDDQPKCSFIFPSIVDRSPLVVAISSSGTAPVLARMLREKLETLLPANLGQMAEVAGQWRDKVKQRFHRMSDRRRFWERAFNGLFASQMSAGNVDEAKRTLDRELLDEPGRQGEIILVGAGPGDSGLLTLRGLQVMQLADVVLYDHLVSDEVLELVRRDADRICVGKRAGAHSVPQEETNQMLVKLALQGKRVVRLKGGDPFIFGRGGEELQAAQQAGIPFQVVPGVTAAAGATAYAGIPLTHRDYAQSVMFITGHCRPDGDDIDWPSLARARQTLAIYMGTVKAALISEALIQHGRAPSTPVAVISRGTRQDQQVVTGTLEQLEALAASAPTPALLVIGEVVNLHGQLAWFQHSAQQGARESAVVNLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABWPM010000023
EMBL· GenBank· DDBJ
NUY98254.1
EMBL· GenBank· DDBJ
Genomic DNA
CABWMH010000006
EMBL· GenBank· DDBJ
VXB44142.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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