A0A013THM9 · A0A013THM9_9GAMM

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 site225S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site248Proton acceptor
Active site270Proton donor
Binding site301-303S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site306S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site331-332S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site383S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site412S-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
      J663_3184

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 826659
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex

Accessions

  • Primary accession
    A0A013THM9

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue129Phosphoserine

Keywords

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-204Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain152-208Sirohaem synthase dimerisation
Region216-457Uroporphyrinogen-III C-methyltransferase
Domain218-427Tetrapyrrole 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
    457
  • Mass (Da)
    50,265
  • Last updated
    2014-06-11 v1
  • Checksum
    56FC056BD5BA3C8E
MDIFPISLKLQQQHCLIVGGGHIALRKANLLAKAGAVIDIIAPAIEEQLLQLVKTTGGEYFAESFAEKILNTPYRLVIAATNDAQVNKAVFEQCEARNLLVNSVDDIPHCRFMVPAIIDRSPLIISVASNGASPVLSRQLRTQIETIVPHGMGKLAEFSGQWRKQVKEKIPNPDERRIFWENLYASPLKEQVFNDNLEVANGLIQQALTEWTAPKGEVYLVGAGPGDPELLTLKALRLMQQADVVIYDRLVSAPILELCRRDATKIYVGKARSNHSVPQDGINALLVEYAQKGKRVCRLKGGDPFIFGRGGEEIQELVEANVTFQVVPGITAASGCSAYAGIPLTHRDYAQSVRFLTGHLKEGSPELPWNELVYENQTLVLYMGLVGLERICEQLIAHGQRADMPVALISKGTTPDQKVVVGTLADIATKVSEHHIVAPTLTIIGEVVNLREQLKWQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JFYD01000007
EMBL· GenBank· DDBJ
EXS32836.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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