A0A351XP33 · A0A351XP33_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.

TypeIDPosition(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
      DCG40_01275
      , DCG46_00560
      , DCL02_00290
      , DCM52_05025
      , DCQ55_01270
      , DCQ62_05030
      , DCQ65_01625
      , DCQ66_00010
      , DCQ71_02410
      , DCQ74_02855
      , DD382_04285
      , DDW63_04190
      , DEP15_05360
      , DEU86_04000
      , DGE70_04340
      , DHI05_01315

Organism names

  • Taxonomic identifier
  • Strains
    • UBA10975
    • UBA11104
    • UBA11330
    • UBA11335
    • UBA8370
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria

Accessions

  • Primary accession
    A0A351XP33

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
Region1-203Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain124-145Siroheme synthase central
Domain150-207Sirohaem synthase dimerisation
Region216-462Uroporphyrinogen-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
    462
  • Mass (Da)
    50,397
  • Last updated
    2018-11-07 v1
  • Checksum
    82D08BA0DC3DB415
MNYLPIFIDITQQPCLVVGGGDIALRKINLLLKANAAVTCVSKECCNGIEKLVKDNKIIRIEKAFEATDINAQVLIVSATDDSDLNAQVSALAKTANIPVNVVDSPDLCSFVMPSIVDRSPIVIAISSAGKAPVLARLIRAKLESTIPHAYGKLAELAGNFRDQVKAKFNNIEDRRYFWEKTFSGIVAEKVFSGKVDEAKADLQAQLDGSTDSGIGEVYLVGGGPGDPDLLTFKALRLMQQADVILYDRLVSDGVMELVRRDAELIYVGKERDNHAVPQGDINQLLVDLAKQGRRVCRLKGGDPFIFGRGGEEIETLAENNIPFQVVPGITAASGCSAYSGIPLTHRDYSQSCRFVTGHLKDGSMNLPWDELAVEQQTIVFYMALVGARHLSEQLISHGMRGDMPVALVEKGTTPDHQVYVTTLAELPNLVENTTIHAPTLIIIGEVVKLREKLNWFDADND

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DMBH01000028
EMBL· GenBank· DDBJ
HAD99074.1
EMBL· GenBank· DDBJ
Genomic DNA
DMBK01000009
EMBL· GenBank· DDBJ
HAE70079.1
EMBL· GenBank· DDBJ
Genomic DNA
DMDS01000008
EMBL· GenBank· DDBJ
HAG47336.1
EMBL· GenBank· DDBJ
Genomic DNA
DMQZ01000024
EMBL· GenBank· DDBJ
HAO44475.1
EMBL· GenBank· DDBJ
Genomic DNA
DMRA01000124
EMBL· GenBank· DDBJ
HAO53896.1
EMBL· GenBank· DDBJ
Genomic DNA
DMRD01000050
EMBL· GenBank· DDBJ
HAO70285.1
EMBL· GenBank· DDBJ
Genomic DNA
DMRG01000076
EMBL· GenBank· DDBJ
HAO97890.1
EMBL· GenBank· DDBJ
Genomic DNA
DMRF01000064
EMBL· GenBank· DDBJ
HAP05563.1
EMBL· GenBank· DDBJ
Genomic DNA
DMRE01000001
EMBL· GenBank· DDBJ
HAP44802.1
EMBL· GenBank· DDBJ
Genomic DNA
DMJS01000116
EMBL· GenBank· DDBJ
HAP92831.1
EMBL· GenBank· DDBJ
Genomic DNA
DNRK01000101
EMBL· GenBank· DDBJ
HBG03696.1
EMBL· GenBank· DDBJ
Genomic DNA
DOBR01000126
EMBL· GenBank· DDBJ
HBN58491.1
EMBL· GenBank· DDBJ
Genomic DNA
DOWW01000119
EMBL· GenBank· DDBJ
HCA68786.1
EMBL· GenBank· DDBJ
Genomic DNA
DPFW01000094
EMBL· GenBank· DDBJ
HCH58704.1
EMBL· GenBank· DDBJ
Genomic DNA
DPMG01000119
EMBL· GenBank· DDBJ
HCV74928.1
EMBL· GenBank· DDBJ
Genomic DNA
DPPC01000045
EMBL· GenBank· DDBJ
HCW71725.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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