A0A377NHH8 · A0A377NHH8_9GAMM

  • Protein
    Siroheme synthase
  • Gene
    cysG_2
  • 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.

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 site226S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site249Proton acceptor
Active site271Proton donor
Binding site302-304S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site307S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site332-333S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site384S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site413S-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
      cysG_2
    • Synonyms
      cysG
    • ORF names
      NCTC12157_03963

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NCTC12157
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Ewingella

Accessions

  • Primary accession
    A0A377NHH8

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
Domain124-144Siroheme synthase central
Domain150-207Sirohaem synthase dimerisation
Region217-474Uroporphyrinogen-III C-methyltransferase
Domain219-428Tetrapyrrole 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
    474
  • Mass (Da)
    51,284
  • Last updated
    2018-11-07 v1
  • Checksum
    12BBD22716D69D6B
MDYLPIFADLRQRPVLVVGGGEIAARKIDLLLRAGAAVRIVAQSLSSELEHRLQQSQVSWLAKQFEPQQLDDVFLVIAATDDAALNAEVFEQANRRQLLANVVDDQPKCSFIFPSIVDRSPIVVAISSSGTAPVLARMLREKLETLLPTSLGKMAEIAGSFRDRVKQRFSSMTARRRFWEQTFDGRFASLVTAGQIPEAEQVLQQQLDNPESISRNGEVTLVGAGPGDAGLLTLRGLQVMQQADVVLYDHLVSDEILDLVRRDADRICVGKRAGSHSVVQEETNRMLVELAQQGKKVVRLKGGDPFIFGRGGEELQAVSAAGIPFQVVPGVTAAAGATAYAGIPLTHRDYAQCVMFITGHSRPDGNGMQWETLAKGNQTLAIYMGTVKAAEISQQLIAHGRAASTPVAVIGRGTRVDQQVLTGTLDNLELLAQQAPTPALLVIGEVVALHDKLAWFGHQPQTDDAVRPSVVNLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UGGO01000001
EMBL· GenBank· DDBJ
STQ46192.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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