A0A357I7K6 · A0A357I7K6_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

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)
Binding site228S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site251Proton acceptor
Active site273Proton donor
Binding site304-306S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site309S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site334-335S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site386S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site415S-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
      DD979_00880

Organism names

Accessions

  • Primary accession
    A0A357I7K6

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-204Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase
Domain120-146Siroheme synthase central
Domain151-207Sirohaem synthase dimerisation
Region219-487Uroporphyrinogen-III C-methyltransferase
Domain221-430Tetrapyrrole 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
    487
  • Mass (Da)
    52,779
  • Last updated
    2018-11-07 v1
  • Checksum
    27B16389AA1A8710
MNYLPLCLKLDDKPCLVVGAGAVGARKIAYLRHSGARVVVVAPTLSEDVLAQVADADGITLHQRAFRERDITGKQLVIAASSSPDVNAEVARLCRASGVPVNVVDDTDACTFVVPAVIHRGPVQVAISTGGASPVLARTLKMRLESYIPSAYGDLASLVQRYRQAVKHAFHAVRERKHFWERVLEGPIAELVFAGRLTEAEHSLKAAVANPQSASQEQGEVYLVGAGPGDPDLLTLRALRLMQQADVVVYDRLVSPPIIDMVRANAQRIYAGKKKSDHAIPQGGINALLVQLAREGKRVLRLKGGDPFIFGRGGEEIQTLIDEGVAFQIVPGVTAASGCATYSGIPLTHRDHSQACIFVTGHLKDGTSDLNWDMLANEQQTVVFYMGLQGVDVICRELIAHGRKATTPAALIQQGTTPSHRVLIGDLNSLPALVRSNDVRAPTLIIVGEVVSLHEKLKWFRPGEELIAPAVRDMHDYFEHSHKRHKS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DOIU01000022
EMBL· GenBank· DDBJ
HBR95919.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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