A8G9Y3 · CYSG1_SERP5
- ProteinSiroheme synthase 1
- GenecysG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids476 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- 2 S-adenosyl-L-methionine + uroporphyrinogen III = H+ + precorrin-2 + 2 S-adenosyl-L-homocysteine
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 | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 22-23 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EV | ||||||
Binding site | 43-44 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QS | ||||||
Binding site | 228 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Active site | 251 | Proton acceptor | ||||
Sequence: D | ||||||
Active site | 273 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 304-306 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GGD | ||||||
Binding site | 309 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 334-335 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: TA | ||||||
Binding site | 386 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 415 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NAD binding | |
Molecular Function | precorrin-2 dehydrogenase activity | |
Molecular Function | sirohydrochlorin ferrochelatase activity | |
Molecular Function | uroporphyrin-III C-methyltransferase activity | |
Biological Process | cobalamin biosynthetic process | |
Biological Process | methylation | |
Biological Process | siroheme biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSiroheme synthase 1
Including 3 domains:
- Recommended nameUroporphyrinogen-III C-methyltransferase 1
- EC number
- Short namesUrogen III methylase 1
- Alternative names
- Recommended namePrecorrin-2 dehydrogenase 1
- EC number
- Recommended nameSirohydrochlorin ferrochelatase 1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia
Accessions
- Primary accessionA8G9Y3
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000330557 | 1-476 | Siroheme synthase 1 | |||
Sequence: MDYLPIFADLKQRPVLVVGGGEVAARKVDLLLRAGAEIRIVAQSLSPILEQLSQQGQIHWLGQAFAAEQLDEVFLVIAATDDSALNAEVFSEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARMLREKLEALLPASLGQMAEVAGRWRGQVKQRLNAIGERRRFWEKTFGGRFATLVANGQTAEAQRQLEQDLEQFAQGSEGTQGEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSDEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDGLDWADLARARQTLAIYMGTMKAADISQRLIAHGRAATTPVAVISRGTRADQLVQTGTLQQLEQLAQQAPLPALLVIGEVVELHHQIAWFGHQPQAEGVSRPAVVNLA | ||||||
Modified residue | 128 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-203 | Precorrin-2 dehydrogenase /sirohydrochlorin ferrochelatase | ||||
Sequence: MDYLPIFADLKQRPVLVVGGGEVAARKVDLLLRAGAEIRIVAQSLSPILEQLSQQGQIHWLGQAFAAEQLDEVFLVIAATDDSALNAEVFSEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARMLREKLEALLPASLGQMAEVAGRWRGQVKQRLNAIGERRRFWEKTFGGRFATLVANGQTAEAQRQL | ||||||
Region | 219-476 | Uroporphyrinogen-III C-methyltransferase | ||||
Sequence: GEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSDEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDGLDWADLARARQTLAIYMGTMKAADISQRLIAHGRAATTPVAVISRGTRADQLVQTGTLQQLEQLAQQAPLPALLVIGEVVELHHQIAWFGHQPQAEGVSRPAVVNLA |
Sequence similarities
In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
In the C-terminal section; belongs to the precorrin methyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length476
- Mass (Da)51,267
- Last updated2007-11-13 v1
- Checksum2DAB7E09F9A3B2B9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000826 EMBL· GenBank· DDBJ | ABV39923.1 EMBL· GenBank· DDBJ | Genomic DNA |