A0A2D2LUQ4 · A0A2D2LUQ4_MOROS
- ProteinSiroheme synthase
- GenecobA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids466 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 H+ + siroheme = Fe2+ + sirohydrochlorin
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: PS | ||||||
Active site | 257 | Proton acceptor | ||||
Sequence: D | ||||||
Active site | 279 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 310-312 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GGD | ||||||
Binding site | 315 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 340-341 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: TA | ||||||
Binding site | 392 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 421 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: A |
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
Including 3 domains:
- Recommended nameUroporphyrinogen-III C-methyltransferase
- EC number
- Short namesUrogen III methylase
- Alternative names
- Recommended namePrecorrin-2 dehydrogenase
- EC number
- Recommended nameSirohydrochlorin ferrochelatase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Moraxella
Accessions
- Primary accessionA0A2D2LUQ4
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 128 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-206 | Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase | ||||
Sequence: MNTLPLFFKLENRPVLVVGGGEVALRKADLLDKAGATITFVAPSYEPRLTAQFSDSRHQLINDVYQQKYLDKQTIVIACTDDETVNAQIFHDCEDRFIPVNVVDNPPLCTFIFPAIVDRNPITIAVSSAGKAPVLARLLRAKIETVVPPQYGELAGLAGKFRDKVKAALPNVTARRKFWEQAFEGQVAESVFEGNTNSLSKAENQL | ||||||
Domain | 119-144 | Siroheme synthase central | ||||
Sequence: RNPITIAVSSAGKAPVLARLLRAKIE | ||||||
Domain | 151-202 | Sirohaem synthase dimerisation | ||||
Sequence: YGELAGLAGKFRDKVKAALPNVTARRKFWEQAFEGQVAESVFEGNTNSLSKA | ||||||
Region | 225-466 | Uroporphyrinogen-III C-methyltransferase | ||||
Sequence: GKVYIVGAGAGDPDLLTFKALRLMQQADVVFYDNLVSAQILDLCRRDATKIYVGKKASDHAVRQEKINELLVEQAQQGQRVLRLKGGDPYVFGRGGEEAEALVAAGVDFEVVPGITAATAAASCAGIPLTHREYAHSVKFVTASLKTDTINEDFASWLDDNQTVVFYMGLKQLDKLTRGLIDAGKNPSTPIAIVSNASLPHQQVLTGTLETIVAKQAEANLPAPAILIMGNVVKLHHRLNKR | ||||||
Domain | 226-436 | Tetrapyrrole methylase | ||||
Sequence: KVYIVGAGAGDPDLLTFKALRLMQQADVVFYDNLVSAQILDLCRRDATKIYVGKKASDHAVRQEKINELLVEQAQQGQRVLRLKGGDPYVFGRGGEEAEALVAAGVDFEVVPGITAATAAASCAGIPLTHREYAHSVKFVTASLKTDTINEDFASWLDDNQTVVFYMGLKQLDKLTRGLIDAGKNPSTPIAIVSNASLPHQQVLTGTLETI |
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 statusComplete
- Length466
- Mass (Da)50,857
- Last updated2018-01-31 v1
- ChecksumE4DC2EEE578E5DBE