A0A225CCL5 · A0A225CCL5_9MICO
- ProteinDeferrochelatase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids442 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the protoporphyrin ring intact.
Catalytic activity
- heme b + 2 H+ = protoporphyrin IX + Fe2+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per subunit.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ferrochelatase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | peroxidase activity | |
Biological Process | iron import into cell |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDeferrochelatase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Clavibacter
Accessions
- Primary accessionA0A225CCL5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-22 | Disordered | ||||
Sequence: MRDTADALEDPSAPTAPAAPRG | ||||||
Domain | 73-233 | Dyp-type peroxidase N-terminal | ||||
Sequence: QAGITTPAQDRLHFAAFDVADIDRDGLVSLLRDWSAAAARMTAGGSAGALGAVDGAYDSPPDDTGEALDLPPAGLTITFGLGPSLFTTADGVDRFGIADRRPAALVDLPRFPGEALVPQATGGDLCVQACSDDPQVAVHAIRNLSRIAFGRASLRWSQLGF | ||||||
Domain | 245-429 | Dyp-type peroxidase C-terminal | ||||
Sequence: TPRNLFGFKDGTANVKSEDTRVVDEHVWADAGSAPGEAWMEGGSYLVARRIRMTVETWDRSSLREQERVVGRTKGSGAPLSGGEEHTAPDFAATGRGGAPLIDPASHVRLAHPDANAGAVLLRRGYNFVDGNDDLGRLNAGLFFLAFQRDPRTQFIPIQRSLAKDAMNEYLRHVGSGIWAVPPGA | ||||||
Region | 310-330 | Disordered | ||||
Sequence: QERVVGRTKGSGAPLSGGEEH |
Sequence similarities
Belongs to the DyP-type peroxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length442
- Mass (Da)45,936
- Last updated2017-10-25 v1
- ChecksumB764CED5C505864F