Detail Information for IndEnz0018001219
IED ID IndEnz0018001219
Enzyme Type ID peroxidase001219
Protein Name Deferrochelatase
EC 4.99.1.1
Peroxidase EfeB
EC 1.11.1.-
Gene Name efeB YPN_2267 YP516_2548
Organism Yersinia pestis bv. Antiqua (strain Nepal516)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Yersiniaceae Yersinia Yersinia pseudotuberculosis complex Yersinia pestis Yersinia pestis bv. Antiqua (strain Nepal516)
Enzyme Sequence MRDKTGPKFGPYQPDDEAVSPSRRRLILGMGMVSGALVLGGAKTAQAADCRSPDVAGTQDERWQKQPFYGQHQAGVLTPQQAAMMLVAFDVLATDKTSLIRLFKLLTERLAFLTTGGRAPSVNAKLPPLDSGIMGPEIYPDNLTVTVSVGNALFDERFGLQGQKPLRLQRMTRFPNDSLDAGLCHGDVMLQICANTNETVIHALRDIIKHTPDLLSVRWKREGFISAHAARSKGQDTPINLLGFKDGTANPKISNKPLINNVVWVSNNAGEPAWAVGGSYQVVRIIRFKVEFWDRTPLQEQQTIFGRDKNSGAPLGMQHEHDEPNYAKDPEGKVIPMDAHIRLANPRTIETQRNLMLRRGYSYSLGVSNSGQLDMGLLFVCYQSDLAQAFLTVQERLNGEALEEYVKPIGGGYFFTLPGVADANHYLAQSLLEA
Enzyme Length 434
Uniprot Accession Number Q1CHD5
Absorption
Active Site
Activity Regulation
Binding Site BINDING 358; /note=Heme b; /evidence=ECO:0000250|UniProtKB:P31545
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1; Evidence={ECO:0000250|UniProtKB:P31545};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585; Evidence={ECO:0000250|UniProtKB:P31545};
DNA Binding
EC Number 4.99.1.1; 1.11.1.-
Enzyme Function FUNCTION: Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the protoporphyrin ring intact. {ECO:0000250|UniProtKB:P31545}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (1); Chain (1); Metal binding (1); Region (2); Signal peptide (1)
Keywords Heme;Iron;Lyase;Metal-binding;Oxidoreductase;Periplasm;Peroxidase;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Signal Peptide SIGNAL 1..45; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,801
Kinetics
Metal Binding METAL 340; /note=Iron (heme b proximal ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P31545
Rhea ID RHEA:22584; RHEA:22585
Cross Reference Brenda