Detail Information for IndEnz0018001026
IED ID IndEnz0018001026
Enzyme Type ID peroxidase001026
Protein Name Deferrochelatase
EC 4.99.1.1
Peroxidase EfeB
EC 1.11.1.-
Gene Name efeB c1157
Organism Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Enzyme Sequence MQYEDENGVNEPSRRRLLKGIGALALAGSCPVAHAQKTQSAPGTLSPDARNEKQPFYGEHQAGILTPQQAAMMLVAFDVLASDKADLERLFRLLTQRFAFLTQGGAAPETPNPRLPPLDSGILGGYIAPDNLTITLSVGHSLFDERFGLAPQMPKKLQKMTRFPNDSLDAALCHGDVLLQICANTQDTVIHALRDIIKHTPDLLSVRWKREGFISDHAARSKGKETPINLLGFKDGTANPDSQNDKLMQKVVWVTADQQEPAWTIGGSYQAVRLIQFRVEFWDRTPLKEQQTIFGRDKQTGAPLGMLHEHDVPDYASDPEGKVIALDSHIRLANPRTAESESSLMLRRGYSYSLGVTNSGQLDMGLLFVCYQHDLEKGFLTVQKRLNGEALEEYVKPIGGGYFFALPGVKDANDYLGSALLRV
Enzyme Length 423
Uniprot Accession Number Q8CW71
Absorption
Active Site
Activity Regulation
Binding Site BINDING 347; /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 INDUCTION: Expressed in response to iron deprivation at pH 7. {ECO:0000269|PubMed:16987175}.
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..35; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 46,664
Kinetics
Metal Binding METAL 329; /note=Iron (heme b proximal ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P31545
Rhea ID RHEA:22584; RHEA:22585
Cross Reference Brenda