IED ID | IndEnz0018001025 |
Enzyme Type ID | peroxidase001025 |
Protein Name |
Deferrochelatase EC 4.99.1.1 Peroxidase EfeB EC 1.11.1.- |
Gene Name | efeB SF1021 S1091 |
Organism | Shigella flexneri |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella flexneri |
Enzyme Sequence | MQYKDENGVNEPSRRRLLKGIGALAGSCPVAHAQKTQSAPGTLSPDARNEKQPFYGEHQAGILTPQQAAMMLVAFDVLASDKADLERLFRLLTQRFAFLSQGGAAPETPNPRLPPLDSGILGGYIAPDNLTITLSVGHSLFDERFGLAPQMPKKLQKMTRFPNDSLDAALCHGDVLLQICANTQDTVNHALRDIIKHTPDLLSVRWKREGFISDHAARSKGKETPINLLGFKDGTANPDSQNDKLMQKVVWVTADQQEPAWTIGGSYQAVRLIQFRVEFWDRTPLKEQQTIFGRDKQTGAPLGMQHEHDVPDYASDPEGKVIALDSHIRLANPRTAESESSLMLRRGYSYSLGVTNSGQLDMGLLFVCYQHDLEKGFLTVQKRLNGEALEEYVKPIGGGYFFSLPGVKDANDYLGRALLQV |
Enzyme Length | 421 |
Uniprot Accession Number | Q83LK4 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 345; /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 (3); Signal peptide (1) |
Keywords | Heme;Iron;Lyase;Metal-binding;Oxidoreductase;Periplasm;Peroxidase;Reference proteome;Repeat;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..33; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 46,538 |
Kinetics | |
Metal Binding | METAL 327; /note=Iron (heme b proximal ligand); via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P31545 |
Rhea ID | RHEA:22584; RHEA:22585 |
Cross Reference Brenda |