Brand  (β version)

PDB ID: 6FXQ

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Ligands
Code Name Style Show Link
FEC 1,3,5,8-tetramethyl-porphine-2,4,6,7-tetrapropionic acid ferrous complex PoSSuM
MPD (4s)-2-methyl-2,4-pentanediol PoSSuM
NA Sodium ion PoSSuM
VOV Harderoheme (III) PoSSuM
Non-standard Residues
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Structure summary

Code : 6FXQ   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Structure of coproheme decarboxylase from Listeria monocytogenes during turnover
Release Data : 2019-07-10
Compound :
mol_id molecule chains synonym
1 Putative heme-dependent peroxidase lmo2113 A,B,C,D,E UPF0447 protein lmo2113
ec: 1.11.1.-
Source :
mol_id organism_scientific expression_system
1 Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)  (taxid:169963) Escherichia coli BL21(DE3)  (taxid:469008)
strain: ATCC BAA-679 / EGD-e
gene: lmo2113
Authors : Hofbauer, S., Pfanzagl, V., Mlynek, G., Puehringer, D.
Keywords : coproheme decarboxylase, iron coproporphyrin III, monovinyl monopropionate deuteroheme, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.6900 Å )
Citation :

Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Hemeb.

Milazzo, L.,Gabler, T.,Puhringer, D.  et al.
(2019)  Acs Catalysis  9 : 6766 - 6782

PubMed: 31423350
DOI: 10.1021/acscatal.9b00963

Reaction

Chain : A, B, C, D, E
UniProt : Q8Y5F1 (CHDC_LISMO)
Reaction: EC: Evidence:
Physiological Direction:
Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme b 1.3.98.5 HAMAP- Rule:MF_01442, PubMed:27758026, PubMed:29536725, PubMed:31423350
left-to-right HAMAP-Rule:MF_01442, PubMed:27758026, PubMed:31423350
Fe-coproporphyrin III + H(+) + H2O2 = CO2 + 2 H2O + harderoheme III - HAMAP- Rule:MF_01442, PubMed:31423350
left-to-right HAMAP-Rule:MF_01442, PubMed:27758026, PubMed:31423350
H(+) + H2O2 + harderoheme III = CO2 + 2 H2O + heme b - HAMAP-Rule:MF_01442, PubMed:31423350
left-to-right HAMAP-Rule:MF_01442, PubMed:27758026, PubMed:31423350