ID CPFC_BACSU Reviewed; 310 AA. AC P32396; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 04-NOV-2026, entry version 166. DE RecName: Full=Coproporphyrin III ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000305}; DE EC=4.99.1.9 {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25908396}; DE AltName: Full=Water-soluble ferrochelatase {ECO:0000303|PubMed:8119288}; GN Name=cpfC {ECO:0000255|HAMAP-Rule:MF_00323, GN ECO:0000303|PubMed:28123057}; GN Synonyms=hemF, hemH {ECO:0000303|PubMed:1459957}; GN OrderedLocusNames=BSU10130; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY. RX PubMed=1459957; DOI=10.1128/jb.174.24.8081-8093.1992; RA Hansson M., Hederstedt L.; RT "Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, RT which encodes protoheme IX biosynthetic enzymes."; RL J. Bacteriol. 174:8081-8093(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=9579061; DOI=10.1099/00221287-144-4-859; RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., RA Venema G., Bron S.; RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus RT subtilis chromosome contains several dysfunctional genes, the glyB marker, RT many genes encoding transporter proteins, and the ubiquitous hit gene."; RL Microbiology 144:859-875(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, SUBCELLULAR RP LOCATION, AND DISRUPTION PHENOTYPE. RC STRAIN=3G18; RX PubMed=8119288; DOI=10.1111/j.1432-1033.1994.tb18615.x; RA Hansson M., Hederstedt L.; RT "Purification and characterisation of a water-soluble ferrochelatase from RT Bacillus subtilis."; RL Eur. J. Biochem. 220:201-208(1994). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=25646457; DOI=10.1073/pnas.1416285112; RA Dailey H.A., Gerdes S., Dailey T.A., Burch J.S., Phillips J.D.; RT "Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway RT that does not use protoporphyrin."; RL Proc. Natl. Acad. Sci. U.S.A. 112:2210-2215(2015). RN [6] RP PATHWAY, AND REVIEW. RX PubMed=25711532; DOI=10.1016/j.abb.2015.02.017; RA Dailey H.A., Gerdes S.; RT "HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme RT synthesis in Firmicutes and Actinobacteria."; RL Arch. Biochem. Biophys. 574:27-35(2015). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=25908396; DOI=10.1111/mmi.13041; RA Lobo S.A., Scott A., Videira M.A., Winpenny D., Gardner M., Palmer M.J., RA Schroeder S., Lawrence A.D., Parkinson T., Warren M.J., Saraiva L.M.; RT "Staphylococcus aureus haem biosynthesis: characterisation of the enzymes RT involved in final steps of the pathway."; RL Mol. Microbiol. 97:472-487(2015). RN [8] RP FUNCTION, AND INTERACTION WITH FRA. RC STRAIN=168; RX PubMed=25826316; DOI=10.1371/journal.pone.0122538; RA Mielcarek A., Blauenburg B., Miethke M., Marahiel M.A.; RT "Molecular insights into frataxin-mediated iron supply for heme RT biosynthesis in Bacillus subtilis."; RL PLoS ONE 10:e0122538-e0122538(2015). RN [9] RP NOMENCLATURE, AND REVIEW. RX PubMed=28123057; DOI=10.1128/mmbr.00048-16; RA Dailey H.A., Dailey T.A., Gerdes S., Jahn D., Jahn M., O'Brian M.R., RA Warren M.J.; RT "Prokaryotic heme biosynthesis: multiple pathways to a common essential RT product."; RL Microbiol. Mol. Biol. Rev. 81:e00048-e00048(2017). RN [10] RP 3D-STRUCTURE MODELING. RX PubMed=9141132; RX DOI=10.1002/(sici)1097-0134(199704)27:4<517::aid-prot5>3.3.co;2-b; RA Hansson M., Gough S.P., Brody S.S.; RT "Structure prediction and fold recognition for the ferrochelatase family of RT proteins."; RL Proteins 27:517-522(1997). RN [11] {ECO:0007744|PDB:1AK1} RP X-RAY CRYSTALLOGRAPHY. RX PubMed=9384565; DOI=10.1016/s0969-2126(97)00299-2; RA Al-Karadaghi S., Hansson M., Nikonov S., Jonsson B., Hederstedt L.; RT "Crystal structure of ferrochelatase: the terminal enzyme in heme RT biosynthesis."; RL Structure 5:1501-1510(1997). RN [12] {ECO:0007744|PDB:1C1H, ECO:0007744|PDB:1C9E, ECO:0007744|PDB:1DOZ} RP X-RAY CRYSTALLOGRAPHY IN COMPLEXES WITH N-METHYLMESOPORPHYRIN INHIBITOR; RP COPPER AND MAGNESIUM, AND ACTIVITY REGULATION. RX PubMed=10704318; DOI=10.1006/jmbi.2000.3569; RA Lecerof D., Fodje M., Hansson A., Hansson M., Al-Karadaghi S.; RT "Structural and mechanistic basis of porphyrin metallation by RT ferrochelatase."; RL J. Mol. Biol. 297:221-232(2000). RN [13] {ECO:0007744|PDB:1LD3, ECO:0007744|PDB:1N0I} RP X-RAY CRYSTALLOGRAPHY IN COMPLEXES WITH ZINC; MAGNESIUM AND CADMIUM, RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-272. RX PubMed=12761666; DOI=10.1007/s00775-002-0436-1; RA Lecerof D., Fodje M.N., Alvarez Leon R., Olsson U., Hansson A., RA Sigfridsson E., Ryde U., Hansson M., Al-Karadaghi S.; RT "Metal binding to Bacillus subtilis ferrochelatase and interaction between RT metal sites."; RL J. Biol. Inorg. Chem. 8:452-458(2003). RN [14] {ECO:0007744|PDB:2AC2, ECO:0007744|PDB:2AC4} RP X-RAY CRYSTALLOGRAPHY OF PHE-13 AND CYS-183 MUTANTS IN COMPLEXES WITH ZINC, RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF TYR-13 AND HIS-183. RX PubMed=16140324; DOI=10.1016/j.jmb.2005.08.002; RA Shipovskov S., Karlberg T., Fodje M., Hansson M.D., Ferreira G.C., RA Hansson M., Reimann C.T., Al-Karadaghi S.; RT "Metallation of the transition-state inhibitor N-methyl mesoporphyrin by RT ferrochelatase: implications for the catalytic reaction mechanism."; RL J. Mol. Biol. 352:1081-1090(2005). RN [15] {ECO:0007744|PDB:2H1V, ECO:0007744|PDB:2H1W, ECO:0007744|PDB:2HK6} RP X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANTS ALA-87 AND ALA-183 IN RP COMPLEXES WITH IRON AND MAGNESIUM, AND MUTAGENESIS OF LYS-87; HIS-88; RP HIS-183 AND GLU-264. RX PubMed=17198378; DOI=10.1021/bi061760a; RA Hansson M.D., Karlberg T., Rahardja M.A., Al-Karadaghi S., Hansson M.; RT "Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase RT direct and facilitate the insertion of metal ion into protoporphyrin IX."; RL Biochemistry 46:87-94(2007). RN [16] {ECO:0007744|PDB:2Q2N, ECO:0007744|PDB:2Q2O, ECO:0007744|PDB:2Q3J} RP X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANTS ALA-183 AND CYS-183 IN RP COMPLEXES WITH MAGNESIUM; N-METHYLMESOPORPHYRIN INHIBITOR AND RP 2,4-DISULFONIC ACID DEUTEROPORPHYRIN IX INHIBITOR, AND ACTIVITY REGULATION. RX PubMed=18423489; DOI=10.1016/j.jmb.2008.03.040; RA Karlberg T., Hansson M.D., Yengo R.K., Johansson R., Thorvaldsen H.O., RA Ferreira G.C., Hansson M., Al-Karadaghi S.; RT "Porphyrin binding and distortion and substrate specificity in the RT ferrochelatase reaction: the role of active site residues."; RL J. Mol. Biol. 378:1074-1083(2008). RN [17] {ECO:0007744|PDB:3GOQ, ECO:0007744|PDB:3M4Z} RP X-RAY CRYSTALLOGRAPHY OF WILD-TYPE IN COMPLEX WITH COBALT AND MAGNESIUM AND RP MUTANT MET-13 IN COMPLEX WITH MAGNESIUM, FUNCTION, AND MUTAGENESIS OF RP TYR-13. RX PubMed=21052751; DOI=10.1007/s00775-010-0720-4; RA Hansson M.D., Karlberg T., Soederberg C.A., Rajan S., Warren M.J., RA Al-Karadaghi S., Rigby S.E., Hansson M.; RT "Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal RT specificity of Bacillus subtilis ferrochelatase."; RL J. Biol. Inorg. Chem. 16:235-242(2011). CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis CC (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous CC iron into coproporphyrin III to form Fe-coproporphyrin III CC (PubMed:25646457, PubMed:25908396). It can also insert iron into CC protoporphyrin IX (PubMed:1459957, PubMed:21052751, PubMed:25646457, CC PubMed:8119288). Has weaker activity with 2,4 disulfonate, CC deuteroporphyrin and 2,4 hydroxyethyl (PubMed:12761666, CC PubMed:25646457). In vitro, can also use Zn(2+) or Cu(2+) CC (PubMed:12761666, PubMed:16140324, PubMed:21052751, PubMed:8119288). CC {ECO:0000269|PubMed:12761666, ECO:0000269|PubMed:1459957, CC ECO:0000269|PubMed:16140324, ECO:0000269|PubMed:21052751, CC ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25826316, CC ECO:0000269|PubMed:25908396, ECO:0000269|PubMed:8119288}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+); CC Xref=Rhea:RHEA:49572, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:68438, ChEBI:CHEBI:131725; EC=4.99.1.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323, CC ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25908396}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323, CC ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25908396}; CC -!- ACTIVITY REGULATION: Stimulated by Mg(2+) (PubMed:12761666). Inhibited CC by Cd(2+) (PubMed:12761666). Inhibited by N-methylmesoporphyrin (N- CC MeMP) and 2,4-disulfonic acid deuteroporphyrin IX (dSDP) CC (PubMed:10704318, PubMed:16140324, PubMed:18423489). CC {ECO:0000269|PubMed:10704318, ECO:0000269|PubMed:12761666, CC ECO:0000269|PubMed:16140324, ECO:0000269|PubMed:18423489}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=7.8 uM for coproporphyrin III {ECO:0000269|PubMed:25646457}; CC KM=0.15 uM for Fe(2+) {ECO:0000269|PubMed:25908396}; CC KM=17 uM for Zn(2+) {ECO:0000269|PubMed:8119288}; CC KM=170 uM for Cu(2+) {ECO:0000269|PubMed:8119288}; CC Note=kcat is 0.11 min(-1) with coproporphyrin III as substrate CC (PubMed:25646457). kcat is 78 min(-1) with Fe(2+) as substrate CC (PubMed:25908396). {ECO:0000269|PubMed:25646457, CC ECO:0000269|PubMed:25908396}; CC pH dependence: CC Optimum pH is 7.2 with Zn(2+) and protoporphyrin IX as substrates. CC {ECO:0000269|PubMed:8119288}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00323, CC ECO:0000269|PubMed:1459957, ECO:0000269|PubMed:25646457, CC ECO:0000269|PubMed:8119288, ECO:0000305|PubMed:25711532}. CC -!- SUBUNIT: Monomer (PubMed:8119288). Interacts with frataxin/Fra CC (PubMed:25826316). {ECO:0000269|PubMed:25826316, CC ECO:0000269|PubMed:8119288}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323, CC ECO:0000269|PubMed:8119288}. CC -!- DISRUPTION PHENOTYPE: Deletion mutant requires hemin for growth. CC {ECO:0000269|PubMed:8119288}. CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP- CC Rule:MF_00323, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M97208; AAA22518.1; -; Genomic_DNA. DR EMBL; Y14083; CAA74519.1; -; Genomic_DNA. DR EMBL; AL009126; CAB12853.1; -; Genomic_DNA. DR PIR; C47045; C47045. DR RefSeq; NP_388894.1; NC_000964.3. DR RefSeq; WP_003244736.1; NC_000964.3. DR PDB; 1AK1; X-ray; 1.90 A; A=1-310. DR PDB; 1C1H; X-ray; 1.90 A; A=1-310. DR PDB; 1C9E; X-ray; 2.30 A; A=5-310. DR PDB; 1DOZ; X-ray; 1.80 A; A=2-310. DR PDB; 1LD3; X-ray; 2.60 A; A=1-310. DR PDB; 1N0I; X-ray; 2.00 A; A=1-310. DR PDB; 2AC2; X-ray; 2.50 A; A=2-310. DR PDB; 2AC4; X-ray; 2.10 A; A=2-310. DR PDB; 2H1V; X-ray; 1.20 A; A=1-310. DR PDB; 2H1W; X-ray; 2.60 A; A=1-310. DR PDB; 2HK6; X-ray; 1.71 A; A=1-310. DR PDB; 2Q2N; X-ray; 1.80 A; A=2-310. DR PDB; 2Q2O; X-ray; 2.10 A; A=2-310. DR PDB; 2Q3J; X-ray; 2.39 A; A=2-310. DR PDB; 3GOQ; X-ray; 1.60 A; A=1-310. DR PDB; 3M4Z; X-ray; 1.94 A; A=2-310. DR PDB; 9KTA; X-ray; 1.00 A; A=2-310. DR PDB; 9KTB; X-ray; 1.13 A; A=2-310. DR PDB; 9KTC; X-ray; 1.50 A; A=2-310. DR PDB; 9KTD; X-ray; 1.38 A; A=2-310. DR PDB; 9KTE; X-ray; 1.46 A; A=2-310. DR PDB; 9KTF; X-ray; 1.44 A; A=2-310. DR PDB; 9KTG; X-ray; 1.44 A; A=2-310. DR PDB; 9KTH; X-ray; 1.90 A; A=2-310. DR AlphaFoldDB; P32396; -. DR MDRepo; P32396; -. DR SMR; P32396; -. DR FunCoup; P32396; 712. DR STRING; 224308.BSU10130; -. DR DrugBank; DB01911; N-Methylmesoporphyrin. DR DrugBank; DB02188; N-Methylmesoporphyrin containing copper. DR jPOST; P32396; -. DR PaxDb; 224308-BSU10130; -. DR EnsemblBacteria; CAB12853; CAB12853; BSU_10130. DR GeneID; 939772; -. DR KEGG; bsu:BSU10130; -. DR PATRIC; fig|224308.179.peg.1089; -. DR eggNOG; COG0276; Bacteria. DR InParanoid; P32396; -. DR OMA; AACSYQM; -. DR OrthoDB; 9776380at2; -. DR PhylomeDB; P32396; -. DR BioCyc; BSUB:BSU10130-MONOMER; -. DR BioCyc; MetaCyc:BSU10130-MONOMER; -. DR BRENDA; 4.98.1.1; 658. DR BRENDA; 4.99.1.9; 658. DR UniPathway; UPA00252; -. DR EvolutionaryTrace; P32396; -. DR Proteomes; UP000001570; Chromosome. DR AbasyAtlas; P32396; -. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0004325; F:protoporphyrin ferrochelatase activity; IBA:GO_Central. DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central. DR CDD; cd00419; Ferrochelatase_C; 1. DR CDD; cd03411; Ferrochelatase_N; 1. DR FunFam; 3.40.50.1400:FF:000009; Ferrochelatase; 1. DR Gene3D; 3.40.50.1400; -; 2. DR HAMAP; MF_00323; Ferrochelatase; 1. DR InterPro; IPR001015; Ferrochelatase. DR InterPro; IPR019772; Ferrochelatase_AS. DR InterPro; IPR033644; Ferrochelatase_C. DR InterPro; IPR033659; Ferrochelatase_N. DR NCBIfam; TIGR00109; hemH; 1. DR NCBIfam; NF009095; PRK12435.1; 1. DR PANTHER; PTHR11108; FERROCHELATASE; 1. DR PANTHER; PTHR11108:SF1; FERROCHELATASE, MITOCHONDRIAL; 1. DR Pfam; PF00762; Ferrochelatase; 1. DR SUPFAM; SSF53800; Chelatase; 1. DR PROSITE; PS00534; FERROCHELATASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Heme biosynthesis; Iron; Lyase; Magnesium; KW Metal-binding; Porphyrin biosynthesis; Reference proteome. FT CHAIN 1..310 FT /note="Coproporphyrin III ferrochelatase" FT /id="PRO_0000175114" FT BINDING 13 FT /ligand="Fe-coproporphyrin III" FT /ligand_id="ChEBI:CHEBI:68438" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323" FT BINDING 13 FT /ligand="N-methylmesoporphyrin" FT /ligand_id="ChEBI:CHEBI:176424" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:10704318, FT ECO:0007744|PDB:1C1H" FT BINDING 20 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305|PubMed:17198378, FT ECO:0000305|PubMed:21052751" FT BINDING 30 FT /ligand="Fe-coproporphyrin III" FT /ligand_id="ChEBI:CHEBI:68438" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323" FT BINDING 31..33 FT /ligand="N-methylmesoporphyrin" FT /ligand_id="ChEBI:CHEBI:176424" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:10704318, FT ECO:0007744|PDB:1C1H" FT BINDING 46..47 FT /ligand="Fe-coproporphyrin III" FT /ligand_id="ChEBI:CHEBI:68438" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323" FT BINDING 46 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305|PubMed:12761666" FT BINDING 54 FT /ligand="Fe-coproporphyrin III" FT /ligand_id="ChEBI:CHEBI:68438" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323" FT BINDING 125 FT /ligand="Fe-coproporphyrin III" FT /ligand_id="ChEBI:CHEBI:68438" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323" FT BINDING 183 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323, FT ECO:0000305|PubMed:12761666, ECO:0000305|PubMed:16140324, FT ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751" FT BINDING 183 FT /ligand="N-methylmesoporphyrin" FT /ligand_id="ChEBI:CHEBI:176424" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:10704318, FT ECO:0007744|PDB:1C1H" FT BINDING 188 FT /ligand="N-methylmesoporphyrin" FT /ligand_id="ChEBI:CHEBI:176424" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:10704318, FT ECO:0007744|PDB:1C1H" FT BINDING 264 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323, FT ECO:0000305|PubMed:12761666, ECO:0000305|PubMed:16140324, FT ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305|PubMed:12761666" FT BINDING 272 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305|PubMed:12761666" FT MUTAGEN 13 FT /note="Y->F: No change in activity." FT /evidence="ECO:0000269|PubMed:16140324" FT MUTAGEN 13 FT /note="Y->M: Changes the metal specificity of the enzyme. FT Can insert Co(2+) into protoporphyrin IX at a higher rate FT than the wild-type enzyme, but loses the ability to insert FT Cu(2+) and Zn(2+)." FT /evidence="ECO:0000269|PubMed:21052751" FT MUTAGEN 87 FT /note="K->A: Retains 92% of activity." FT /evidence="ECO:0000269|PubMed:17198378" FT MUTAGEN 88 FT /note="H->A: Retains 5% of activity." FT /evidence="ECO:0000269|PubMed:17198378" FT MUTAGEN 183 FT /note="H->A,C: Loss of activity." FT /evidence="ECO:0000269|PubMed:16140324, FT ECO:0000269|PubMed:17198378" FT MUTAGEN 264 FT /note="E->Q: Retains 21% of activity." FT /evidence="ECO:0000269|PubMed:17198378" FT MUTAGEN 264 FT /note="E->V: Retains less than 1% of activity." FT /evidence="ECO:0000269|PubMed:17198378" FT MUTAGEN 272 FT /note="E->S: Abolishes the effect of Mg(2+)." FT /evidence="ECO:0000269|PubMed:12761666" FT STRAND 4..12 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 22..29 FT /evidence="ECO:0007829|PDB:9KTA" FT TURN 30..32 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 37..49 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 54..74 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 76..92 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 93..102 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 107..116 FT /evidence="ECO:0007829|PDB:9KTA" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 122..136 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 151..167 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 175..183 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 187..192 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 196..211 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:1C1H" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 235..246 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:9KTA" FT TURN 267..271 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 272..280 FT /evidence="ECO:0007829|PDB:9KTA" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:9KTA" FT HELIX 294..307 FT /evidence="ECO:0007829|PDB:9KTA" SQ SEQUENCE 310 AA; 35348 MW; 5BFD9972689CE761 CRC64; MSRKKMGLLV MAYGTPYKEE DIERYYTHIR RGRKPEPEML QDLKDRYEAI GGISPLAQIT EQQAHNLEQH LNEIQDEITF KAYIGLKHIE PFIEDAVAEM HKDGITEAVS IVLAPHFSTF SVQSYNKRAK EEAEKLGGLT ITSVESWYDE PKFVTYWVDR VKETYASMPE DERENAMLIV SAHSLPEKIK EFGDPYPDQL HESAKLIAEG AGVSEYAVGW QSEGNTPDPW LGPDVQDLTR DLFEQKGYQA FVYVPVGFVA DHLEVLYDND YECKVVTDDI GASYYRPEMP NAKPEFIDAL ATVVLKKLGR //