CPFC_BACSU
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 03-AUG-2022, entry version 152.
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, ECO:0000303|PubMed:28123057};
GN Synonyms=hemF, hemH {ECO:0000303|PubMed:1459957};
GN OrderedLocusNames=BSU10130;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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>3.0.co;2-7;
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 (1.9 ANGSTROMS).
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 (1.80 ANGSTROMS) OF 2-310 IN COMPLEXES WITH
RP N-METHYLMESOPORPHYRIN INHIBITOR; COPPER AND MAGNESIUM, AND ACTIVITY
RP 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 (2.00 ANGSTROMS) IN COMPLEXES WITH ZINC; MAGNESIUM
RP AND CADMIUM, 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 (2.10 ANGSTROMS) OF 2-310 OF PHE-13 AND CYS-183
RP MUTANTS IN COMPLEXES WITH ZINC, FUNCTION, ACTIVITY REGULATION, AND
RP 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 (1.20 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-87 AND
RP ALA-183 IN COMPLEXES WITH IRON AND MAGNESIUM, AND MUTAGENESIS OF LYS-87;
RP HIS-88; 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 (1.80 ANGSTROMS) OF 2-310 OF WILD-TYPE AND MUTANTS
RP ALA-183 AND CYS-183 IN COMPLEXES WITH MAGNESIUM; N-METHYLMESOPORPHYRIN
RP INHIBITOR AND 2,4-DISULFONIC ACID DEUTEROPORPHYRIN IX INHIBITOR, AND
RP 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 (1.60 ANGSTROMS) OF 2-310 OF WILD-TYPE IN COMPLEX
RP WITH COBALT AND MAGNESIUM AND MUTANT MET-13 IN COMPLEX WITH MAGNESIUM,
RP FUNCTION, AND MUTAGENESIS OF 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:8119288, PubMed:21052751,
CC PubMed:25646457). Has weaker activity with 2,4 disulfonate,
CC deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457,
CC PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+)
CC (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666).
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}.
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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; NZ_JNCM01000035.1.
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 PDBsum; 1AK1; -.
DR PDBsum; 1C1H; -.
DR PDBsum; 1C9E; -.
DR PDBsum; 1DOZ; -.
DR PDBsum; 1LD3; -.
DR PDBsum; 1N0I; -.
DR PDBsum; 2AC2; -.
DR PDBsum; 2AC4; -.
DR PDBsum; 2H1V; -.
DR PDBsum; 2H1W; -.
DR PDBsum; 2HK6; -.
DR PDBsum; 2Q2N; -.
DR PDBsum; 2Q2O; -.
DR PDBsum; 2Q3J; -.
DR PDBsum; 3GOQ; -.
DR PDBsum; 3M4Z; -.
DR AlphaFoldDB; P32396; -.
DR SMR; P32396; -.
DR STRING; 224308.BSU10130; -.
DR DrugBank; DB01911; N-Methylmesoporphyrin.
DR DrugBank; DB02188; N-Methylmesoporphyrin containing copper.
DR jPOST; P32396; -.
DR PaxDb; P32396; -.
DR PRIDE; P32396; -.
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; LGDPYHC; -.
DR PhylomeDB; P32396; -.
DR BioCyc; BSUB:BSU10130-MON; -.
DR BioCyc; MetaCyc:BSU10130-MON; -.
DR BRENDA; 4.99.1.1; 658.
DR BRENDA; 4.99.1.9; 658.
DR UniPathway; UPA00252; -.
DR EvolutionaryTrace; P32396; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR CDD; cd00419; Ferrochelatase_C; 1.
DR CDD; cd03411; Ferrochelatase_N; 1.
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 PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR TIGRFAMs; TIGR00109; hemH; 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:2H1V"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:2H1V"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 76..92
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:2H1V"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 196..211
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1C1H"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1DOZ"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:2H1V"
FT TURN 267..271
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:2H1V"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2H1V"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:2H1V"
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
