CPFC1_BACAN
ID CPFC1_BACAN Reviewed; 311 AA.
AC Q81U22; Q6I2A7; Q6KW38;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Coproporphyrin III ferrochelatase 1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE EC=4.99.1.9 {ECO:0000255|HAMAP-Rule:MF_00323};
GN Name=cpfC1 {ECO:0000255|HAMAP-Rule:MF_00323}; Synonyms=hemH-1, hemH1;
GN OrderedLocusNames=BA_1071, GBAA_1071, BAS1000;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC Catalyzes the insertion of ferrous iron into coproporphyrin III to form
CC Fe-coproporphyrin III. {ECO:0000255|HAMAP-Rule:MF_00323}.
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 PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
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; AE016879; AAP25051.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30171.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53324.1; -; Genomic_DNA.
DR RefSeq; NP_843565.1; NC_003997.3.
DR RefSeq; WP_000726793.1; NZ_WXXJ01000044.1.
DR RefSeq; YP_027273.1; NC_005945.1.
DR PDB; 2C8J; X-ray; 2.10 A; A/B=1-311.
DR PDBsum; 2C8J; -.
DR AlphaFoldDB; Q81U22; -.
DR SMR; Q81U22; -.
DR IntAct; Q81U22; 14.
DR STRING; 261594.GBAA_1071; -.
DR DNASU; 1089001; -.
DR EnsemblBacteria; AAP25051; AAP25051; BA_1071.
DR EnsemblBacteria; AAT30171; AAT30171; GBAA_1071.
DR GeneID; 45021099; -.
DR KEGG; ban:BA_1071; -.
DR KEGG; bar:GBAA_1071; -.
DR KEGG; bat:BAS1000; -.
DR PATRIC; fig|198094.11.peg.1058; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_2_1_9; -.
DR OMA; LGDPYHC; -.
DR UniPathway; UPA00252; -.
DR EvolutionaryTrace; Q81U22; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
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; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..311
FT /note="Coproporphyrin III ferrochelatase 1"
FT /id="PRO_0000175102"
FT BINDING 12
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 29
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 45..46
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 53
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 124
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 182
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 263
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:2C8J"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 53..73
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 75..91
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2C8J"
FT TURN 266..270
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:2C8J"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2C8J"
FT HELIX 293..308
FT /evidence="ECO:0007829|PDB:2C8J"
SQ SEQUENCE 311 AA; 35349 MW; 936EAA609AE3609F CRC64;
MKKKIGLLVM AYGTPYKEED IERYYTHIRR GRKPSPEMLE DLTERYRAIG GISPLATITL
EQAKKLEKRL NEVQDEVEYH MYLGLKHIEP FIEDAVKEMH NDGIQDAIAL VLAPHYSTFS
VKSYVGRAQE EAEKLGNLTI HGIDSWYKEP KFIQYWVDAV KSIYSGMSDA EREKAVLIVS
AHSLPEKIIA MGDPYPDQLN ETADYIARGA EVANYAVGWQ SAGNTPDPWI GPDVQDLTRE
LNEKYGYTSF VYAPVGFVAE HLEVLYDNDF ECKVVTDEIG AKYYRPEMPN ASDAFIDCLT
DVVVKKKESV M
