ID B2IFD3_BEII9 Unreviewed; 353 AA. AC B2IFD3; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 02-SEP-2026, entry version 97. DE RecName: Full=Ferrochelatase {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607}; DE EC=4.98.1.1 {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607}; DE AltName: Full=Heme synthase {ECO:0000256|HAMAP-Rule:MF_00323}; DE AltName: Full=Protoheme ferro-lyase {ECO:0000256|HAMAP-Rule:MF_00323}; GN Name=hemH {ECO:0000256|HAMAP-Rule:MF_00323}; GN OrderedLocusNames=Bind_3476 {ECO:0000313|EMBL:ACB97033.1}; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB OS 8712). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB97033.1, ECO:0000313|Proteomes:UP000001695}; RN [1] {ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712 RC {ECO:0000313|Proteomes:UP000001695}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N., RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.; RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC RT 9039."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACB97033.1, ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712 RC {ECO:0000313|Proteomes:UP000001695}; RX PubMed=20601475; DOI=10.1128/JB.00656-10; RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C., RA Dunfield P.F.; RT "Complete genome sequence of Beijerinckia indica subsp. indica."; RL J. Bacteriol. 192:4532-4533(2010). CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. CC {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607}. 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:0000256|ARBA:ARBA00024536}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49574; CC Evidence={ECO:0000256|ARBA:ARBA00024536}; CC -!- CATALYTIC ACTIVITY: CC Reaction=heme b + 2 H(+) = protoporphyrin IX + Fe(2+); CC Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.98.1.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00323, CC ECO:0000256|RuleBase:RU000607}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00323, ECO:0000256|RuleBase:RU000607}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00323, CC ECO:0000256|RuleBase:RU000607}. CC -!- SIMILARITY: Belongs to the ferrochelatase family. CC {ECO:0000256|ARBA:ARBA00007718, ECO:0000256|HAMAP-Rule:MF_00323, CC ECO:0000256|RuleBase:RU000607}. 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; CP001016; ACB97033.1; -; Genomic_DNA. DR RefSeq; WP_012386381.1; NC_010581.1. DR AlphaFoldDB; B2IFD3; -. DR STRING; 395963.Bind_3476; -. DR KEGG; bid:Bind_3476; -. DR eggNOG; COG0276; Bacteria. DR HOGENOM; CLU_018884_0_0_5; -. DR OrthoDB; 9809741at2; -. DR UniPathway; UPA00252; UER00325. DR Proteomes; UP000001695; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004325; F:protoporphyrin ferrochelatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00419; Ferrochelatase_C; 1. DR CDD; cd03411; Ferrochelatase_N; 1. DR FunFam; 3.40.50.1400:FF:000002; 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 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 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00323}; KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133, ECO:0000256|HAMAP- KW Rule:MF_00323}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00323}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00323}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00323}; KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP- KW Rule:MF_00323}; Reference proteome {ECO:0000313|Proteomes:UP000001695}. FT BINDING 219 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00323" FT BINDING 300 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00323" SQ SEQUENCE 353 AA; 39066 MW; DA69584A0B88D0FA CRC64; MKPLAASTTK ARLTDRIGVL LVNLGTPDAT DYWSMRRYLR EFLSDRRVVE LPRWVWWPIL HGIILTTRPH RSGRRYAGIW DKERNESPLK TITRAQGELL ARSIGASSAP GDGKAQDIVI DFAMRYGNPS IASGLDRLLQ QNCGRILVVP LYPQYAAATT ASVADKVFEI LRARRWQPAL RIAPPYYAEP FYIEALARSV RRGLAGLDFE PDAILLSFHG IPKSSVDKGD PYYEHCLITA DLLRQALGLD EAHCVTTFQS RFGRAEWIGP ATDATVKALA ARGVKKLAVV MPGFAADCLE TIEEVGGEIR ALFLGAGGED YAALPCLNAS EEGMEVIARL VRRELQGWLT STD //