ID COXX_RICFE Reviewed; 305 AA. AC Q4UM22; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=Protoheme IX farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154}; DE EC=2.5.1.141 {ECO:0000255|HAMAP-Rule:MF_00154}; DE AltName: Full=Heme B farnesyltransferase {ECO:0000255|HAMAP-Rule:MF_00154}; DE AltName: Full=Heme O synthase {ECO:0000255|HAMAP-Rule:MF_00154}; GN Name=ctaB {ECO:0000255|HAMAP-Rule:MF_00154}; GN OrderedLocusNames=RF_0550; OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=315456; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). CC -!- FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of CC the vinyl group on carbon 2 of heme B porphyrin ring with a CC hydroxyethyl farnesyl side group. {ECO:0000255|HAMAP-Rule:MF_00154}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + CC Fe(II)-heme o; Xref=Rhea:RHEA:28070, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:60344, ChEBI:CHEBI:60530, CC ChEBI:CHEBI:175763; EC=2.5.1.141; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00154}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme O biosynthesis; CC heme O from protoheme: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00154}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00154}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00154}. CC -!- MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined CC according to the Fischer nomenclature. {ECO:0000255|HAMAP- CC Rule:MF_00154}. CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX CC farnesyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_00154}. 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; CP000053; AAY61401.1; -; Genomic_DNA. DR AlphaFoldDB; Q4UM22; -. DR SMR; Q4UM22; -. DR STRING; 315456.RF_0550; -. DR KEGG; rfe:RF_0550; -. DR eggNOG; COG0109; Bacteria. DR HOGENOM; CLU_029631_0_2_5; -. DR OrthoDB; 9814417at2; -. DR UniPathway; UPA00834; UER00712. DR Proteomes; UP000008548; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0048034; P:heme O biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd13957; PT_UbiA_Cox10; 1. DR Gene3D; 1.10.357.140; UbiA prenyltransferase; 1. DR HAMAP; MF_00154; CyoE_CtaB; 1. DR InterPro; IPR006369; Protohaem_IX_farnesylTrfase. DR InterPro; IPR000537; UbiA_prenyltransferase. DR InterPro; IPR030470; UbiA_prenylTrfase_CS. DR InterPro; IPR044878; UbiA_sf. DR NCBIfam; TIGR01473; cyoE_ctaB; 1. DR PANTHER; PTHR43448:SF7; 4-HYDROXYBENZOATE SOLANESYLTRANSFERASE; 1. DR PANTHER; PTHR43448; PROTOHEME IX FARNESYLTRANSFERASE, MITOCHONDRIAL; 1. DR Pfam; PF01040; UbiA; 1. DR PROSITE; PS00943; UBIA; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..305 FT /note="Protoheme IX farnesyltransferase" FT /id="PRO_0000274893" FT TRANSMEM 31..51 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 52..72 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 102..119 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 123..145 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 151..171 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 179..199 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 225..245 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 247..267 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" FT TRANSMEM 284..304 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00154" SQ SEQUENCE 305 AA; 34261 MW; E51B64737D984DB1 CRC64; MSSLVTPINL DKINHSQSTV KDYILLMKPR VMSLVIFTGF VGIWLAPYSV HPFIAGIAVV CIALGAGSAG AINMWYDRDI DSLMKRTQKR PIVRGAIEPD EALSFGLITG FFAVFFMALC VNLLASFLLL FTIFYYICIY TIWLKRRSIQ NIVIGGVSGA LPPVIGYAAV SNTISLESII LFLIIFIWTP PHSWALALFC NDDYKNCKVP MMPAVKGNLY TKKQILIYSI LLFIVSLMPF FIGMNNFIYL ITSGILGLVF LYYSGSLFYD TPDNKQAKRF FAYSIFYLFF IFLLLSSTST ISLIS //