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COXX_FRACC
ID   COXX_FRACC              Reviewed;         289 AA.
AC   Q2JCG7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Francci3_1649;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00154};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000249; ABD11025.1; -; Genomic_DNA.
DR   RefSeq; WP_011436088.1; NZ_JENI01000041.1.
DR   AlphaFoldDB; Q2JCG7; -.
DR   SMR; Q2JCG7; -.
DR   STRING; 106370.Francci3_1649; -.
DR   EnsemblBacteria; ABD11025; ABD11025; Francci3_1649.
DR   KEGG; fra:Francci3_1649; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_1_11; -.
DR   OMA; QFFWQFP; -.
DR   OrthoDB; 1875497at2; -.
DR   PhylomeDB; Q2JCG7; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR   HAMAP; MF_00154; CyoE_CtaB; 1.
DR   InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..289
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327055"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        190..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   289 AA;  31071 MW;  8B70326E30477941 CRC64;
     MSAKARGYVA LMKLRVVELL LITTVPVMML AERGVPSLRL IAVTLVAGTL AAGSANTINC
     YVDRDIDQMM GRTKRRPLVR ATVTPTEALT FGIVIGIVST LLFGFLVNWP SALLADGAIA
     FYVFVYTLGL KRRTPSNIVI GGAAGCFPVL IGWSAVTGTV GWAAVLLFAV VFFWTPPHFW
     ALAMKFRDDY AAAGVPMLPV VASVQVVTRR MLGYAYAMVA ASLAVAPVAS TGPVYLVAAV
     AVGAWFLVES HRVARRARHG EDPRPMRLFH MSITYLTLLF VAIAVTALV
 
 
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