ID   COXX_BORA1              Reviewed;         298 AA.
AC   Q2KTX0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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}; OrderedLocusNames=BAV3280;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50890.1; -; Genomic_DNA.
DR   RefSeq; WP_012418917.1; NC_010645.1.
DR   AlphaFoldDB; Q2KTX0; -.
DR   SMR; Q2KTX0; -.
DR   STRING; 360910.BAV3280; -.
DR   EnsemblBacteria; CAJ50890; CAJ50890; BAV3280.
DR   GeneID; 41395110; -.
DR   KEGG; bav:BAV3280; -.
DR   eggNOG; COG0109; Bacteria.
DR   HOGENOM; CLU_029631_0_2_4; -.
DR   OMA; QFFWQFP; -.
DR   OrthoDB; 1875497at2; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001977; 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; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Heme biosynthesis; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..298
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000327013"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   298 AA;  32797 MW;  718175581AD60C0F CRC64;
     MTSIAAPQPG LLRQYLVLTK PRVTQLAVFC AVIGMFLAVP GLPDLKRVLF GTIGIWLLAA
     AAFAINCLIE QEIDARMTRT ARRGTARGTI SPAQVLSLSG LLGGAGMLVL YHLVNPLTMW
     LTFATFVGYA VIYTVILKPR TPQNIVIGGL SGAMPPALGW ASVANAVPAE AWVLVLIIFI
     WTPPHFWALA LYRTEDYRKA GLPMLPITHG SKHTRLQIML YSFALFAVTL LPYFMHMNGL
     LYLLAAVILG GIFVAHALRL YRSYSDERSR RLFRYSILYL ALLFGALLVD HWVGVLSA