ID   COXX_KORCO              Reviewed;         294 AA.
AC   B1L5A4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Kcr_0887;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB07633.1; -; Genomic_DNA.
DR   RefSeq; WP_012309530.1; NC_010482.1.
DR   AlphaFoldDB; B1L5A4; -.
DR   SMR; B1L5A4; -.
DR   STRING; 374847.Kcr_0887; -.
DR   EnsemblBacteria; ACB07633; ACB07633; Kcr_0887.
DR   GeneID; 6094164; -.
DR   KEGG; kcr:Kcr_0887; -.
DR   eggNOG; arCOG00479; Archaea.
DR   HOGENOM; CLU_029631_0_1_2; -.
DR   InParanoid; B1L5A4; -.
DR   OMA; PPLMGYC; -.
DR   OrthoDB; 97092at2157; -.
DR   PhylomeDB; B1L5A4; -.
DR   UniPathway; UPA00834; UER00712.
DR   Proteomes; UP000001686; 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:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
DR   GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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 membrane; Heme biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..294
FT                   /note="Protoheme IX farnesyltransferase"
FT                   /id="PRO_0000346087"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        41..61
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        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00154"
SQ   SEQUENCE   294 AA;  32268 MW;  634CED6ECCC5C6AE CRC64;
     MQVEVFKVKL SDLLCLTKPK QTFLLLLTSI FTYVGAGGMR LDALLLLTAA MLLSISGTTS
     VNMALDADID AMMPRTKDRP VPSGRVSRVE ALSFGLLLFI VGLGLSYLIN PWTAFATSLG
     MAFDILVYTM WTKRRTPLSI IFGGVAGAAP SLAGWAAARG SIELQAIMIA LITILWIPSH
     IWYISIYYLD DYAAARVPMA PVVWGIERTS KLIVASNVLM IILQLLLFLM GPLGPIFLVL
     SLPITLRFLI HSIRYARSPS RGEARRMYKV ASPVEGVIFL AIALDGIFRI LWSS