ID   COX10_YARLI             Reviewed;         471 AA.
AC   Q6C0L2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Protoheme IX farnesyltransferase, mitochondrial;
DE            EC=2.5.1.141 {ECO:0000250|UniProtKB:P24009};
DE   AltName: Full=Heme O synthase;
DE   Flags: Precursor;
GN   Name=COX10; OrderedLocusNames=YALI0F23727g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O.
CC       {ECO:0000250}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P24009};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382132; CAG78611.1; -; Genomic_DNA.
DR   RefSeq; XP_505800.1; XM_505800.1.
DR   AlphaFoldDB; Q6C0L2; -.
DR   SMR; Q6C0L2; -.
DR   STRING; 4952.CAG78611; -.
DR   EnsemblFungi; CAG78611; CAG78611; YALI0_F23727g.
DR   GeneID; 2908754; -.
DR   KEGG; yli:YALI0F23727g; -.
DR   VEuPathDB; FungiDB:YALI0_F23727g; -.
DR   HOGENOM; CLU_029631_2_1_1; -.
DR   InParanoid; Q6C0L2; -.
DR   OMA; MGREPDF; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
DR   GO; GO:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006784; P:heme A biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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; IPR016315; Protohaem_IX_farnesylTrfase_mt.
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   PIRSF; PIRSF001773; COX10; 1.
DR   TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
KW   Heme biosynthesis; Membrane; Mitochondrion; Reference proteome;
KW   Transferase; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..60
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           61..471
FT                   /note="Protoheme IX farnesyltransferase, mitochondrial"
FT                   /id="PRO_0000045421"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  51187 MW;  38958CB4D963D58F CRC64;
     MLLSNVAVNR TVVHTQLVSG SRSALHALSR TSHSVPVTHT HQRRHIFSHK RRLSSSTLAI
     PFALSNTNSA TTAPLQFLSN VSLCRVTPGT ITTSAKATAP NLDKMSAEAA TTAAQASASP
     VEDSFLKKAV SCQSETEREA VMAARAAKKA LRETKETWWA PYVALTKPRL TVLVVLSAMS
     SYALTPEAVS LTNLLFLTVG TALCSGSANA INMGREPAYD SMMTRTRGRP VVRGAVTPNQ
     AFTFAGITGT VGTAALYFGV NPTVAILGAS NIALYGGLYT TLKRKHIINT WVGAVVGAIP
     PLMGWAASGG SLLHPGAWCL AGLLYAWQFP HFNALSYSIR DEYKKAGYVM TAWKNPGLNA
     RVGLRYALLM FPLCVGLSYY NVTDWWFVLD SSVLNAWMAW WAFKFWQQEN VNIALAAAGK
     QYSQNPFARK LFWGSVVHLP GVLLLAMIHK KGQWDWLFGP SEDEKKKTLS S