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COX10_MAGO7
ID   COX10_MAGO7             Reviewed;         552 AA.
AC   P0C150; A4QWN3; G4N4A4;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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; ORFNames=MGG_05944;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001233; EHA51972.1; -; Genomic_DNA.
DR   RefSeq; XP_003711779.1; XM_003711731.1.
DR   AlphaFoldDB; P0C150; -.
DR   SMR; P0C150; -.
DR   STRING; 318829.MGG_05944T0; -.
DR   EnsemblFungi; MGG_05944T0; MGG_05944T0; MGG_05944.
DR   GeneID; 2684031; -.
DR   KEGG; mgr:MGG_05944; -.
DR   VEuPathDB; FungiDB:MGG_05944; -.
DR   eggNOG; KOG1380; Eukaryota.
DR   HOGENOM; CLU_029631_2_0_1; -.
DR   InParanoid; P0C150; -.
DR   OMA; YGMYPIS; -.
DR   OrthoDB; 1260807at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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:0008495; F:protoheme IX farnesyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..552
FT                   /note="Protoheme IX farnesyltransferase, mitochondrial"
FT                   /id="PRO_0000045418"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          118..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  58840 MW;  1192112C4B442D07 CRC64;
     MPGPRASLPS LSAVDNVCWR CCSSSSGRPV PGQRLRGFAI ANQARPLSTS PVRPLRFGAT
     TTVRAAASQS PRPNGAYFLS NVLLERFGGF QFSPRSRAIA GTSGSNISNT KRNATVAAAD
     IPPSTSTPRP QVDEELPPHR RRQAARRTAE QAASASSNAP SEAAQTTPVT PPPAAPSGEI
     PPDASSILSN AAAAQPAQSL RRRLTTLLAL SKPRLTMLVV LSAMVPYALY PVPDFLTPGV
     SAPSLSPLTL LFLTTGTTLC SAAANALNMI YEPKTDALMS RTRTRPLVRN LVTTRAAVCF
     ALFCATTGIL ALQFGVNPTV AFLGAANIVL YAGIYTPLKR VSALNTWVGA VVGGIPPLMG
     WAAAAGESAV GDGSWRELLL APDGSSAGGW LFAALLFTWQ FPHFMALSWG VRDEYRAAGL
     RMLAWTNPAR NARVALRYGL VFVPLCVGLC AVGVTEWSFA VTSLPVNLWL ARESIRFWQT
     QGAAGSARGL FWASVWHLPV VMVLALLQKK GMWGRVWRSV FGEPDLDDDL ASDDGWEYLD
     ESEEPPAVTT RS
 
 
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