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