COX10_GIBZE
ID COX10_GIBZE Reviewed; 507 AA.
AC Q4I5G1; A0A0E0SGC1; V6RGV1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=FGRRES_07547, FGSG_07547;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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; DS231666; ESU13818.1; -; Genomic_DNA.
DR EMBL; HG970335; CEF85484.1; -; Genomic_DNA.
DR RefSeq; XP_011327325.1; XM_011329023.1.
DR AlphaFoldDB; Q4I5G1; -.
DR SMR; Q4I5G1; -.
DR STRING; 5518.FGSG_07547P0; -.
DR EnsemblFungi; ESU13818; ESU13818; FGSG_07547.
DR GeneID; 23554619; -.
DR KEGG; fgr:FGSG_07547; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G25069; -.
DR eggNOG; KOG1380; Eukaryota.
DR HOGENOM; CLU_029631_2_0_1; -.
DR InParanoid; Q4I5G1; -.
DR Proteomes; UP000070720; Chromosome 4.
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 ?..507
FT /note="Protoheme IX farnesyltransferase, mitochondrial"
FT /id="PRO_0000045416"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 72..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 55397 MW; FCACC851BE274587 CRC64;
MRPPRCLFPA AEILLKAPPS RRCMSSAAAF QPPKIVAAIP WKGSSFFLSN RLFDRSTCLD
FVVLRRANGI RSTSASASTT HDSTLSSSPT ANHSTSAHKD HKIAPHRKRQ AQRREKAAAE
AAAAAARGEK PLPPDASSLL AAHAASQTSP LRRHLSACLS LAKPRLTMLV VLTAMATYAL
YPVPEMLSPS TTETPSLSPL TLLFLTIGTT FCSASANALN MLYEPSTDAK MTRTRNRPLV
RNLISKRAAV LFAILSGFVG TGALYFGVNP TVSGLGFANI VIYAGMYTPL KAVTAFNTWI
GAVVGGIPPL MGWAAAAGET ATKDGSWREL LFASDGSSIG GWVMAGLLFA WQFPHFMALS
WPIREEYKKA GLRMLAWTNP ARNGRVALRY SFVFIPLCLS LCAAGVTEWS FAVTSFPINA
WLIRESVRFW RYEGNKGSAR GLFWASVWHL PGVMILALLH KKGMWTRVWR SVFGEDEGEW
EEEELDEMMS VAVANTNSHM QNQKTVR