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COX10_ASPFU
ID   COX10_ASPFU             Reviewed;         512 AA.
AC   Q4WP81;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-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=AFUA_4G08340;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000005; EAL89953.1; -; Genomic_DNA.
DR   RefSeq; XP_751991.1; XM_746898.1.
DR   AlphaFoldDB; Q4WP81; -.
DR   SMR; Q4WP81; -.
DR   STRING; 746128.CADAFUBP00006370; -.
DR   EnsemblFungi; EAL89953; EAL89953; AFUA_4G08340.
DR   GeneID; 3509179; -.
DR   KEGG; afm:AFUA_4G08340; -.
DR   VEuPathDB; FungiDB:Afu4g08340; -.
DR   eggNOG; KOG1380; Eukaryota.
DR   HOGENOM; CLU_029631_2_0_1; -.
DR   InParanoid; Q4WP81; -.
DR   OMA; YGMYPIS; -.
DR   OrthoDB; 1260807at2759; -.
DR   Proteomes; UP000002530; 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: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: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..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..512
FT                   /note="Protoheme IX farnesyltransferase, mitochondrial"
FT                   /id="PRO_0000045412"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          91..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  55840 MW;  47D570FEE8B66264 CRC64;
     MIYLRSSLLR SGLARDPARL CSQCFSRLSP SRRPVAVRSF FSSSRLRAGI ADHESTPSTV
     QKTYFSANRT ADGLLASLSA VNSSPRSIAD NALSQGAASS ESITSQSTSQ ELPHRRRKRL
     KEEAAKNNAA ETELPPDASS QLSTLSSALP ATSLRRKLAA FLALTKPRLS FLIVLTTTSA
     YGMYPISSLL TLDPSMTPLP TLSTSTLTFL YLTTGTFLSS CSANTLNMLL EPKYDALMSR
     TRNRPLVRGL LSRRAAVLFA IATAAAGLGL LYIGTNPTTT ALSASNICLY AFVYTPLKRI
     SVINTWVGAV VGGIPPLMGW TAAAGQTATT GHDSWRDMLF SKDSIGGWLL GGILFAWQFP
     HFNALSYMIR EEYKAAGYRM LAWTNPAANA RVALRYSLLM FPFSVGLWWV GVVGNGFLVG
     STAANGWLVK EAYKFWRHQG ANGSARRLFW ASIWQLPILL VGGLVTKKGL WDGVWNNVFG
     QPVEDEDDYL WEDEDEVAEA ERKMIPAKTS SS
 
 
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