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