COX10_ASHGO
ID COX10_ASHGO Reviewed; 435 AA.
AC Q75F43;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Protoheme IX farnesyltransferase, mitochondrial;
DE EC=2.5.1.-;
DE AltName: Full=Heme O synthase;
DE Flags: Precursor;
GN Name=COX10; OrderedLocusNames=AAL115W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE016814; AAS50251.1; -; Genomic_DNA.
DR RefSeq; NP_982427.1; NM_207780.1.
DR AlphaFoldDB; Q75F43; -.
DR SMR; Q75F43; -.
DR STRING; 33169.AAS50251; -.
DR EnsemblFungi; AAS50251; AAS50251; AGOS_AAL115W.
DR GeneID; 4618542; -.
DR KEGG; ago:AGOS_AAL115W; -.
DR eggNOG; KOG1380; Eukaryota.
DR HOGENOM; CLU_029631_2_1_1; -.
DR InParanoid; Q75F43; -.
DR OMA; MGREPDF; -.
DR Proteomes; UP000000591; Chromosome I.
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:InterPro.
DR GO; GO:0006784; P:heme A biosynthetic process; IEA:EnsemblFungi.
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 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..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..435
FT /note="Protoheme IX farnesyltransferase, mitochondrial"
FT /id="PRO_0000045411"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 435 AA; 48116 MW; DA133FDAEBDD89E2 CRC64;
MPALCATYLI HSGNLRACLR IVPLTKPSVV IAYRHLSKSS SKIAPAAALN TAPIEFTPNT
SAASLHERST VIKDAARSAL RCNDTTPTPA LPFDVKRVDK ANRAAGRKLP AASGVLSAYA
LMGPYIQLAK PRLTVLVMLS AICSYALSPY PATVLELLSL TVGTTLCSAA ANGINMGREP
DFDRQMMRTQ ARPVVRGLVT PMQAYKFSAV SGVIGTAILY AGVNPTVALL GASNIVLYSW
FYTSLKRKHI INTWFGAITG AIPPLMGWAA ASPLTHPGCW CLAGLLYAWQ FPHFNTLSHN
IRNEYKNAGH VMTAWKNPKL NARVALRYSL LMFPLCFGLS YYGITDWTYQ IDSALVNGWM
SFWAFKFWWQ QRYNYSKKVY NNKAEFNKGM VLANVYARKT FWVSVLHLPA VLILAIVHKK
GRWDWLFSDE GKLVA