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COX10_DICDI
ID   COX10_DICDI             Reviewed;         449 AA.
AC   Q54JB3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Probable protoheme IX farnesyltransferase, mitochondrial;
DE            EC=2.5.1.-;
DE   AltName: Full=Heme O synthase;
DE   Flags: Precursor;
GN   Name=cox10; ORFNames=DDB_G0288169;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O.
CC       {ECO:0000250}.
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; AAFI02000109; EAL63372.1; -; Genomic_DNA.
DR   RefSeq; XP_636880.1; XM_631788.1.
DR   AlphaFoldDB; Q54JB3; -.
DR   SMR; Q54JB3; -.
DR   STRING; 44689.DDB0231473; -.
DR   PaxDb; Q54JB3; -.
DR   EnsemblProtists; EAL63372; EAL63372; DDB_G0288169.
DR   GeneID; 8626492; -.
DR   KEGG; ddi:DDB_G0288169; -.
DR   dictyBase; DDB_G0288169; cox10.
DR   eggNOG; KOG1380; Eukaryota.
DR   HOGENOM; CLU_610348_0_0_1; -.
DR   InParanoid; Q54JB3; -.
DR   OMA; VTPLNTW; -.
DR   PhylomeDB; Q54JB3; -.
DR   Reactome; R-DDI-189451; Heme biosynthesis.
DR   PRO; PR:Q54JB3; -.
DR   Proteomes; UP000002195; Chromosome 5.
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; ISS:dictyBase.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
DR   GO; GO:0008495; F:protoheme IX farnesyltransferase activity; ISS:dictyBase.
DR   GO; GO:0006784; P:heme A biosynthetic process; ISS:dictyBase.
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; IPR044878; UbiA_sf.
DR   PANTHER; PTHR43448; PTHR43448; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   PIRSF; PIRSF001773; COX10; 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           ?..449
FT                   /note="Probable protoheme IX farnesyltransferase,
FT                   mitochondrial"
FT                   /id="PRO_0000327206"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          99..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  50427 MW;  11ADA67B9FA8AE19 CRC64;
     MMLSKIINNI SKSGLRNTTN SKNGGLLYFQ NYYMKSSTTI TRLNSGNNNY SNNNNNNNNI
     ILNDKFLNKQ QNDKKIIYNN IFEEKNQFLK RIYSTSTTTT STTTTTNINE NNIKNENNNE
     NNNENSNNNN EQSIKSNQTK SKGFLRGPYM TLIKLPITVY VTLTAIAGYV AACPIGAFDW
     VVLSQVSIGT FLASCSANIH NQEIEVQHDR KMPRTKDRPL VIGTINRGKA WVGSIALLTL
     GFGTMAVTPS LFVPGTLAAC NVILYCWYTD LKRVTPLNTW IGAFVGAIPP LIGSVAATGE
     FEAIGMLLAT FMYIWQIPHF LALSQVLREQ YRGAGYKMLS VTHEKKTVDR VSLAHALFGI
     PLPFIFDYFF NFNVHPITLT CMALSSASLA LPFITKISPK RLYIISLISL PITLFLSCLL
     RQPFAYYTDD DDEDKDKDNQ NQIENQDKK
 
 
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