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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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