COX10_NEUCR
ID COX10_NEUCR Reviewed; 511 AA.
AC Q7S5E7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Protoheme IX farnesyltransferase, mitochondrial;
DE EC=2.5.1.-;
DE AltName: Full=Heme O synthase;
DE AltName: Full=Protoheme farnesyltransferase 1;
DE Flags: Precursor;
GN Name=pft-1; Synonyms=cox10; ORFNames=NCU06141;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002242; EAA30767.2; -; Genomic_DNA.
DR RefSeq; XP_960003.2; XM_954910.2.
DR AlphaFoldDB; Q7S5E7; -.
DR SMR; Q7S5E7; -.
DR STRING; 5141.EFNCRP00000005348; -.
DR EnsemblFungi; EAA30767; EAA30767; NCU06141.
DR GeneID; 3876125; -.
DR KEGG; ncr:NCU06141; -.
DR VEuPathDB; FungiDB:NCU06141; -.
DR HOGENOM; CLU_029631_2_0_1; -.
DR InParanoid; Q7S5E7; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..511
FT /note="Protoheme IX farnesyltransferase, mitochondrial"
FT /id="PRO_0000045419"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 54111 MW; A937862566ACD806 CRC64;
MSSSTESLPG TLRRTLTTSR APAATSSQRL KAGYFVSNAF LPRVKANGIH DSASSQRSTT
VASTTSTTAD AADGSSSTTQ PTTAADLPPV DNTLLPHRRR QAQRKAAAAA AAAAANGETP
TPLINPDAPT ADLAPDASSQ LAAAAASAPA DSLKRRLSSL LSLSKPRLTV LVVLSAMVPY
ALYPVPSFLT SSALDTSLAP SLSPLTLLFL TTGTTLCSAS ANALNMLYEP DTDSKMTRTR
TRPLVRRLLT TKAAVLFAVG CGLAGTLALY FGVNPTVSFL GAANIALYAG AYTPLKRISA
VNTWVGAIVG GIPPLMGWAA AAGESATGDG TWRELLFASD GSSLGGWLFA GLLFAWQFPH
FMPLSWGIRH EYKAAGLRML AWTNPARNGR VALRYSLAFI PLCVGLSATG VTEWSFAVTS
LPVNAWLVWE AIKFWRLEGH KGSARGLFWA SVWHLPVIMV LALAQKKGMW GRVWRSVFGE
PEEEEGEWVY EDEDEEEGGG VGEVVKGVVK K
