COQ1_YARLI
ID COQ1_YARLI Reviewed; 452 AA.
AC Q6CBH3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable hexaprenyl pyrophosphate synthase, mitochondrial;
DE Short=HPS;
DE EC=2.5.1.-;
DE Flags: Precursor;
GN Name=COQ1; OrderedLocusNames=YALI0C18755g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Assembly of polyisoprenoid side chains. The polyprenyl
CC synthase of coenzyme Q biosynthesis catalyzes the formation from
CC isopentenyl diphosphate of all trans-polyprenyl pyrophosphates
CC generally ranging in length of between 6 and 10 isoprene units
CC depending on the species (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; CR382129; CAG82309.1; -; Genomic_DNA.
DR RefSeq; XP_501989.1; XM_501989.1.
DR AlphaFoldDB; Q6CBH3; -.
DR SMR; Q6CBH3; -.
DR STRING; 4952.CAG82309; -.
DR EnsemblFungi; CAG82309; CAG82309; YALI0_C18755g.
DR GeneID; 2909963; -.
DR KEGG; yli:YALI0C18755g; -.
DR VEuPathDB; FungiDB:YALI0_C18755g; -.
DR HOGENOM; CLU_014015_1_0_1; -.
DR InParanoid; Q6CBH3; -.
DR OMA; RVAKYYT; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0032476; C:decaprenyl diphosphate synthase complex; IEA:EnsemblFungi.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:EnsemblFungi.
DR GO; GO:1990234; C:transferase complex; IBA:GO_Central.
DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0000010; F:trans-hexaprenyltranstransferase activity; IEA:EnsemblFungi.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:EnsemblFungi.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..452
FT /note="Probable hexaprenyl pyrophosphate synthase,
FT mitochondrial"
FT /id="PRO_0000016476"
FT BINDING 108
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 111
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 204
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 220
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 303
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 49382 MW; 63F08EAFB2CE6DC4 CRC64;
MLRVGRIGTK TLASSSLRFV AGARPKSTLT EAVLETTGLL KTTPQNPEWS GAVKQASRLV
ETDTPIRDPF SIVSQEMSTL ANNIGSLIGS GHPTLNKVAT YYFQSEGKHV RPLIVLLLSR
ALSAIPESER DRGTFDASDV TENVGELNPE PSINDPLSPI EILHGINPDI VLNPLSRPSD
PLPYESNGIL PKQRRLAEIV EMIHTASLLH DDVIDNSATR RGSPTGNVAF GNKMAILAGD
FLLGRASVAI ARLRNAEVIE LLSTTIANLV EGEFMQLKNT IVDNSEIANK ATFEYYIHKT
YLKTASLMSK SCRAAAVLSG ARNPIVDASY KFGKNLGLCF QVVDDMLDYS EGESHLGKPA
GADLKLGLAT APVLFAWEKY PELGDMIKRK FDGPGDVERA RFLVQQADGL SRTRELAQKY
CDEAVANLDL LPYSESREAL RNLTMKMMNR SK
