COQ1_NEUCR
ID COQ1_NEUCR Reviewed; 449 AA.
AC Q7S565;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable hexaprenyl pyrophosphate synthase, mitochondrial;
DE Short=HPS;
DE EC=2.5.1.-;
DE Flags: Precursor;
GN ORFNames=NCU02305;
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: 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; CM002242; EAA30713.1; -; Genomic_DNA.
DR RefSeq; XP_959949.1; XM_954856.2.
DR AlphaFoldDB; Q7S565; -.
DR SMR; Q7S565; -.
DR STRING; 5141.EFNCRP00000003125; -.
DR PRIDE; Q7S565; -.
DR EnsemblFungi; EAA30713; EAA30713; NCU02305.
DR GeneID; 3876064; -.
DR KEGG; ncr:NCU02305; -.
DR VEuPathDB; FungiDB:NCU02305; -.
DR HOGENOM; CLU_014015_1_0_1; -.
DR InParanoid; Q7S565; -.
DR OMA; RVAKYYT; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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 ?..449
FT /note="Probable hexaprenyl pyrophosphate synthase,
FT mitochondrial"
FT /id="PRO_0000016475"
FT BINDING 122
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 125
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 200
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
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 216
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 300
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 449 AA; 48473 MW; 2E4B709E38D169C6 CRC64;
MQLRTGAASV VRTGLGLTQS RCAVQSLTAV PLERRIRQSK AFYHNTKKND SAWAAAVSVA
GNIVNNAVTK AIKGTDGLPT IDPLRLVAGE MKFLTGNIRK LLGSGHPSLD RAAKYYTQAE
GKHVRPLIVL LMSRATALCP KAPQRQQSTL QASAAIDTSI SPLNILSDFN PSDATPVSIP
ADTDILPSQR RLAEITELIH TASLLHDDVI DHSESRRGAP SANLEFGNKM AVLAGDFLLG
RASVALARLR HAEVVELLAT VIANLVEGEF MQLKNTARDE KNPKWSEETL TYYLQKTYLK
TASLISKSCR ASALLGGADA ATVDAAYLYG KNLGLAFQLV DDMLDYTRSE KELGKPAGAD
LELGLATAPL LFAWKTMPEL GPLVGRKFEK EGDAARAREL VLQSNGIEQT RALAQDYAEK
AIEAISGFPD SEAKDGLIEM AVKTLKRNK
