COQ9_ASHGO
ID COQ9_ASHGO Reviewed; 246 AA.
AC Q75CR6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ubiquinone biosynthesis protein COQ9, mitochondrial;
DE Flags: Precursor;
GN Name=COQ9; OrderedLocusNames=ACL147W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Lipid-binding protein involved in the biosynthesis of
CC coenzyme Q, also named ubiquinone, an essential lipid-soluble electron
CC transporter for aerobic cellular respiration.
CC {ECO:0000250|UniProtKB:O75208, ECO:0000250|UniProtKB:Q05779}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000250|UniProtKB:Q05779}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q05779}.
CC -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000305}.
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DR EMBL; AE016816; AAS51081.1; -; Genomic_DNA.
DR RefSeq; NP_983257.1; NM_208610.1.
DR AlphaFoldDB; Q75CR6; -.
DR SMR; Q75CR6; -.
DR STRING; 33169.AAS51081; -.
DR EnsemblFungi; AAS51081; AAS51081; AGOS_ACL147W.
DR GeneID; 4619377; -.
DR KEGG; ago:AGOS_ACL147W; -.
DR eggNOG; KOG2969; Eukaryota.
DR HOGENOM; CLU_057411_1_1_1; -.
DR InParanoid; Q75CR6; -.
DR OMA; WFLAGDK; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:EnsemblFungi.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR GO; GO:1901006; P:ubiquinone-6 biosynthetic process; IEA:EnsemblFungi.
DR InterPro; IPR013718; COQ9.
DR InterPro; IPR012762; Ubiq_biosynth_COQ9.
DR PANTHER; PTHR21427; PTHR21427; 1.
DR Pfam; PF08511; COQ9; 1.
DR TIGRFAMs; TIGR02396; diverge_rpsU; 1.
PE 3: Inferred from homology;
KW Lipid-binding; Mitochondrion; Reference proteome; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..58
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 59..246
FT /note="Ubiquinone biosynthesis protein COQ9, mitochondrial"
FT /id="PRO_0000227685"
FT BINDING 175..178
FT /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:57613"
FT /evidence="ECO:0000250|UniProtKB:O75208"
SQ SEQUENCE 246 AA; 27484 MW; 1DF790D6DF089210 CRC64;
MFRVCRRLYH PNTLEHAVGN RLRPLAYEQD SPQYKVLQRA LEAHVPVLGF NERAIVRAAG
DLGYGSAVLS ALAAPNSPAL LNVPSAVLEL VKFHLVTKRV ALADAAAQGN VSMEQLFLQR
VEADRPLAGQ LTQLLSILSL PGEFLVNTAM PELFRLSDDL IYYSGEKDHP DLAWYSKRAA
VAMAYVSTNL FMARDRSPAL EETLHFARRR LQQVDSLGTA YNNVEEFAWY QLLMAMNLVK
SQLTRG
