ID   COQ9B_XENLA             Reviewed;         293 AA.
AC   Q5PPX7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Ubiquinone biosynthesis protein COQ9-B, mitochondrial;
DE   Flags: Precursor;
GN   Name=coq9-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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. Binds a phospholipid of
CC       at least 10 carbons in each acyl group. {ECO:0000250|UniProtKB:O75208}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000250|UniProtKB:Q8K1Z0}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O75208}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}.
CC   -!- DOMAIN: Structurally similar to the bacterial FadR protein (fatty acid
CC       metabolism regulator protein). {ECO:0000250|UniProtKB:O75208}.
CC   -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000305}.
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DR   EMBL; BC087448; AAH87448.1; -; mRNA.
DR   RefSeq; NP_001088784.1; NM_001095315.1.
DR   AlphaFoldDB; Q5PPX7; -.
DR   SMR; Q5PPX7; -.
DR   DNASU; 496049; -.
DR   GeneID; 496049; -.
DR   KEGG; xla:496049; -.
DR   CTD; 496049; -.
DR   Xenbase; XB-GENE-6252821; coq9.S.
DR   OrthoDB; 1304924at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 496049; Expressed in muscle tissue and 20 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Lipid-binding; Mitochondrion; Reference proteome; Transit peptide;
KW   Ubiquinone biosynthesis.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..293
FT                   /note="Ubiquinone biosynthesis protein COQ9-B,
FT                   mitochondrial"
FT                   /id="PRO_0000228641"
FT   REGION          21..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         216..219
FT                   /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT                   /ligand_id="ChEBI:CHEBI:57613"
FT                   /evidence="ECO:0000250|UniProtKB:O75208"
SQ   SEQUENCE   293 AA;  32805 MW;  1D000852A72F2DBE CRC64;
     MLVLTQPFLL MPRKLWVSSA LRSDDQKQPP FSSSSTHAET PEHAEEQYQQ QQSPPRYTDQ
     AGEESEDYES EEQLQQRILT AALQFVPDFG WSADAIAEGA KSLDMSAAAG GMFEDGGSEL
     VLHFVTQCNL QLTELLEKEH KLVQLGTSEK KPTAQFLRDA VKARLRMHIP YIEQWPQALG
     MLLLPRNIPS SLKLLSAMVD DMWHYAGDQS TDVSWYTSRA VLTGIYNSTE LVMLQDSSPD
     FEDTWKFLEN RISEAMTMGN SMKQVASTGE AVIQGLMGAA VTLKNLTGLN QRR