COQ2_DICDI
ID COQ2_DICDI Reviewed; 463 AA.
AC Q54U71;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_03189};
DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=PHB:PPT {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=PHB:polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
GN Name=coq2 {ECO:0000255|HAMAP-Rule:MF_03189}; ORFNames=DDB_G0281241;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with
CC an all-trans polyprenyl group. Mediates the second step in the final
CC reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the
CC condensation of the polyisoprenoid side chain with PHB.
CC -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with
CC an all-trans polyprenyl group. Mediates the second step in the final
CC reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the
CC condensation of the polyisoprenoid side chain with PHB, generating the
CC first membrane-bound Q intermediate. {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-
CC hydroxy-3-all-trans-polyprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:44504, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9564,
CC ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58914,
CC ChEBI:CHEBI:78396; EC=2.5.1.39; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03189};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03189};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03189}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03189}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03189}.
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; AAFI02000040; EAL66917.1; -; Genomic_DNA.
DR RefSeq; XP_640905.1; XM_635813.1.
DR AlphaFoldDB; Q54U71; -.
DR SMR; Q54U71; -.
DR STRING; 44689.DDB0231591; -.
DR PaxDb; Q54U71; -.
DR EnsemblProtists; EAL66917; EAL66917; DDB_G0281241.
DR GeneID; 8622964; -.
DR KEGG; ddi:DDB_G0281241; -.
DR dictyBase; DDB_G0281241; coq2.
DR eggNOG; KOG1381; Eukaryota.
DR HOGENOM; CLU_034879_0_2_1; -.
DR InParanoid; Q54U71; -.
DR OMA; VINDMAD; -.
DR PhylomeDB; Q54U71; -.
DR Reactome; R-DDI-1268020; Mitochondrial protein import.
DR Reactome; R-DDI-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q54U71; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:dictyBase.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; ISS:dictyBase.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:dictyBase.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubiquinone biosynthesis.
FT CHAIN 1..463
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000328211"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 51925 MW; 00E676D1035B59F3 CRC64;
MIKSILSLQN FKFIKPCTNS SILKYNNNNN TNNNNNNNGI NKYNSTFNNN NSNFSNKNLF
SSKQYQQQSI CNIPILSTIS YHNKNNTNIN TIINNNNSSN NNLINLNDKF NNLNNKTSPI
IFNKNYSTTV STLLDDNNSN SNNNNNSNNN KPSTTFVNDW ISKFPNSVQP YLRLSRVDKP
IGVWLLLYPC CWSISLAAPA GSFPDLKTML VFGIGAYVMR SAGCVINDMA DYKFDSKVER
TKTRPIASKQ LTHKQSLIFL GGQLLASFGL ILSSLNYYTI ALCASSLPIV VLYPFMKRFT
YYPQFVLGLA FNWGALAGYS AIAGSCNWSI VAPLYLAGIS WTMVYDTIYA HQDKRDDILV
GVKSTALKFA EKSRIILSVF SGLVISGMFL TGIAANMPLF YYLGTAACSS HLIWQLKTVD
FNNPSSCLEK FISNKNFGLY FLLIIIVSKL LQDKENENEI QKK
