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 01-MAY-2013, entry version 50.
DE RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial;
DE EC=2.5.1.39;
DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase;
DE Short=PHB:polyprenyltransferase;
DE Flags: Precursor;
GN Name=coq2; ORFNames=DDB_G0281241;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; 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.,
RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA 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.,
RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA 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)
CC with an all-trans polyprenyl group. Mediates the second step in
CC the final reaction sequence of coenzyme Q (CoQ) biosynthesis,
CC which is the condensation of the polyisoprenoid side chain with
CC PHB.
CC -!- CATALYTIC ACTIVITY: A polyprenyl diphosphate + 4-hydroxybenzoate =
CC diphosphate + a 4-hydroxy-3-polyprenylbenzoate.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
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DR EMBL; AAFI02000040; EAL66917.1; -; Genomic_DNA.
DR RefSeq; XP_640905.1; XM_635813.1.
DR STRING; 44689.DDB_0231591; -.
DR EnsemblProtists; DDB0231591; DDB0231591; DDB_G0281241.
DR GeneID; 8622964; -.
DR KEGG; ddi:DDB_G0281241; -.
DR dictyBase; DDB_G0281241; coq2.
DR eggNOG; COG0382; -.
DR KO; K06125; -.
DR OMA; VINDMAD; -.
DR ProtClustDB; CLSZ2430582; -.
DR UniPathway; UPA00232; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:dictyBase.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:EC.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; ISS:dictyBase.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:dictyBase.
DR InterPro; IPR006370; HB_polyprenyl-transferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 3: Inferred from homology;
KW Complete proteome; Isoprene biosynthesis; Membrane; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix; Ubiquinone biosynthesis.
FT TRANSIT 1 20 Mitochondrion (Potential).
FT CHAIN 21 463 4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial.
FT /FTId=PRO_0000328211.
FT TRANSMEM 181 201 Helical; (Potential).
FT TRANSMEM 206 226 Helical; (Potential).
FT TRANSMEM 257 277 Helical; (Potential).
FT TRANSMEM 305 325 Helical; (Potential).
FT TRANSMEM 330 350 Helical; (Potential).
FT TRANSMEM 375 395 Helical; (Potential).
FT TRANSMEM 431 451 Helical; (Potential).
FT COMPBIAS 26 38 Poly-Asn.
FT COMPBIAS 48 53 Poly-Asn.
FT COMPBIAS 94 97 Poly-Asn.
FT COMPBIAS 137 150 Poly-Asn.
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
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