COQ2_ARATH
ID COQ2_ARATH Reviewed; 407 AA.
AC Q93YP7; Q9FRU7; Q9SUR1;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 Short=4HPT;
DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_03189};
DE AltName: Full=4-hydroxybenzoate nonaprenyltransferase {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};
DE AltName: Full=Polyprenyltransferase 1;
DE Short=AtPPT1;
DE Flags: Precursor;
GN Name=PPT1 {ECO:0000255|HAMAP-Rule:MF_03189}; OrderedLocusNames=At4g23660;
GN ORFNames=F9D16.130;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija-2;
RX PubMed=15604701; DOI=10.1007/s11103-004-1298-4;
RA Okada K., Ohara K., Yazaki K., Nozaki K., Uchida N., Kawamukai M.,
RA Nojiri H., Yamane H.;
RT "The AtPPT1 gene encoding 4-hydroxybenzoate polyprenyl diphosphate
RT transferase in ubiquinone biosynthesis is required for embryo development
RT in Arabidopsis thaliana.";
RL Plant Mol. Biol. 55:567-577(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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. Required for embryo development.
CC {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15604701}.
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, ECO:0000269|PubMed:15604701}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side
CC {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q93YP7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:15604701}.
CC -!- DISRUPTION PHENOTYPE: Arrest of embryo development at an early stage of
CC zygotic embryogenesis. {ECO:0000269|PubMed:15604701}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79321.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB052553; BAB20818.2; -; mRNA.
DR EMBL; AL035394; CAA23032.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161559; CAB79321.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84790.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84791.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67087.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67088.1; -; Genomic_DNA.
DR EMBL; AY059864; AAL24346.1; -; mRNA.
DR EMBL; BT008496; AAP37855.1; -; mRNA.
DR PIR; T05598; T05598.
DR RefSeq; NP_001320050.1; NM_001341624.1. [Q93YP7-1]
DR RefSeq; NP_001328939.1; NM_001341625.1. [Q93YP7-1]
DR RefSeq; NP_567688.1; NM_118497.4. [Q93YP7-1]
DR RefSeq; NP_849431.1; NM_179100.4. [Q93YP7-1]
DR AlphaFoldDB; Q93YP7; -.
DR SMR; Q93YP7; -.
DR STRING; 3702.AT4G23660.3; -.
DR PRIDE; Q93YP7; -.
DR ProteomicsDB; 240952; -. [Q93YP7-1]
DR EnsemblPlants; AT4G23660.1; AT4G23660.1; AT4G23660. [Q93YP7-1]
DR EnsemblPlants; AT4G23660.2; AT4G23660.2; AT4G23660. [Q93YP7-1]
DR EnsemblPlants; AT4G23660.4; AT4G23660.4; AT4G23660. [Q93YP7-1]
DR EnsemblPlants; AT4G23660.5; AT4G23660.5; AT4G23660. [Q93YP7-1]
DR GeneID; 828466; -.
DR Gramene; AT4G23660.1; AT4G23660.1; AT4G23660. [Q93YP7-1]
DR Gramene; AT4G23660.2; AT4G23660.2; AT4G23660. [Q93YP7-1]
DR Gramene; AT4G23660.4; AT4G23660.4; AT4G23660. [Q93YP7-1]
DR Gramene; AT4G23660.5; AT4G23660.5; AT4G23660. [Q93YP7-1]
DR KEGG; ath:AT4G23660; -.
DR Araport; AT4G23660; -.
DR eggNOG; KOG1381; Eukaryota.
DR PhylomeDB; Q93YP7; -.
DR BioCyc; MetaCyc:MON-17042; -.
DR BRENDA; 2.5.1.39; 399.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q93YP7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93YP7; baseline and differential.
DR Genevisible; Q93YP7; AT.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Isoprene biosynthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CHAIN 21..407
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000405435"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 279..299
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"
SQ SEQUENCE 407 AA; 44604 MW; 3A4E4941A1413A9C CRC64;
MAFFGLSRVS RRLLKSSVSV TPSSSSALLQ SQHKSLSNPV TTHYTNPFTK CYPSWNDNYQ
VWSKGRELHQ EKFFGVGWNY RLICGMSSSS SVLEGKPKKD DKEKSDGVVV KEASWIDLYL
PEEVRGYAKL ARLDKPIGTW LLAWPCMWSI ALAADPGSLP SFKYMALFGC GALLLRGAGC
TINDLLDQDI DTKVDRTKLR PIASGLLTPF QGIGFLGLQL LLGLGILLQL NNYSRVLGAS
SLLLVFSYPL MKRFTFWPQA FLGLTINWGA LLGWTAVKGS IAPSIVLPLY LSGVCWTLVY
DTIYAHQDKE DDVKVGVKST ALRFGDNTKL WLTGFGTASI GFLALSGFSA DLGWQYYASL
AAASGQLGWQ IGTADLSSGA DCSRKFVSNK WFGAIIFSGV VLGRSFQ
