ID A0A421JHZ6_9ASCO Unreviewed; 762 AA.
AC A0A421JHZ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03189};
DE Short=4-HB polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_03189};
DE EC=2.5.1.39 {ECO:0000256|HAMAP-Rule:MF_03189};
DE AltName: Full=4-hydroxybenzoate hexaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_03189};
DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_03189};
DE Short=PHB:PPT {ECO:0000256|HAMAP-Rule:MF_03189};
DE Short=PHB:polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_03189};
GN Name=COQ2 {ECO:0000256|HAMAP-Rule:MF_03189};
GN ORFNames=JA1_005072 {ECO:0000313|EMBL:RLV89629.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV89629.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV89629.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV89629.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_03189};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03189};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03189}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03189}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03189}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03189}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005985, ECO:0000256|HAMAP-Rule:MF_03189}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV89629.1}.
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DR EMBL; NSGQ01000068; RLV89629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JHZ6; -.
DR STRING; 2028339.A0A421JHZ6; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000285775; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03144; GATase1_ScBLP_like; 1.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; UbiA prenyltransferase; 1.
DR Gene3D; 1.20.120.1780; UbiA prenyltransferase; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR019197; Biotin-prot_ligase_N.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR029062; Class_I_gatase-like.
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 NCBIfam; TIGR01474; ubiA_proteo; 1.
DR PANTHER; PTHR11048:SF28; 4-HYDROXYBENZOATE POLYPRENYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11048; PRENYLTRANSFERASES; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF09825; BPL_N; 1.
DR Pfam; PF01040; UbiA; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_03189};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03189};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03189};
KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03189};
KW Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03189};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03189};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03189}; Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03189}.
FT TRANSMEM 585..601
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT TRANSMEM 613..641
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT TRANSMEM 702..719
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT TRANSMEM 740..761
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT DOMAIN 1..225
FT /note="Biotin-protein ligase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09825"
FT DOMAIN 329..441
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|Pfam:PF03099"
SQ SEQUENCE 762 AA; 84236 MW; ECFBB6C39AE564A2 CRC64;
MPGGADLPYC NILNGVGNRK ISNYVKQGGA YLGFCAGAYF ASTRCEFEIG NLNLEVSGPR
ELAFYPDAKR GCAFKGFQYE SHAGSRAVKL SVNTSVLSDV PSNVYNYYNG GGVFINASKY
KDVEVLARYD ERIDVEDIDK AAVVFRKVGK GRVLLTGTHP EFSYNLLKPF EHEHDEHFTG
VIETLKEKDH DRKLFTKACL KKLGLRVSEN IDGSAMPNVT PLIVVSPVEN SIGEIYDNLK
TNLDIKNDFF KDNNDTFVFQ DESNEEYHIE NEHTEEEDPT QATKHVKFMT SGTIPASKTT
PYFNMTKYFD HLKELSSGNI GKYGSVLGYA EVTTSTNTIL EKNPNWLEHL PSGFTLTATT
QIAGRGRGGN VWINPRGVLA TSILFKIPQS AKSSSSVVTM QYLCGLALIE AILGYGSVES
GKGIGYEDMP LRLKWPNDIY ILKPEFFNSL QDKNDISNTV EGWLSKLPEK WIPYFELMRV
EKPVGTWLLL IPSMWGITMA SYSIHAPLTT TLTAIGLFSV GAVIMRGAGC TINDIWDRNL
DNQVARTMER PITSGRVTVP QAVGWLGVQC FAGLGVLLSL PIECFYLGAL SLPFVAAYPL
FKRFTYYPQA MLSICYSWGC LLGFPAVGAP LDLMVAVPLF ISNWIWCMTY DTIYAHQDKK
FDIHAGIKST ALAWGDKSKP ILKGLTIAQA GFYTLAGVMN SMGPGFYIAG AVAIGRLYNQ
LVKVDLDDQK SCWKAFTSNI GTGFVFLFGI AADYVLLLLG IL
//
