DPDP_THEFY
ID DPDP_THEFY Reviewed; 282 AA.
AC Q47RM6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Trans,polycis-polyprenyl diphosphate synthase ((2Z,6E)-farnesyl diphosphate specific);
DE EC=2.5.1.88;
DE AltName: Full=Cis-prenyltransferase;
DE AltName: Full=Dodecaprenyl diphosphate synthase;
GN OrderedLocusNames=Tfu_0853;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
RN [2]
RP FUNCTION AS A DODECAPRENYL DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=19447338; DOI=10.1016/j.jbiosc.2009.02.006;
RA Ambo T., Noike M., Kurokawa H., Koyama T.;
RT "Cloning and functional analysis of cis-prenyltransferase from Thermobifida
RT fusca.";
RL J. Biosci. Bioeng. 107:620-622(2009).
CC -!- FUNCTION: Catalyzes the synthesis of Z,E-mixed prenyl diphosphates by a
CC condensation of isopentenyl diphosphate to an allylic diphosphate. It
CC shows a large substrate specificity accepting dimethylallyl diphosphate
CC (DMAPP), GPP, E,Efarnesyl diphosphate (FPP), E,E,E-geranylgeranyl
CC diphosphate (GGPP), neryl diphosphate (Z-GPP), and (2Z,6E)-farnesyl
CC diphosphate (Z,E-FPP) as allylic substrates. The enzyme exhibits the
CC highest activity when Z,E-FPP is employed as an allylic substrate. The
CC major product is dodecaprenyl diphosphate (C60) under every allylic
CC substrate conditions, but the enzyme is also able to synthesize even
CC C70 prenyl diphosphate as the maximum chain-length product.
CC {ECO:0000269|PubMed:19447338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6E)-farnesyl diphosphate + 10 isopentenyl diphosphate =
CC di-trans,deca-cis-tridecaprenyl diphosphate + 10 diphosphate;
CC Xref=Rhea:RHEA:27614, ChEBI:CHEBI:33019, ChEBI:CHEBI:60385,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.88;
CC Evidence={ECO:0000269|PubMed:19447338};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6E)-farnesyl diphosphate + 11 isopentenyl diphosphate =
CC di-trans,undeca-cis-tetradecaprenyl diphosphate + 11 diphosphate;
CC Xref=Rhea:RHEA:27618, ChEBI:CHEBI:33019, ChEBI:CHEBI:60387,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.88;
CC Evidence={ECO:0000269|PubMed:19447338};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6E)-farnesyl diphosphate + 9 isopentenyl diphosphate = di-
CC trans,nona-cis-dodecaprenyl diphosphate + 9 diphosphate;
CC Xref=Rhea:RHEA:27602, ChEBI:CHEBI:33019, ChEBI:CHEBI:60386,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.88;
CC Evidence={ECO:0000269|PubMed:19447338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; CP000088; AAZ54891.1; -; Genomic_DNA.
DR RefSeq; WP_011291300.1; NC_007333.1.
DR PDB; 7CPM; X-ray; 2.60 A; A/B/C/D/E/F=1-282.
DR PDB; 7CPN; X-ray; 2.28 A; A/B/C/D/E/F=1-282.
DR PDBsum; 7CPM; -.
DR PDBsum; 7CPN; -.
DR AlphaFoldDB; Q47RM6; -.
DR SMR; Q47RM6; -.
DR STRING; 269800.Tfu_0853; -.
DR EnsemblBacteria; AAZ54891; AAZ54891; Tfu_0853.
DR KEGG; tfu:Tfu_0853; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_2_11; -.
DR OMA; PRTEGHK; -.
DR OrthoDB; 1630604at2; -.
DR BioCyc; MetaCyc:MON-15682; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..282
FT /note="Trans,polycis-polyprenyl diphosphate synthase
FT ((2Z,6E)-farnesyl diphosphate specific)"
FT /id="PRO_0000419134"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 45..48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218..220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:7CPN"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:7CPN"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 57..78
FT /evidence="ECO:0007829|PDB:7CPN"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 97..121
FT /evidence="ECO:0007829|PDB:7CPN"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:7CPN"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:7CPN"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:7CPN"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:7CPN"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:7CPN"
SQ SEQUENCE 282 AA; 31967 MW; A1085BD7CB076E90 CRC64;
MSPKTVFSTD THREPIPPQP HPSGARPPQL PRELIPRHVA IVMDGNGRWA KQRGLPRTEG
HKAGESSLFD VIEGALELGV PYLSAYAFST ENWKRSPDEV RFLMGFNRDV IRRRRDELHA
RGVRVRWAGR PGRLWKSVIK ELTEAEELTK HNTKLTLQFC VNYGGRAEIA DAAAALARDV
AAGRLSPNRV TEATLARYLY HPDIPDVDLF IRSSGEQRLS NFLLWQSSYA EFVFLDTLWP
DFDRRHFWQA CEIYARRDRR YGGAEPNPVG PPQSAAGAQG QD
