DPDS_MYCLE
ID DPDS_MYCLE Reviewed; 296 AA.
AC P38119;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Decaprenyl diphosphate synthase;
DE Short=DecaPP;
DE EC=2.5.1.86;
DE EC=2.5.1.87;
DE AltName: Full=Decaprenyl pyrophosphate synthase;
DE AltName: Full=Long-chain isoprenyl diphosphate synthase;
DE AltName: Full=Trans,polycis-decaprenyl diphosphate synthase;
GN Name=uppS; OrderedLocusNames=ML0634; ORFNames=B1937_F2_65;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC diphosphate (IPP) in the cis configuration with (2Z,6E)-farnesyl
CC diphosphate (Z-FPP or EZ-FPP) generating the 50 carbon product
CC trans,polycis-decaprenyl diphosphate. When (2E,6E)-farnesyl diphosphate
CC (E-FPP or EE-FPP) is used in vitro, both primary products decaprenyl
CC diphosphate and (2E,6E,10E)-geranylgeranyl diphosphate (EEE-GGPP) are
CC synthesized. M.tuberculosis does not synthesize (2E,6E,10Z)-
CC geranylgeranyl diphosphate (EEZ-GGPP) and heptaprenyl diphosphate. Can
CC also accept many different allylic substrates, including E-geranyl
CC diphosphate (E-GPP), neryl diphosphate (NPP), and all-trans-geranyl-
CC geranyl diphosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate =
CC (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate + 7
CC diphosphate; Xref=Rhea:RHEA:47096, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:87356, ChEBI:CHEBI:128769, ChEBI:CHEBI:162247;
CC EC=2.5.1.86;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-
CC trans,poly-cis-polyprenyl diphosphate + n diphosphate;
CC Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763;
CC EC=2.5.1.87;
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; U00016; AAA17169.1; -; Genomic_DNA.
DR EMBL; AL583919; CAC30142.1; -; Genomic_DNA.
DR PIR; S72601; S72601.
DR RefSeq; NP_301525.1; NC_002677.1.
DR RefSeq; WP_010907849.1; NC_002677.1.
DR AlphaFoldDB; P38119; -.
DR SMR; P38119; -.
DR STRING; 272631.ML0634; -.
DR EnsemblBacteria; CAC30142; CAC30142; CAC30142.
DR KEGG; mle:ML0634; -.
DR PATRIC; fig|272631.5.peg.1124; -.
DR Leproma; ML0634; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_2_11; -.
DR OMA; PRTEGHK; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cell membrane; Magnesium; Membrane; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..296
FT /note="Decaprenyl diphosphate synthase"
FT /id="PRO_0000123639"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /evidence="ECO:0000250"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 77..80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121..123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250..252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 296 AA; 33891 MW; FF4D28B49E7C6545 CRC64;
MVRNERTLKS TDFPQLPPAP DDYPTFPDKS TWPVVFPMLP PSPDGGPRRP PQHTSKAVAP
RLSAAQLPTH VAIVMDGNGR WANQRGLHRT EGHKMGEAVV IDVACGAIEL GIKWLSLYAF
STENWKRSVE EVRFLMGFNR DVVRRRRENL KEMGVRIRWV GSRPRLWRSV INELAIAEHM
TAGNDVITIN YCVNYGGRTE IAEATREIAR LAAAGRLNPE RITESTITRH LQRPDIPDVD
LFVRTSGEQR SSNFMLWQAA YTEYIFQDKL WPDYDRRDLW AACEEYASRN RRFGSA
