DPDS_MYCBO
ID DPDS_MYCBO Reviewed; 296 AA.
AC P60478; A0A1R3Y360; O05837; X2BKF4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=BQ2027_MB2382C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00994.1; -; Genomic_DNA.
DR RefSeq; NP_856031.1; NC_002945.3.
DR RefSeq; WP_003412212.1; NC_002945.4.
DR AlphaFoldDB; P60478; -.
DR SMR; P60478; -.
DR EnsemblBacteria; SIU00994; SIU00994; BQ2027_MB2382C.
DR PATRIC; fig|233413.5.peg.2617; -.
DR OMA; PRTEGHK; -.
DR Proteomes; UP000001419; 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; Transferase.
FT CHAIN 1..296
FT /note="Decaprenyl diphosphate synthase"
FT /id="PRO_0000123638"
FT REGION 1..24
FT /note="Disordered"
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; 33791 MW; 93895E54253615AA CRC64;
MARDARKRTS SNFPQLPPAP DDYPTFPDTS TWPVVFPELP AAPYGGPCRP PQHTSKAAAP
RIPADRLPNH VAIVMDGNGR WATQRGLART EGHKMGEAVV IDIACGAIEL GIKWLSLYAF
STENWKRSPE EVRFLMGFNR DVVRRRRDTL KKLGVRIRWV GSRPRLWRSV INELAVAEEM
TKSNDVITIN YCVNYGGRTE ITEATREIAR EVAAGRLNPE RITESTIARH LQRPDIPDVD
LFLRTSGEQR SSNFMLWQAA YAEYIFQDKL WPDYDRRDLW AACEEYASRT RRFGSA
