DPDS_MYCTO
ID DPDS_MYCTO Reviewed; 296 AA.
AC P9WFF6; L0T9E4; O05837; P60479;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
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=MT2430;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK46724.1; -; Genomic_DNA.
DR PIR; H70585; H70585.
DR RefSeq; WP_003412212.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WFF6; -.
DR SMR; P9WFF6; -.
DR BindingDB; P9WFF6; -.
DR EnsemblBacteria; AAK46724; AAK46724; MT2430.
DR KEGG; mtc:MT2430; -.
DR PATRIC; fig|83331.31.peg.2618; -.
DR HOGENOM; CLU_038505_1_2_11; -.
DR Proteomes; UP000001020; 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_0000428547"
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..80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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..124
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 168
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"
FT BINDING 292..294
FT /ligand="substrate"
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
