DPDS_MYCS2
ID DPDS_MYCS2 Reviewed; 293 AA.
AC A0R0S4; I7FQ48;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=MSMEG_4490, MSMEI_4379;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION AS FARNESYL DIPHOSPHATE SYNTHASE, AND SUBCELLULAR LOCATION.
RX PubMed=11004176; DOI=10.1128/jb.182.20.5771-5778.2000;
RA Crick D.C., Schulbach M.C., Zink E.E., Macchia M., Barontini S.,
RA Besra G.S., Brennan P.J.;
RT "Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and
RT Mycobacterium smegmatis.";
RL J. Bacteriol. 182:5771-5778(2000).
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 heptaprenyl diphosphate are synthesized. It is probably
CC due to the fact that M.smegmatis synthesizes both (2E,6E,10E)-
CC geranylgeranyl diphosphate (EEE-GGPP) and (2E,6E,10Z)-geranylgeranyl
CC diphosphate (EEZ-GGPP). Can also accept many different allylic
CC substrates, including E-geranyl diphosphate (E-GPP), neryl diphosphate
CC (NPP), and all-trans-geranyl-geranyl diphosphate.
CC {ECO:0000269|PubMed:11004176}.
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:0000269|PubMed:11004176}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; CP000480; ABK71014.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40833.1; -; Genomic_DNA.
DR RefSeq; WP_011729873.1; NZ_SIJM01000026.1.
DR RefSeq; YP_888762.1; NC_008596.1.
DR AlphaFoldDB; A0R0S4; -.
DR SMR; A0R0S4; -.
DR STRING; 246196.MSMEI_4379; -.
DR EnsemblBacteria; ABK71014; ABK71014; MSMEG_4490.
DR EnsemblBacteria; AFP40833; AFP40833; MSMEI_4379.
DR GeneID; 66735822; -.
DR KEGG; msg:MSMEI_4379; -.
DR KEGG; msm:MSMEG_4490; -.
DR PATRIC; fig|246196.19.peg.4396; -.
DR eggNOG; COG0020; Bacteria.
DR OMA; PRTEGHK; -.
DR OrthoDB; 1630604at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033850; F:Z-farnesyl diphosphate synthase 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 Cell membrane; Magnesium; Membrane; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..293
FT /note="Decaprenyl diphosphate synthase"
FT /id="PRO_0000417570"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 74..77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118..120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247..249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 33484 MW; 354BB28117AAD288 CRC64;
MATTRGKKTY PQLPPAPDDY PTFPDKSTWP VVFPEIPAGT NGRFARPPQH TSKAAAPKIP
ADQVPNHVAV VMDGNGRWAT QRGLGRTEGH KMGEAVLIDI TCGAIEIGIK HLTVYAFSTE
NWKRSTEEVR FLMGFNREVV RRRRENLNDM GVRMRWVGSR PRMWRSVIKE FDIAEQMTVD
NDVITINYCV NYGGRTEIVE AARALAQEAV DGKINPARIS EAMFAKHLHR ADIPDVDLFI
RTSGEQRASN FLLWQAAYAE YVFQDKLWPD YDRRDLWAAC EEYVNRNRRF GRA
