DPPRS_MYCTU
ID DPPRS_MYCTU Reviewed; 302 AA.
AC P9WFR5; F2GDG5; L0TGT7; O53583; Q7D4U6;
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-phosphate phosphoribosyltransferase;
DE EC=2.4.2.45;
DE AltName: Full=5-phospho-alpha-D-ribose-1-diphosphate:decaprenyl-phosphate 5-phosphoribosyltransferase;
DE AltName: Full=DPPR synthase;
GN OrderedLocusNames=Rv3806c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RX PubMed=15878857; DOI=10.1074/jbc.m504068200;
RA Huang H., Scherman M.S., D'Haeze W., Vereecke D., Holsters M., Crick D.C.,
RA McNeil M.R.;
RT "Identification and active expression of the Mycobacterium tuberculosis
RT gene encoding 5-phospho-{alpha}-d-ribose-1-diphosphate: decaprenyl-
RT phosphate 5-phosphoribosyltransferase, the first enzyme committed to
RT decaprenylphosphoryl-d-arabinose synthesis.";
RL J. Biol. Chem. 280:24539-24543(2005).
RN [3]
RP FUNCTION, MUTAGENESIS OF ARG-22; ASN-29; PHE-59; PHE-62; ALA-66; TYR-70;
RP ASN-73; ASP-77; ASP-81; HIS-84; ARG-192; GLU-195 AND ARG-201,
RP BIOPHYSICOCHEMICAL PROPERTIES, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=18310020; DOI=10.1099/mic.0.2007/013532-0;
RA Huang H., Berg S., Spencer J.S., Vereecke D., D'Haeze W., Holsters M.,
RA McNeil M.R.;
RT "Identification of amino acids and domains required for catalytic activity
RT of DPPR synthase, a cell wall biosynthetic enzyme of Mycobacterium
RT tuberculosis.";
RL Microbiology 154:736-743(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Involved in the biosynthesis of decaprenylphosphoryl
CC arabinose (DPA) a precursor for arabinan synthesis in mycobacterial
CC cell wall biosynthesis. Catalyzes the transfer of a 5-phosphoribosyl
CC residue from phosphoribose diphosphate (pRpp) to decaprenyl phosphate
CC (DP) to form decaprenylphosphoryl-5-phosphoribose (DPPR). The enzyme
CC favors polyprenyl phosphate with 50-60 carbon atoms uses C-75
CC polyprenyl phosphate less efficiently than C-50 or C-60.
CC {ECO:0000269|PubMed:15878857, ECO:0000269|PubMed:18310020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + H(+) + trans,octa-
CC cis-decaprenyl phosphate = diphosphate + trans,octa-cis-
CC decaprenylphospho-beta-D-ribofuranose 5-phosphate;
CC Xref=Rhea:RHEA:34067, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:65079, ChEBI:CHEBI:66937; EC=2.4.2.45;
CC Evidence={ECO:0000269|PubMed:15878857};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15878857};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15878857};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15878857};
CC Note=Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
CC {ECO:0000269|PubMed:15878857};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.4 uM for DP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15878857, ECO:0000269|PubMed:18310020};
CC KM=120 uM for pRpp (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15878857, ECO:0000269|PubMed:18310020};
CC pH dependence:
CC Optimum pH is between 7.5 and 8. {ECO:0000269|PubMed:15878857,
CC ECO:0000269|PubMed:18310020};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:18310020}; Multi-
CC pass membrane protein {ECO:0000305|PubMed:18310020}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46635.1; -; Genomic_DNA.
DR PIR; B70888; B70888.
DR RefSeq; NP_218323.1; NC_000962.3.
DR RefSeq; WP_003899704.1; NZ_NVQJ01000022.1.
DR AlphaFoldDB; P9WFR5; -.
DR STRING; 83332.Rv3806c; -.
DR PaxDb; P9WFR5; -.
DR DNASU; 886129; -.
DR GeneID; 886129; -.
DR KEGG; mtu:Rv3806c; -.
DR TubercuList; Rv3806c; -.
DR eggNOG; COG0382; Bacteria.
DR OMA; RWFLITT; -.
DR PhylomeDB; P9WFR5; -.
DR BioCyc; MetaCyc:G185E-8102-MON; -.
DR BRENDA; 2.4.2.45; 3445.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0052636; F:arabinosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="Decaprenyl-phosphate phosphoribosyltransferase"
FT /id="PRO_0000420587"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18310020"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..54
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:18310020"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18310020"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:18310020"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18310020"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..169
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:18310020"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18310020"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 265..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 22
FT /note="R->L: The DPPR synthase activity is strongly
FT diminished."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 29
FT /note="N->A: The DPPR synthase activity is strongly
FT diminished."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 59
FT /note="F->A: Only small effects on the DPPR synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 62
FT /note="F->A: Only small effects on the DPPR synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 66
FT /note="A->F: No DPPR synthase activity and the protein is
FT not expressed in the membrane."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 70
FT /note="Y->A: No DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 73
FT /note="N->A: No DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 73
FT /note="N->Q: Slight DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 77
FT /note="D->A: No DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 77
FT /note="D->E: Slight DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 81
FT /note="D->A: No DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 84
FT /note="H->L: Slight DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 192
FT /note="R->A: No DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 195
FT /note="E->A: Substantially reduced the DPPR synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:18310020"
FT MUTAGEN 201
FT /note="R->A: No DPPR synthase activity."
FT /evidence="ECO:0000269|PubMed:18310020"
SQ SEQUENCE 302 AA; 32654 MW; B232C90EE4D32717 CRC64;
MSEDVVTQPP ANLVAGVVKA IRPRQWVKNV LVLAAPLAAL GGGVRYDYVE VLSKVSMAFV
VFSLAASAVY LVNDVRDVEA DREHPTKRFR PIAAGVVPEW LAYTVAVVLG VTSLAGAWML
TPNLALVMVV YLAMQLAYCF GLKHQAVVEI CVVSSAYLIR AIAGGVATKI PLSKWFLLIM
AFGSLFMVAG KRYAELHLAE RTGAAIRKSL ESYTSTYLRF VWTLSATAVV LCYGLWAFER
DGYSGSWFAV SMIPFTIAIL RYAVDVDGGL AGEPEDIALR DRVLQLLALA WIATVGAAVA
FG
