DPPRS_CORGL
ID DPPRS_CORGL Reviewed; 332 AA.
AC Q8NLQ9; Q6M1Y0;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=cg3189, Cgl2880;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION, 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).
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).
CC {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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
CC {ECO:0000250};
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; BA000036; BAC00274.1; -; Genomic_DNA.
DR EMBL; BX927156; CAF20904.1; -; Genomic_DNA.
DR RefSeq; NP_602071.1; NC_003450.3.
DR RefSeq; WP_011015459.1; NC_006958.1.
DR AlphaFoldDB; Q8NLQ9; -.
DR STRING; 196627.cg3189; -.
DR KEGG; cgb:cg3189; -.
DR KEGG; cgl:Cgl2880; -.
DR PATRIC; fig|196627.13.peg.2812; -.
DR eggNOG; COG0382; Bacteria.
DR HOGENOM; CLU_029423_0_0_11; -.
DR OMA; RWFLITT; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..332
FT /note="Decaprenyl-phosphate phosphoribosyltransferase"
FT /id="PRO_0000420586"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 36054 MW; F2DD59586A05DEB8 CRC64;
MSEHAAEHHR DTQNFLTSEP HTTAIEDNKK RQPPKNLADG MIKALRPKQW VKNVLVLAAP
LAAGADAIFN QRTIIDVAIA FVVFCFGASA IYLVNDARDV EADREHPTKR FRPIAAGVLP
VGMAYGMAVA LIALSIGLSF LATDGVALAC VIGVYIALQL GYCFGWKHMP VIDIALVSSG
FMLRAMAGGV AAGIELSQWF LLVAAFGSLF MASGKRYAEI LLHERTGAKI RKSLESYTPT
YLRFVWTMAA TAVVMSYALW GFDLSQHSTD AGPWYQISMV PFTIAILRYA AGVDTGDGGA
PDEVALSDKV LQVLALAWVF CIVMAVYIMP MF
