DPRE2_MYCS2
ID DPRE2_MYCS2 Reviewed; 254 AA.
AC A0R610;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase {ECO:0000305};
DE EC=1.1.1.333 {ECO:0000269|PubMed:22188377};
DE AltName: Full=Decaprenyl-phospho-2'-keto-D-arabinose reductase {ECO:0000305};
DE AltName: Full=Decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase {ECO:0000305};
DE AltName: Full=Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE2 {ECO:0000305};
DE Short=Decaprenyl-phosphoribose 2'-epimerase subunit 2 {ECO:0000305};
DE AltName: Full=NAD-dependent decaprenylphosphoryl-D-2'-keto erythropentose reductase {ECO:0000303|PubMed:22188377};
GN Name=dprE2 {ECO:0000303|PubMed:22188377};
GN OrderedLocusNames=MSMEG_6385, MSMEI_6217; ORFNames=LJ00_31560;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=25657281; DOI=10.1128/genomea.01520-14;
RA Mohan A., Padiadpu J., Baloni P., Chandra N.;
RT "Complete genome sequences of a Mycobacterium smegmatis laboratory strain
RT (MC2 155) and isoniazid-resistant (4XR1/R2) mutant strains.";
RL Genome Announc. 3:E01520-E01520(2015).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=22188377; DOI=10.1021/ja211042r;
RA Trefzer C., Skovierova H., Buroni S., Bobovska A., Nenci S., Molteni E.,
RA Pojer F., Pasca M.R., Makarov V., Cole S.T., Riccardi G., Mikusova K.,
RA Johnsson K.;
RT "Benzothiazinones are suicide inhibitors of mycobacterial
RT decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase DprE1.";
RL J. Am. Chem. Soc. 134:912-915(2012).
CC -!- FUNCTION: Component of the DprE1-DprE2 complex that catalyzes the 2-
CC step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-
CC phospho-arabinose (DPA), a key precursor that serves as the arabinose
CC donor required for the synthesis of cell-wall arabinans. DprE1
CC catalyzes the first step of epimerization, namely FAD-dependent
CC oxidation of the C2' hydroxyl of DPR to yield the keto intermediate
CC decaprenyl-phospho-2'-keto-D-arabinose (DPX) (PubMed:22188377). The
CC intermediate DPX is then transferred to DprE2 subunit of the epimerase
CC complex, most probably through a 'substrate channel' at the interface
CC of DprE1-DprE2 complex (By similarity). DprE2 then catalyzes the second
CC step of epimerization, the NAD(+)-dependent reduction of DPX that leads
CC to the formation of DPA (PubMed:22188377).
CC {ECO:0000250|UniProtKB:P9WGS9, ECO:0000269|PubMed:22188377}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + trans,octa-cis-decaprenylphospho-beta-D-
CC arabinofuranose = H(+) + NADH + trans,octa-cis-decaprenylphospho-
CC beta-D-erythro-pentofuranosid-2-ulose; Xref=Rhea:RHEA:33895,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65066, ChEBI:CHEBI:65067; EC=1.1.1.333;
CC Evidence={ECO:0000269|PubMed:22188377};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:22188377}.
CC -!- SUBUNIT: Interacts with DprE1 to form an epimerase complex.
CC {ECO:0000250|UniProtKB:P9WGS9}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P9WGS9}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CP000480; ABK72059.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42643.1; -; Genomic_DNA.
DR EMBL; CP009494; AIU11366.1; -; Genomic_DNA.
DR RefSeq; WP_011731251.1; NZ_SIJM01000013.1.
DR RefSeq; YP_890598.1; NC_008596.1.
DR AlphaFoldDB; A0R610; -.
DR SMR; A0R610; -.
DR STRING; 246196.MSMEI_6217; -.
DR PRIDE; A0R610; -.
DR EnsemblBacteria; ABK72059; ABK72059; MSMEG_6385.
DR EnsemblBacteria; AFP42643; AFP42643; MSMEI_6217.
DR GeneID; 66737663; -.
DR KEGG; msb:LJ00_31560; -.
DR KEGG; msg:MSMEI_6217; -.
DR KEGG; msm:MSMEG_6385; -.
DR PATRIC; fig|246196.19.peg.6212; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_2_1_11; -.
DR OMA; INAVGNP; -.
DR OrthoDB; 1186478at2; -.
DR BioCyc; MetaCyc:MON-17533; -.
DR BRENDA; 1.1.1.333; 3512.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; NAD; Oxidoreductase; Periplasm;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose
FT reductase"
FT /id="PRO_0000432472"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00334"
SQ SEQUENCE 254 AA; 27137 MW; 4B047565BF22E7E2 CRC64;
MVFDAVGNPQ TILLLGGTSE IGLAICERYL RNASARIVLA VMPGDPGRDA AVEQMRKAGA
SAVDVVDFDA LDTESHPAVI DQAFAGGDVD VAIVAFGLLG DAEELWQNQR KAVQIAGVNY
TAAVSVGVLL GEKMRAQGSG QIIAMSSAAG ERVRRSNFVY GSTKAGLDGF YLGLGEALRE
FGVRVLVIRP GQVRTRMSAH VKEAPLTVDK EYVAELAVTA SAKGKELVWA PGAFRYVMMV
LRHIPRPIFR KLPI
