DPRE2_MYCTO
ID DPRE2_MYCTO Reviewed; 254 AA.
AC P9WGS8; L0TGS1; P66783; P72057;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase {ECO:0000250|UniProtKB:P9WGS9};
DE EC=1.1.1.333 {ECO:0000250|UniProtKB:A0R610};
DE AltName: Full=Decaprenyl-phospho-2'-keto-D-arabinose reductase {ECO:0000250|UniProtKB:P9WGS9};
DE AltName: Full=Decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase {ECO:0000250|UniProtKB:P9WGS9};
DE AltName: Full=Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE2 {ECO:0000250|UniProtKB:P9WGS9};
DE Short=Decaprenyl-phosphoribose 2'-epimerase subunit 2 {ECO:0000250|UniProtKB:P9WGS9};
DE AltName: Full=NAD-dependent decaprenylphosphoryl-D-2-keto-erythropentose reductase {ECO:0000250|UniProtKB:P9WGS9};
GN Name=dprE2 {ECO:0000250|UniProtKB:A0R610}; OrderedLocusNames=MT3899;
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: 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). The intermediate DPX is
CC then transferred to DprE2 subunit of the epimerase complex, most
CC probably through a 'substrate channel' at the interface of DprE1-DprE2
CC complex. DprE2 then catalyzes the second step of epimerization, the
CC NAD(+)-dependent reduction of DPX that leads to the formation of DPA.
CC {ECO:0000250|UniProtKB:P9WGS9}.
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:0000250|UniProtKB:A0R610};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000250|UniProtKB:P9WGS9}.
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; AE000516; AAK48264.1; -; Genomic_DNA.
DR PIR; C70697; C70697.
DR RefSeq; WP_003420632.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGS8; -.
DR SMR; P9WGS8; -.
DR EnsemblBacteria; AAK48264; AAK48264; MT3899.
DR KEGG; mtc:MT3899; -.
DR PATRIC; fig|83331.31.peg.4195; -.
DR HOGENOM; CLU_010194_2_1_11; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001020; 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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; NAD; Oxidoreductase; Periplasm.
FT CHAIN 1..254
FT /note="Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose
FT reductase"
FT /id="PRO_0000428309"
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; 27469 MW; 09CE854881C37138 CRC64;
MVLDAVGNPQ TVLLLGGTSE IGLAICERYL HNSAARIVLA CLPDDPRRED AAAAMKQAGA
RSVELIDFDA LDTDSHPKMI EAAFSGGDVD VAIVAFGLLG DAEELWQNQR KAVQIAEINY
TAAVSVGVLL AEKMRAQGFG QIIAMSSAAG ERVRRANFVY GSTKAGLDGF YLGLSEALRE
YGVRVLVIRP GQVRTRMSAH LKEAPLTVDK EYVANLAVTA SAKGKELVWA PAAFRYVMMV
LRHIPRSIFR KLPI
