ID   E5FNY3_TREPL            Unreviewed;       185 AA.
AC   E5FNY3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=deoxyribose-phosphate aldolase {ECO:0000256|ARBA:ARBA00012515};
DE            EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
DE   Flags: Fragment;
GN   Name=deoC {ECO:0000313|EMBL:ADR64384.1};
OS   Treponema pallidum subsp. pallidum str. Mexico A.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=686990 {ECO:0000313|EMBL:ADR64384.1};
RN   [1] {ECO:0000313|EMBL:ADR64384.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mexico A {ECO:0000313|EMBL:ADR64384.1};
RX   PubMed=21209953; DOI=10.1371/journal.pone.0015713;
RA   Mikalova L., Strouhal M., Cejkova D., Zobanikova M., Pospisilova P.,
RA   Norris S.J., Sodergren E., Weinstock G.M., Smajs D.;
RT   "Genome analysis of Treponema pallidum subsp. pallidum and subsp. pertenue
RT   strains: most of the genetic differences are localized in six regions.";
RL   PLoS ONE 5:E15713-E15713(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000764};
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DR   EMBL; HM585252; ADR64384.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5FNY3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   CDD; cd00959; DeoC; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889:SF1; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lyase {ECO:0000313|EMBL:ADR64384.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADR64384.1"
SQ   SEQUENCE   185 AA;  19583 MW;  9AF78320A0321D7D CRC64;
     ASVCVNPCHV ALAAGAVRGT AVRVCSVIGF PFGTHVTEVK CAEAQRALDD GAQELDMVVR
     IDKVCAGERE VVEREIAQVA ARCHARGAIV KVIVETALLD EMHIAFACSC VEAGHADFIK
     TSTGYASRGG TEGDIQCFKK YLKGETKIKA SGGIRTRAQA QRFIELGCAR IGTSNGVAIM
     EERAS
//