ID   DEOC_THEAC              Reviewed;         246 AA.
AC   Q9HKB7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   10-JUN-2026, entry version 126.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114};
DE            EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
GN   Name=deoC {ECO:0000255|HAMAP-Rule:MF_00114}; OrderedLocusNames=Ta0684;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Methanobacteriati; Thermoplasmatota; Thermoplasmata;
OC   Thermoplasmatales; Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC       and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate +
CC         acetaldehyde; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00114};
CC   -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC       degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC       deoxy-alpha-D-ribose 1-phosphate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00114}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL445065; CAC11822.1; -; Genomic_DNA.
DR   RefSeq; WP_010901106.1; NC_002578.1.
DR   AlphaFoldDB; Q9HKB7; -.
DR   SMR; Q9HKB7; -.
DR   STRING; 273075.gene:9571904; -.
DR   PaxDb; 273075-gene:9571904; -.
DR   EnsemblBacteria; CAC11822; CAC11822; CAC11822.
DR   KEGG; tac:Ta0684; -.
DR   eggNOG; arCOG04320; Archaea.
DR   HOGENOM; CLU_053595_0_2_2; -.
DR   InParanoid; Q9HKB7; -.
DR   OrthoDB; 31145at2157; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006018; P:2-deoxyribose 1-phosphate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:TreeGrafter.
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   HAMAP; MF_00114; DeoC_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR028581; DeoC_typeI.
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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..246
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_0000057292"
FT   ACT_SITE        94
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        158
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        200
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   246 AA;  27759 MW;  8383487625408094 CRC64;
     MKYSIEQVMR LVDHSGLKPY LTEKDIARLI EEAKDMGNYA VCIEPIYGKF AKEYLDEKRY
     KVKLDVTIDF PFGSLATSSR KKIIEDSDYA DEVDIVVPMG YVKSHRWDYV DQDLTDVVKI
     AKDHDLVIKI ITEDGYLTQD EKDRLYRSVI RAKPDFIKTS TGFANKDYCA SLGNAAGATP
     DNVSLMSRIA EELGSDIGIK AAGGIHTYRE IESIIDAAKR PIDPEKLRIG MSGTGKVFEE
     MKKIKK
//