ID   A2BLE9_HYPBU            Unreviewed;       237 AA.
AC   A2BLE9;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
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};
GN   OrderedLocusNames=Hbut_0962 {ECO:0000313|EMBL:ABM80810.1};
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM80810.1, ECO:0000313|Proteomes:UP000002593};
RN   [1] {ECO:0000313|EMBL:ABM80810.1, ECO:0000313|Proteomes:UP000002593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC   {ECO:0000313|Proteomes:UP000002593};
RX   PubMed=17350933;
RA   Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM80810.1; -; Genomic_DNA.
DR   RefSeq; WP_011822128.1; NC_008818.1.
DR   AlphaFoldDB; A2BLE9; -.
DR   STRING; 415426.Hbut_0962; -.
DR   EnsemblBacteria; ABM80810; ABM80810; Hbut_0962.
DR   GeneID; 4781378; -.
DR   KEGG; hbu:Hbut_0962; -.
DR   eggNOG; arCOG04320; Archaea.
DR   HOGENOM; CLU_053595_0_2_2; -.
DR   OrthoDB; 31145at2157; -.
DR   BRENDA; 4.1.2.4; 10772.
DR   Proteomes; UP000002593; Chromosome.
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   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:ABM80810.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002593}.
SQ   SEQUENCE   237 AA;  26309 MW;  28CABFD920BEA012 CRC64;
     MSESFFCRFG VSEIASRIDH AVLKPWSSVS ELEKAIRELE ELNLRCLIIS PTHLRLAREK
     TNKCLGVVVG FPFGYSTIEA KIKELEDSIA LGAQEIDYVA NTQLLLAGRT EEYLNEIRAA
     ITICRDSGVK CKVIIEAPAL PRNLLVEIVE KIAMMDPHPD YIKTSTGYGP RPTYVEDVYL
     IDQTLRRIGK RDEIGIKAAG GIREGLQAAA MLLAGADVIG TSTPRQVIET YKELCRI
//