DEOC_THET8
ID DEOC_THET8 Reviewed; 220 AA.
AC Q5SJ28; Q7SIC8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=TTHA1186;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH AND WITHOUT
RP 2-DEOXYRIBOSE-5-PHOSPHATE, SUBUNIT, AND ACTIVE SITE.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15388928; DOI=10.1107/s0907444904020190;
RA Lokanath N.K., Shiromizu I., Ohshima N., Nodake Y., Sugahara M.,
RA Yokoyama S., Kuramitsu S., Miyano M., Kunishima N.;
RT "Structure of aldolase from Thermus thermophilus HB8 showing the
RT contribution of oligomeric state to thermostability.";
RL Acta Crystallogr. D 60:1816-1823(2004).
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 = 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: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 -!- SUBUNIT: Homotetramer, in solution and in the crystal structure.
CC {ECO:0000269|PubMed:15388928}.
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}.
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DR EMBL; AP008226; BAD71009.1; -; Genomic_DNA.
DR RefSeq; WP_011228499.1; NC_006461.1.
DR RefSeq; YP_144452.1; NC_006461.1.
DR PDB; 1J2W; X-ray; 1.50 A; A/B/C/D=1-220.
DR PDB; 1UB3; X-ray; 1.40 A; A/B/C/D=1-220.
DR PDBsum; 1J2W; -.
DR PDBsum; 1UB3; -.
DR AlphaFoldDB; Q5SJ28; -.
DR SMR; Q5SJ28; -.
DR STRING; 300852.55772568; -.
DR DrugBank; DB04087; Open Form of 2'-Deoxy-Ribofuranose-5'-Phosphate.
DR EnsemblBacteria; BAD71009; BAD71009; BAD71009.
DR GeneID; 3169004; -.
DR KEGG; ttj:TTHA1186; -.
DR PATRIC; fig|300852.9.peg.1167; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_0_1_0; -.
DR OMA; MNACIPP; -.
DR PhylomeDB; Q5SJ28; -.
DR UniPathway; UPA00002; UER00468.
DR EvolutionaryTrace; Q5SJ28; -.
DR Proteomes; UP000000532; 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:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00959; DeoC; 1.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR10889; PTHR10889; 1.
DR PANTHER; PTHR10889:SF1; PTHR10889:SF1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR TIGRFAMs; TIGR00126; deoC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..220
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000231572"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114,
FT ECO:0000305|PubMed:15388928"
FT ACT_SITE 151
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114,
FT ECO:0000305|PubMed:15388928"
FT ACT_SITE 180
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114,
FT ECO:0000305|PubMed:15388928"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1UB3"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1UB3"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1UB3"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:1UB3"
SQ SEQUENCE 220 AA; 23307 MW; F8E933B08155AF53 CRC64;
MDLAAHIDHT LLKPTATLEE VAKAAEEALE YGFYGLCIPP SYVAWVRARY PHAPFRLVTV
VGFPLGYQEK EVKALEAALA CARGADEVDM VLHLGRAKAG DLDYLEAEVR AVREAVPQAV
LKVILETGYF SPEEIARLAE AAIRGGADFL KTSTGFGPRG ASLEDVALLV RVAQGRAQVK
AAGGIRDRET ALRMLKAGAS RLGTSSGVAL VAGEGGTLGY
