DEOC_THEKO
ID DEOC_THEKO Reviewed; 224 AA.
AC Q877I0;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000303|PubMed:15205420};
DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000269|PubMed:15205420};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000303|PubMed:15205420};
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=TK2104;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15205420; DOI=10.1128/jb.186.13.4185-4191.2004;
RA Rashid N., Imanaka H., Fukui T., Atomi H., Imanaka T.;
RT "Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate
RT aldolase reveals a metabolic link between pentoses and central carbon
RT metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis.";
RL J. Bacteriol. 186:4185-4191(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC phosphate. Could be involved in pentose biosynthesis.
CC {ECO:0000269|PubMed:15205420}.
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 ECO:0000269|PubMed:15205420};
CC -!- ACTIVITY REGULATION: Activated by citrate. Inhibited by NaBH(4).
CC Activity is independent of divalent metal cations.
CC {ECO:0000269|PubMed:15205420}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.81 mM for 2-deoxy-D-ribose 5-phosphate (at 95 degrees Celsius)
CC {ECO:0000269|PubMed:15205420};
CC Vmax=285 umol/min/mg enzyme (at 95 degrees Celsius)
CC {ECO:0000269|PubMed:15205420};
CC Note=kcat is 116 sec(-1) (at 95 degrees Celsius).
CC {ECO:0000269|PubMed:15205420};
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:15205420};
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius.
CC {ECO:0000269|PubMed:15205420};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15205420}.
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; AB092961; BAC67708.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD86293.1; -; Genomic_DNA.
DR RefSeq; WP_011251054.1; NC_006624.1.
DR AlphaFoldDB; Q877I0; -.
DR SMR; Q877I0; -.
DR STRING; 69014.TK2104; -.
DR EnsemblBacteria; BAD86293; BAD86293; TK2104.
DR GeneID; 3233914; -.
DR KEGG; tko:TK2104; -.
DR PATRIC; fig|69014.16.peg.2059; -.
DR eggNOG; arCOG04320; Archaea.
DR HOGENOM; CLU_053595_0_2_2; -.
DR InParanoid; Q877I0; -.
DR OMA; MNACIPP; -.
DR OrthoDB; 74992at2157; -.
DR PhylomeDB; Q877I0; -.
DR BRENDA; 4.1.2.4; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IBA:GO_Central.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IBA:GO_Central.
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 Cytoplasm; Direct protein sequencing; Lyase; Reference proteome;
KW Schiff base.
FT CHAIN 1..224
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057291"
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 187
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ SEQUENCE 224 AA; 24506 MW; B3EFEC0569702F4A CRC64;
MNKREIARYI DQTNLKPYAT KEDIIKLCDE AIEYGFYAVC VNPYRVKLAK DYLREKNADV
KVASVIGFPL GATPTEVKVF EAKRALEDGA DELDMVINIG ALKDKDYEYV KNDIAEVVKV
AHERGAKVKV IIETCYLTEE EKVKACELAK EAGADFVKTS TGFGTGGATV EDVRLMRKVV
GPEMGVKAAG GIRTYEQALE MIEAGANRIG TSSGVKIVEG APDE
