DEOC_THEMA
ID DEOC_THEMA Reviewed; 248 AA.
AC Q9X1P5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000303|PubMed:17905878};
DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000269|PubMed:17905878};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000303|PubMed:17905878};
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=TM_1559;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17905878; DOI=10.1128/aem.01101-07;
RA Sakuraba H., Yoneda K., Yoshihara K., Satoh K., Kawakami R., Uto Y.,
RA Tsuge H., Takahashi K., Hori H., Ohshima T.;
RT "Sequential aldol condensation catalyzed by hyperthermophilic 2-deoxy-d-
RT ribose-5-phosphate aldolase.";
RL Appl. Environ. Microbiol. 73:7427-7434(2007).
RN [3] {ECO:0007744|PDB:3R12, ECO:0007744|PDB:3R13}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a deoxyribose-phosphate aldolase (TM_1559) from
RT Thermotoga maritima at 1.75 A resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
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 ECO:0000269|PubMed:17905878}.
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:17905878};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.02 mM for 2-deoxy-D-ribose 5-phosphate
CC {ECO:0000269|PubMed:17905878};
CC pH dependence:
CC Optimum pH is 6.5 for 2-deoxy-D-ribose 5-phosphate cleavage.
CC {ECO:0000269|PubMed:17905878};
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}.
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DR EMBL; AE000512; AAD36625.1; -; Genomic_DNA.
DR PIR; B72240; B72240.
DR RefSeq; NP_229359.1; NC_000853.1.
DR RefSeq; WP_004081965.1; NZ_CP011107.1.
DR PDB; 3R12; X-ray; 1.75 A; A/B=1-248.
DR PDB; 3R13; X-ray; 1.83 A; A/B=1-248.
DR PDBsum; 3R12; -.
DR PDBsum; 3R13; -.
DR AlphaFoldDB; Q9X1P5; -.
DR SMR; Q9X1P5; -.
DR STRING; 243274.THEMA_06485; -.
DR EnsemblBacteria; AAD36625; AAD36625; TM_1559.
DR KEGG; tma:TM1559; -.
DR eggNOG; COG0274; Bacteria.
DR InParanoid; Q9X1P5; -.
DR OMA; MNACIPP; -.
DR OrthoDB; 1227369at2; -.
DR UniPathway; UPA00002; UER00468.
DR EvolutionaryTrace; Q9X1P5; -.
DR Proteomes; UP000008183; 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 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..248
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057280"
FT ACT_SITE 117
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 179
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 208
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT HELIX 1..16
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3R12"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:3R12"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:3R12"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3R12"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:3R12"
SQ SEQUENCE 248 AA; 27285 MW; 7236D2ECA2CA1951 CRC64;
MIEYRIEEAV AKYREFYEFK PVRESAGIED VKSAIEHTNL KPFATPDDIK KLCLEARENR
FHGVCVNPCY VKLAREELEG TDVKVVTVVG FPLGANETRT KAHEAIFAVE SGADEIDMVI
NVGMLKAKEW EYVYEDIRSV VESVKGKVVK VIIETCYLDT EEKIAACVIS KLAGAHFVKT
STGFGTGGAT AEDVHLMKWI VGDEMGVKAS GGIRTFEDAV KMIMYGADRI GTSSGVKIVQ
GGEERYGG
