DEOC_PYRAE
ID DEOC_PYRAE Reviewed; 226 AA.
AC Q8ZXK7;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 120.
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=PAE1231;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN [2] {ECO:0007744|PDB:1VCV}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
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).
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=0.066 mM for 2-deoxy-D-ribose 5-phosphate
CC {ECO:0000269|PubMed:17905878};
CC pH dependence:
CC Optimum pH is 6.0 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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17905878}.
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; AE009441; AAL63340.1; -; Genomic_DNA.
DR PDB; 1VCV; X-ray; 2.00 A; A/B=1-226.
DR PDBsum; 1VCV; -.
DR AlphaFoldDB; Q8ZXK7; -.
DR SMR; Q8ZXK7; -.
DR STRING; 178306.PAE1231; -.
DR EnsemblBacteria; AAL63340; AAL63340; PAE1231.
DR KEGG; pai:PAE1231; -.
DR PATRIC; fig|178306.9.peg.909; -.
DR eggNOG; arCOG04320; Archaea.
DR HOGENOM; CLU_053595_0_2_2; -.
DR InParanoid; Q8ZXK7; -.
DR OMA; KRGIGNE; -.
DR UniPathway; UPA00002; UER00468.
DR EvolutionaryTrace; Q8ZXK7; -.
DR Proteomes; UP000002439; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..226
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057290"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 146
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:1VCV"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1VCV"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:1VCV"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:1VCV"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1VCV"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1VCV"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:1VCV"
SQ SEQUENCE 226 AA; 24539 MW; 3ECD181C7C3391C4 CRC64;
MIHLVDYALL KPYLTVDEAV AGARKAEELG VAAYCVNPIY APVVRPLLRK VKLCVVADFP
FGALPTASRI ALVSRLAEVA DEIDVVAPIG LVKSRRWAEV RRDLISVVGA AGGRVVKVIT
EEPYLRDEER YTLYDIIAEA GAHFIKSSTG FAEEAYAARQ GNPVHSTPER AAAIARYIKE
KGYRLGVKMA GGIRTREQAK AIVDAIGWGE DPARVRLGTS TPEALL
