DEOC_ACIB4
ID DEOC_ACIB4 Reviewed; 222 AA.
AC B5IEU6;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000303|Ref.3};
DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000269|Ref.3};
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};
GN OrderedLocusNames=Aboo_0156 {ECO:0000312|EMBL:ADD07968.1};
GN ORFNames=ABOONEI_332 {ECO:0000312|EMBL:EDY35261.1};
OS Aciduliprofundum boonei (strain DSM 19572 / T469).
OC Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX NCBI_TaxID=439481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19572 / T469;
RX PubMed=18445019; DOI=10.1111/j.1472-4669.2008.00152.x;
RA Reysenbach A.L., Flores G.E.;
RT "Electron microscopy encounters with unusual thermophiles helps direct
RT genomic analysis of Aciduliprofundum boonei.";
RL Geobiology 6:331-336(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19572 / T469;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT "Complete sequence of Aciduliprofundum boonei T469.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RA Yin X., Wang Q., Zhao S.J., Du P.F., Xie K.L., Jin P., Xie T.;
RT "Cloning and characterization of a thermostable 2-deoxy-D-ribose-5-
RT phosphate aldolase from Aciduliprofundum boonei.";
RL Afr. J. Biotechnol. 10:16260-16266(2011).
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, ECO:0000269|Ref.3}.
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, ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Shows high stability to high concentrations of
CC acetaldehyde. {ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for 2-deoxy-D-ribose 5-phosphate {ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 7.0. Extremely stable over a wide range of pH levels.
CC {ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. {ECO:0000269|Ref.3};
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|Ref.3}.
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; DS990524; EDY35261.1; -; Genomic_DNA.
DR EMBL; CP001941; ADD07968.1; -; Genomic_DNA.
DR RefSeq; WP_008085134.1; NZ_DS990524.1.
DR AlphaFoldDB; B5IEU6; -.
DR SMR; B5IEU6; -.
DR STRING; 439481.Aboo_0156; -.
DR EnsemblBacteria; ADD07968; ADD07968; Aboo_0156.
DR EnsemblBacteria; EDY35261; EDY35261; ABOONEI_332.
DR GeneID; 8827093; -.
DR KEGG; abi:Aboo_0156; -.
DR eggNOG; arCOG04320; Archaea.
DR HOGENOM; CLU_053595_0_2_2; -.
DR OMA; MNACIPP; -.
DR OrthoDB; 74992at2157; -.
DR BRENDA; 4.1.2.4; 13712.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000001400; 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 Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..222
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000446450"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 156
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 185
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ SEQUENCE 222 AA; 24062 MW; CE9C7F762DB127D5 CRC64;
MDARELAKYI DHTNLKAFAT REDIKRLCEE AKEYGFYAVC VNPYRVKDAA EFLKGTDIKI
ASVVGFPLGA TFTETKVQEA IMAVRNGADE IDMVMNIGAM KDGDYGFVER DIREVVEAVH
PMGAKVKVII ETCYLSDEEK IKACELAKKA GADFVKTSTG FGTAGAKVED VKLMRSVVGN
DMGVKAAGGI HNAKQAIAMI EAGATRIGAS RSVEIIETLE LI
