DEOC_RHOE4
ID DEOC_RHOE4 Reviewed; 221 AA.
AC C0ZUQ6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000303|PubMed:22222309};
DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000269|PubMed:22222309};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000303|PubMed:22222309};
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, ECO:0000303|PubMed:22222309};
GN OrderedLocusNames=RER_15930 {ECO:0000312|EMBL:BAH32301.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 311;
RX PubMed=22222309; DOI=10.1016/j.jbiotec.2011.12.018;
RA Kullartz I., Pietruszka J.;
RT "Cloning and characterisation of a new 2-deoxy-D-ribose-5-phosphate
RT aldolase from Rhodococcus erythropolis.";
RL J. Biotechnol. 161:174-180(2012).
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:22222309}.
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:22222309};
CC -!- ACTIVITY REGULATION: Inhibited by tetrahydrofurane, acetonitrile and
CC isopropanol. {ECO:0000269|PubMed:22222309}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.84 mM for 2-deoxy-D-ribose 5-phosphate
CC {ECO:0000269|PubMed:22222309};
CC KM=418 mM for 2-deoxy-D-ribose {ECO:0000269|PubMed:22222309};
CC Note=kcat is 18 sec(-1) with 2-deoxy-D-ribose 5-phosphate as
CC substrate. kcat is 1.23 sec(-1) with 2-deoxy-D-ribose as substrate.
CC {ECO:0000269|PubMed:22222309};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:22222309};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. However, half-life of the
CC protein at those temperatures is low (approximately 2 minutes).
CC {ECO:0000269|PubMed:22222309};
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:22222309}.
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; AP008957; BAH32301.1; -; Genomic_DNA.
DR RefSeq; WP_020906748.1; NC_012490.1.
DR AlphaFoldDB; C0ZUQ6; -.
DR SMR; C0ZUQ6; -.
DR STRING; 234621.RER_15930; -.
DR EnsemblBacteria; BAH32301; BAH32301; RER_15930.
DR KEGG; rer:RER_15930; -.
DR PATRIC; fig|234621.6.peg.2078; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_0_0_11; -.
DR OMA; KRGIGNE; -.
DR BRENDA; 4.1.2.4; 5389.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000002204; 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; Schiff base.
FT CHAIN 1..221
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000442143"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 155
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 221 AA; 22190 MW; FD23142BD311DAB8 CRC64;
MSEAALTRSQ VAAMVDHTLL KPEATAADVT ALIDEARSLG VLAVCVSPSM LPIRADGLVT
AAVVGFPSGK HHSLVKGAEA RLAVDQGATE IDMVIDVGAA VAGDYSAVLA DILTVREAMG
ESAILKVILE TAALSDEAIV ECCRAAVRAG ANFVKTSTGF HPAGGATVEA VELMARTVGP
GVGVKASGGI RTTQAALDMI AAGATRLGLS GTRAVLDGLT D
