(data stored in ACNUC7421 zone)

SWISSPROT: DEOC_EDWI9

ID   DEOC_EDWI9              Reviewed;         259 AA.
AC   C5BHJ2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=DERA {ECO:0000255|HAMAP-Rule:MF_00592};
DE            EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00592};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
GN   Name=deoC {ECO:0000255|HAMAP-Rule:MF_00592};
GN   OrderedLocusNames=NT01EI_0562;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between
CC       acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-
CC       D-ribose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00592}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-
CC         glyceraldehyde 3-phosphate; Xref=Rhea:RHEA:12821,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:59776, ChEBI:CHEBI:62877;
CC         EC=4.1.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00592};
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_00592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00592}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00592}.
DR   EMBL; CP001600; ACR67791.1; -; Genomic_DNA.
DR   RefSeq; WP_015869991.1; NC_012779.2.
DR   SMR; C5BHJ2; -.
DR   PRIDE; C5BHJ2; -.
DR   EnsemblBacteria; ACR67791; ACR67791; NT01EI_0562.
DR   GeneID; 7960330; -.
DR   KEGG; eic:NT01EI_0562; -.
DR   PATRIC; fig|634503.3.peg.507; -.
DR   eggNOG; ENOG4105FCI; Bacteria.
DR   eggNOG; COG0274; LUCA.
DR   HOGENOM; HOG000241644; -.
DR   KO; K01619; -.
DR   OMA; MNACIPP; -.
DR   OrthoDB; 1227369at2; -.
DR   BioCyc; EICT634503:G1GVC-523-MONOMER; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000001485; 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_00592; DeoC_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/lacD_aldolase.
DR   InterPro; IPR023649; DeoC_typeII.
DR   PANTHER; PTHR10889; PTHR10889; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   TIGRFAMs; TIGR00126; deoC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHJ2.
DR   SWISS-2DPAGE; C5BHJ2.
KW   Complete proteome; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN         1    259       Deoxyribose-phosphate aldolase.
FT                                /FTId=PRO_1000212174.
FT   ACT_SITE    102    102       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00592}.
FT   ACT_SITE    167    167       Schiff-base intermediate with
FT                                acetaldehyde. {ECO:0000255|HAMAP-
FT                                Rule:MF_00592}.
FT   ACT_SITE    201    201       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00592}.
SQ   SEQUENCE   259 AA;  27705 MW;  021F90D0F1C17DAB CRC64;
     MTELQIAAQR ALRLMDLTTL NDNDTDEKVI ALCHQAKSPA GDTAAVCIYP RFIPIARKTL
     REQGTPDVRI ATVTNFPHGN DDIEIALVET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD
     LVKACKEACA AANVLLKVII ETGELKDAAL IRKASEISIK AGADFIKTST GKVPVNATLE
     SAELMMSVIR DMGVAKRVGF KPAGGVRTAE DAAQYLALAD RLLGEGWADS RHFRFGASSL
     LASLLQTLGY DAKGTGSSY
//

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