ID E5YK96_9ENTR Unreviewed; 259 AA.
AC E5YK96;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00592};
DE Short=DERA {ECO:0000256|HAMAP-Rule:MF_00592};
DE EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00592};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00592};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00592};
DE Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00592};
GN Name=deoC {ECO:0000256|HAMAP-Rule:MF_00592};
GN ORFNames=HMPREF0864_02960 {ECO:0000313|EMBL:EFV39444.1};
OS Enterobacteriaceae bacterium 9_2_54FAA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=469613 {ECO:0000313|EMBL:EFV39444.1, ECO:0000313|Proteomes:UP000004908};
RN [1] {ECO:0000313|EMBL:EFV39444.1, ECO:0000313|Proteomes:UP000004908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV39444.1,
RC ECO:0000313|Proteomes:UP000004908};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Sibley C., Haas B., Nusbaum C.,
RA Birren B.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFV39444.1, ECO:0000313|Proteomes:UP000004908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV39444.1,
RC ECO:0000313|Proteomes:UP000004908};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Ambrose C.,
RA Strauss J., Sibley C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterobacteriaceae bacterium 9_2_54FAA.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00592}.
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:0000256|ARBA:ARBA00000764, ECO:0000256|HAMAP-
CC 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.
CC {ECO:0000256|ARBA:ARBA00004816, ECO:0000256|HAMAP-Rule:MF_00592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00592}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009473, ECO:0000256|HAMAP-
CC Rule:MF_00592}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFV39444.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADCU02000001; EFV39444.1; -; Genomic_DNA.
DR AlphaFoldDB; E5YK96; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000004908; Unassembled WGS sequence.
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; Aldolase class I; 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 NCBIfam; TIGR00126; deoC; 1.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00592};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00592};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00592}.
FT ACT_SITE 102
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00592"
FT ACT_SITE 167
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00592"
FT ACT_SITE 201
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00592"
SQ SEQUENCE 259 AA; 27638 MW; 61219A29D83ED4DD CRC64;
MTDLKVAAKR ALQLMDLTTL NEDDTDEKVI ALCHQAKSPV GNTAAVCIYP RFIPIARKTL
REQGTPEIHI ATVTNFPHGN DDIAIALAET KAAIAYGADE VDVVFPYRAL MAGNEQVGFD
MVKVCKDACN EAGVLLKVII ETGELKDAAL IRKASEISIK AGADFIKTST GKVPVNATLE
SAEIMMTVIR DMGVSKTVGF KPAGGVRTAE DAAEYLALAG RLLGDDWADS RHFRFGASSL
LASLLKTLGY DTKGTGSAY
//
