ID L0MAQ5_ENTBF Unreviewed; 259 AA.
AC L0MAQ5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=D782_3884 {ECO:0000313|EMBL:AGB79791.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB79791.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB79791.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB79791.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
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}.
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DR EMBL; CP003938; AGB79791.1; -; Genomic_DNA.
DR AlphaFoldDB; L0MAQ5; -.
DR STRING; 693444.D782_3884; -.
DR KEGG; ebf:D782_3884; -.
DR PATRIC; fig|693444.3.peg.3707; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_3_1_6; -.
DR OrthoDB; 6579831at2; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000011002; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000011002};
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; 27572 MW; 72F8B2EFBDBBDA03 CRC64;
MTDLTASSLR ALKLMDLTTL NEDDTDAKVI ALCHQAKTPV GNTAAVCIYP RFIPIARKTL
NEQGTPDIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL IAGNEQVGFD
LVKACKDACA AANVLLKVII ETGELKEEAL IRKASEISIK AGADFIKTST GKVPVNATPE
SARIMMEVIR DMGVSKTVGF KPAGGVRSAE DAQQFLAIAD ELFGADWADS RHYRFGASSL
LASLLKALGH GDGKSASSY
//
