ID A0A0R2C5N6_9LACO Unreviewed; 238 AA.
AC A0A0R2C5N6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE Short=DERA {ECO:0000256|HAMAP-Rule:MF_00114};
DE EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00114};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
GN Name=deoC {ECO:0000256|HAMAP-Rule:MF_00114};
GN ORFNames=FD19_GL001697 {ECO:0000313|EMBL:KRM86839.1};
OS Lacticaseibacillus thailandensis DSM 22698 = JCM 13996.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423810 {ECO:0000313|EMBL:KRM86839.1, ECO:0000313|Proteomes:UP000051789};
RN [1] {ECO:0000313|EMBL:KRM86839.1, ECO:0000313|Proteomes:UP000051789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22698 {ECO:0000313|EMBL:KRM86839.1,
RC ECO:0000313|Proteomes:UP000051789};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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_00114}.
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_00114};
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:0000256|HAMAP-
CC Rule:MF_00114}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00114}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00010936, ECO:0000256|HAMAP-
CC Rule:MF_00114}.
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:KRM86839.1}.
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DR EMBL; AYZK01000005; KRM86839.1; -; Genomic_DNA.
DR RefSeq; WP_054750533.1; NZ_BBER01000004.1.
DR AlphaFoldDB; A0A0R2C5N6; -.
DR STRING; 1423810.FD19_GL001697; -.
DR PATRIC; fig|1423810.4.peg.1745; -.
DR OrthoDB; 9778711at2; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000051789; 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_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 NCBIfam; TIGR00126; deoC; 1.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF1; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00114};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00114};
KW Reference proteome {ECO:0000313|Proteomes:UP000051789};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT ACT_SITE 95
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 159
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ SEQUENCE 238 AA; 25984 MW; 079D400E269009CF CRC64;
MTAYSLDDFA RLIDHTNLHA DATRADMIKL CNEAKKYHFK MVAINQVQSA LCAEQLQGTD
IDTGAAIAFP LGQTSIAAKV FEAKDAMDHG ANEIDYVLNI TELKDGNDDY IEDEMTQMVA
ACHERNVPCK VIFENCYLTK EEIVRAATIA KRVRPDFIKT STGFGTGGAT VADVRLMKQT
VGDAVHVKAA GGIRNSDDFL AMIEAGADRI GTSSGVKIIE ALRRRMADDH VDSIAINR
//
