ID A0A430JVF7_9ACTO Unreviewed; 220 AA.
AC A0A430JVF7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=EKN07_00670 {ECO:0000313|EMBL:RTE50696.1};
OS Actinobaculum sp. 352.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=2490946 {ECO:0000313|EMBL:RTE50696.1, ECO:0000313|Proteomes:UP000273303};
RN [1] {ECO:0000313|EMBL:RTE50696.1, ECO:0000313|Proteomes:UP000273303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=352 {ECO:0000313|EMBL:RTE50696.1,
RC ECO:0000313|Proteomes:UP000273303};
RA Zhu W.;
RL Submitted (NOV-2018) 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_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:RTE50696.1}.
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DR EMBL; RQSN01000001; RTE50696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430JVF7; -.
DR OrthoDB; 6579831at2; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000273303; 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, ECO:0000313|EMBL:RTE50696.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273303};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT ACT_SITE 94
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 156
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 186
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ SEQUENCE 220 AA; 22828 MW; 188195A9789748B5 CRC64;
MSQYSREQVA GMVDHTLLKP EATLDDVRRL IADAKELGTY SVCISPSMLP LPADIDLGEV
KLAVVCGFPS GAHRSEVKAA EAKQAVADGA DEVDMVINVG HAVEGRYDAV QADIAAVREA
IPNAVLKVII ESAALSDEQI VAVCEASKAA GADFVKTSTG FHPTGGASVH AVELMKKTVG
DDLEVKASGG IRDGAFASEL LDAGATRLGL SSTQKVLDTL
//
