ID C2MAD5_9PORP Unreviewed; 288 AA.
AC C2MAD5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=deoxyribose-phosphate aldolase {ECO:0000256|ARBA:ARBA00012515};
DE EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|ARBA:ARBA00031814};
GN Name=deoC {ECO:0000313|EMBL:EEK17296.1};
GN ORFNames=PORUE0001_1209 {ECO:0000313|EMBL:EEK17296.1};
OS Porphyromonas uenonis 60-3.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=596327 {ECO:0000313|EMBL:EEK17296.1, ECO:0000313|Proteomes:UP000003303};
RN [1] {ECO:0000313|EMBL:EEK17296.1, ECO:0000313|Proteomes:UP000003303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=60-3 {ECO:0000313|EMBL:EEK17296.1,
RC ECO:0000313|Proteomes:UP000003303};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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};
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}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009473}.
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:EEK17296.1}.
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DR EMBL; ACLR01000088; EEK17296.1; -; Genomic_DNA.
DR RefSeq; WP_007364871.1; NZ_ACLR01000088.1.
DR AlphaFoldDB; C2MAD5; -.
DR STRING; 596327.PORUE0001_1209; -.
DR eggNOG; COG0274; Bacteria.
DR OrthoDB; 9778711at2; -.
DR Proteomes; UP000003303; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR CDD; cd00959; DeoC; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
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 Lyase {ECO:0000313|EMBL:EEK17296.1}.
SQ SEQUENCE 288 AA; 31500 MW; 1DFF61D20E97EBA1 CRC64;
MHQIDKYHKA ISLYEPIEGD VTAKVQAIID KHYKECYTPE VLKLLYSCID LTTLMGGDTD
ESVTKMVAGV NDFETNHPDI PNVAAICVYP ALVPTVKATL TCPDVRIASV AAGFPASQTF
PEIKVAEVSM AVAEGANEVD VVLNLNRFLS EDYDGVCTEI EELKDAARGA HLKVIIESGL
LADPRQIQIA SILSLYSGAD FIKTSTGKEY PGASLEAAYV MCQTLRKYYE LHGERRGFKA
SGGVRTPEDV VKYYCIVKEI LGEEWLTPEL FRLGASSLGK NLLKAIEG
//
