ID A0A345QUN9_9RHOB Unreviewed; 329 AA.
AC A0A345QUN9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:AXI49026.1};
GN ORFNames=C1J03_21005 {ECO:0000313|EMBL:AXI49026.1};
OS Sulfitobacter sp. SK012.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389005 {ECO:0000313|EMBL:AXI49026.1, ECO:0000313|Proteomes:UP000253903};
RN [1] {ECO:0000313|EMBL:AXI49026.1, ECO:0000313|Proteomes:UP000253903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK012 {ECO:0000313|EMBL:AXI49026.1,
RC ECO:0000313|Proteomes:UP000253903};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-2018) 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}.
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DR EMBL; CP025804; AXI49026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345QUN9; -.
DR KEGG; sulz:C1J03_21005; -.
DR OrthoDB; 6579831at2; -.
DR Proteomes; UP000253903; Chromosome.
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 SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000253903}.
SQ SEQUENCE 329 AA; 35357 MW; 5B842A5663988BD6 CRC64;
MLRAPTATEN HLPQVAEPRN PGMPLDLNWV LGAQANTSAI ERRAASLPAR RSVKKAHQAA
WLLRAITCID LTTLSGDDTD RRVARLCAKA RQPVAPALLK SLGMAPVTTG AVCVYHEMIP
AAVKALAGSG IPVAAVSTGF PAGLSPLPLR IAEIEQSVAE GAAEIDIVIS RRHVLTGNWH
ALYNEMQQFH VACGDAHVKA ILATGELGSL RNVARASLVC MMAGADFIKT STGKESVNAT
LPVSLVMIRA IRDYYDRTGI RVGYKPAGGI SKAKDSITYL ALIKEELGDR WLRPDLFRFG
ASSLLNDIER QLEHHVTGNY SAGYRHATS
//
