ID A0A433K2P6_9GAMM Unreviewed; 253 AA.
AC A0A433K2P6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
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:RUR12293.1};
GN ORFNames=ELY15_05480 {ECO:0000313|EMBL:RUR12293.1};
OS Legionella sp. km772.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=2498111 {ECO:0000313|EMBL:RUR12293.1, ECO:0000313|Proteomes:UP000287796};
RN [1] {ECO:0000313|EMBL:RUR12293.1, ECO:0000313|Proteomes:UP000287796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=km772 {ECO:0000313|Proteomes:UP000287796};
RA Wu H.;
RT "Legionella sp,whole genome shotgun sequence.";
RL Submitted (DEC-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}.
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:RUR12293.1}.
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DR EMBL; RZGQ01000031; RUR12293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433K2P6; -.
DR OrthoDB; 6579831at2; -.
DR Proteomes; UP000287796; 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 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:RUR12293.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287796}.
SQ SEQUENCE 253 AA; 27900 MW; 8352A53372ECD68D CRC64;
MSINNHLNKV LGDFLSKPSE LISNQQLTSC IDLTLLNEQA SPNDLSSINH LAARHQVAAL
CVFPKDLVHC KKHSDIHLAT VINFPHGNQN LNECVTQINQ SRLNGVKEID YVIPFRAYLE
GKEQEAINHA AAISTYCKEQ GLLLKVILET GEFSDLAMLY QLTNELLTLN IDFLKTSTGK
TPQGASLSAV FTLLSALKDS RKNCGIKVSG GIKTVAQAKN YAALAQYFLQ KTIDKNWFRI
GASSLLEELT KSN
//
