ID   D3HTC1_LEGLN            Unreviewed;       254 AA.
AC   D3HTC1;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
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:CBJ12163.1};
GN   OrderedLocusNames=LLO_1786 {ECO:0000313|EMBL:CBJ12163.1};
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ12163.1, ECO:0000313|Proteomes:UP000001060};
RN   [1] {ECO:0000313|EMBL:CBJ12163.1, ECO:0000313|Proteomes:UP000001060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150 {ECO:0000313|EMBL:CBJ12163.1,
RC   ECO:0000313|Proteomes:UP000001060};
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(2010).
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; FN650140; CBJ12163.1; -; Genomic_DNA.
DR   RefSeq; WP_003636983.1; NC_013861.1.
DR   AlphaFoldDB; D3HTC1; -.
DR   STRING; 661367.LLO_1786; -.
DR   KEGG; llo:LLO_1786; -.
DR   eggNOG; COG0274; Bacteria.
DR   HOGENOM; CLU_053595_3_1_6; -.
DR   OrthoDB; 6579831at2; -.
DR   Proteomes; UP000001060; 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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000001060}.
SQ   SEQUENCE   254 AA;  28158 MW;  1756C23FED9EBD99 CRC64;
     MTVENHLNNV MEKLLDRFPK QFITVKQLIH SIDLTLLDEH ASTEELTQLK HDAQQNGVAA
     LCIYMQHLPE IMPQHSVSTA TVINFPQGME PLDVSLASID KAAHLGVNEI DYVFPYSMYL
     EGHTQKALHQ CYTISELCKQ HNLVLKVILE SGAFSNLQDI YTISRELIDL ECNFIKTSTG
     KIMPGASLSA AIAILSAIKD ANASCGIKIS GGIKKPQQAF HYAVLAELMI NKPINKNWFR
     IGASSLLGEL LKTN
//