ID   K1SNH8_9ZZZZ            Unreviewed;       123 AA.
AC   K1SNH8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 15.
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};
DE   Flags: Fragment;
GN   ORFNames=LEA_11987 {ECO:0000313|EMBL:EKC62167.1};
OS   human gut metagenome.
OC   unclassified sequences; metagenomes; organismal metagenomes.
OX   NCBI_TaxID=408170 {ECO:0000313|EMBL:EKC62167.1};
RN   [1] {ECO:0000313|EMBL:EKC62167.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22891823; DOI=10.1111/j.1462-2920.2012.02845.x;
RA   Ferrer M., Ruiz A., Lanza F., Haange S.B., Oberbach A., Till H.,
RA   Bargiela R., Campoy C., Segura M.T., Richter M., von Bergen M., Seifert J.,
RA   Suarez A.;
RT   "Microbiota from the distal guts of lean and obese adolescents exhibit
RT   partial functional redundancy besides clear differences in community
RT   structure.";
RL   Environ. Microbiol. 15:211-226(2013).
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:EKC62167.1}.
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DR   EMBL; AJWY01008095; EKC62167.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1SNH8; -.
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   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EKC62167.1}.
FT   NON_TER         123
FT                   /evidence="ECO:0000313|EMBL:EKC62167.1"
SQ   SEQUENCE   123 AA;  13004 MW;  CD4894133769A6EF CRC64;
     MALHTGADEI DIVIPVGKFL SGDYEGMCDE IEELKAVCGE HHLKVILETG ALGSASNIKK
     ASILSMYSGA DFIKTSTGKE NPAATPEAAL VMCEAIKEYY MTTGRKVGFK PAGGINTVHD
     ALV
//