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Database: UniProt
Entry: A0A1I6JCI7_9BURK
LinkDB: A0A1I6JCI7_9BURK
Original site: A0A1I6JCI7_9BURK 
ID   A0A1I6JCI7_9BURK        Unreviewed;       258 AA.
AC   A0A1I6JCI7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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   ORFNames=SAMN05428960_1328 {ECO:0000313|EMBL:SFR76679.1};
OS   Mitsuaria sp. PDC51.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1881035 {ECO:0000313|EMBL:SFR76679.1, ECO:0000313|Proteomes:UP000199246};
RN   [1] {ECO:0000313|EMBL:SFR76679.1, ECO:0000313|Proteomes:UP000199246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PDC51 {ECO:0000313|EMBL:SFR76679.1,
RC   ECO:0000313|Proteomes:UP000199246};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOZE01000001; SFR76679.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6JCI7; -.
DR   STRING; 1881035.SAMN05428960_1328; -.
DR   Proteomes; UP000199246; 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   Reference proteome {ECO:0000313|Proteomes:UP000199246}.
SQ   SEQUENCE   258 AA;  26370 MW;  FB2157941F9BC498 CRC64;
     MKTEMSLEQA ARLALQCLDL TSLNDGDTAA DIDALCARAI GAPERGHVAA VCVWPRFVAQ
     ARAALPADIR VAAVANFPDG SLDLPRVLAE VDAIAQAGAQ EVDVVLPYKA LMAGQSTEVA
     EFLAEVRHAT RPLTLKVIIE SGELGSPARI AEATRQALMA GADFVKTSTG KSPVSATPEA
     AATMLREIAA SGLGNAGFKA SGGIRSVADA RGYLQLAADA LGVSALTAQR MRFGASGLLG
     DIEAVLAGQD SAAVSAAY
//
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