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Database: UniProt
Entry: B6ATT5_9RHOB
LinkDB: B6ATT5_9RHOB
Original site: B6ATT5_9RHOB 
ID   B6ATT5_9RHOB            Unreviewed;       307 AA.
AC   B6ATT5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 63.
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:EDZ44176.1};
GN   ORFNames=RB2083_3691 {ECO:0000313|EMBL:EDZ44176.1};
OS   Rhodobacteraceae bacterium HTCC2083.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ44176.1, ECO:0000313|Proteomes:UP000005746};
RN   [1] {ECO:0000313|Proteomes:UP000005746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX   PubMed=21036993; DOI=10.1128/JB.01268-10;
RA   Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT   Roseobacter.";
RL   J. Bacteriol. 193:319-320(2011).
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; DS995276; EDZ44176.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6ATT5; -.
DR   STRING; 314270.RB2083_3691; -.
DR   eggNOG; COG0274; Bacteria.
DR   HOGENOM; CLU_053595_3_0_5; -.
DR   Proteomes; UP000005746; 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   Lyase {ECO:0000313|EMBL:EDZ44176.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005746}.
SQ   SEQUENCE   307 AA;  33403 MW;  C261B066CBB30242 CRC64;
     MDLDLSWVRS VQANTSSIER RAKTLPGRRS VKKDYQAAWL LRAIECIDLT TLSGDDTAER
     VRRLCAKARA PLRDDLKDAL GISSLHTGAI CVYHDMIETA VDALAGSGIP VAAVSTGFPA
     GLSPFHLRVA EIEESVKVGA AEIDIVISRR HVLAGDWQAL YDEMRAFRAA CGDAHVKAIL
     ATGELGTLRN VARASLICMM AGADFIKTST GKESVNATLP VSLVMIRAIR DYHERTGFRV
     GYKPAGGISK AKDALVYLAL MKDELGDRWL QPDLFRFGAS SLLNDIERQL EHHVTGAYSA
     GYRHALA
//
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