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Database: UniProt
Entry: A0A1M6B7Z8_9RHOB
LinkDB: A0A1M6B7Z8_9RHOB
Original site: A0A1M6B7Z8_9RHOB 
ID   A0A1M6B7Z8_9RHOB        Unreviewed;       330 AA.
AC   A0A1M6B7Z8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN05444000_101152 {ECO:0000313|EMBL:SHI44861.1};
OS   Shimia gijangensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1470563 {ECO:0000313|EMBL:SHI44861.1, ECO:0000313|Proteomes:UP000183982};
RN   [1] {ECO:0000313|Proteomes:UP000183982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100564 {ECO:0000313|Proteomes:UP000183982};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FQZQ01000001; SHI44861.1; -; Genomic_DNA.
DR   RefSeq; WP_073248387.1; NZ_FQZQ01000001.1.
DR   AlphaFoldDB; A0A1M6B7Z8; -.
DR   STRING; 1470563.SAMN05444000_101152; -.
DR   OrthoDB; 6579831at2; -.
DR   Proteomes; UP000183982; 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   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000183982}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   330 AA;  36193 MW;  11A75BD659DF3AFD CRC64;
     MHSPTTTPTD HQLPQAIEPR NPGMELDLDW VRRAQANTSA IERRAKSLPG RRSVKKDYQA
     AWLLKAITCM DLTTLSGDDT EGRVRRLCAK ARQPVRAELL EQLGMPDITT GAICVYHDMI
     STAVDALDGS GIPVAAVSTG FPAGLSPFHL RVEEIREGVK AGADEIDIVI TRRHVLQGNW
     QALYDEMRAF REACGDAHVK AILATGELGT LRNVARASLV CMMAGADFIK TSTGKESVNA
     TLPVSLVMVR AIRDYYDRTG YRVGYKPAGG ISKAKDAVTY LSLMKDELGD RWLQPDLFRF
     GASSLLGDIE RQLEHHVTGA YSATYRHALA
//
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