ID A0A1I6TNA0_9RHOB Unreviewed; 333 AA.
AC A0A1I6TNA0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04488040_2365 {ECO:0000313|EMBL:SFS90712.1};
OS Sulfitobacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=394264 {ECO:0000313|EMBL:SFS90712.1, ECO:0000313|Proteomes:UP000199239};
RN [1] {ECO:0000313|Proteomes:UP000199239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23422 {ECO:0000313|Proteomes:UP000199239};
RA Varghese N., Submissions S.;
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; FPAJ01000003; SFS90712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6TNA0; -.
DR STRING; 394264.SAMN04488040_2365; -.
DR OrthoDB; 6579831at2; -.
DR Proteomes; UP000199239; 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:UP000199239}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 36051 MW; CF5EA1A3DA4301CD CRC64;
MSTHVTTPAG IAQSHLPQVT EPRNPGMPLD MDWVRSVQVN TSAVERRASS IAARRSVKKD
HQAAWLLRAI TCIDLTTLSG DDTARRVERL CAKARQPVSP DLMKALGMGP ITVGAVCVYH
EMIAPAKAAL TGTNIPIAAV STGFPAGLSP FELRIKEIEM SVAEGAAEID IVISRRHVLS
GDWQALYDEM RAFRTACGDA HVKAILATGE LGSLRNVARA SLVCMMAGAD FIKTSTGKES
VNATLPVTLV MIRAIRDYFD RTGIRVGYKP AGGISKAKDA ITYLALIKEE LGDRWLRPDL
FRFGASSLLG DIERQLEHHV TGSYSASYRH AIS
//
