ID A0A1K2FTR0_9ACTN Unreviewed; 333 AA.
AC A0A1K2FTR0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:SFY50956.1};
GN ORFNames=STEPF1_04212 {ECO:0000313|EMBL:SFY50956.1};
OS Streptomyces sp. F-1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY50956.1, ECO:0000313|Proteomes:UP000095403};
RN [1] {ECO:0000313|EMBL:SFY50956.1, ECO:0000313|Proteomes:UP000095403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY50956.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
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; FKJI03000010; SFY50956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K2FTR0; -.
DR Proteomes; UP000095403; 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 Lyase {ECO:0000313|EMBL:SFY50956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095403};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..333
FT /note="deoxyribose-phosphate aldolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009677974"
SQ SEQUENCE 333 AA; 35223 MW; 8FD3412EBBE356A0 CRC64;
MYSRYARRYA RLVTMPTTAP PAHALADVTA SDSTLRRFLH GLPGVDAVGL EARAASLGTR
SIKTTAKAYA IDLAISMVDL TTLEGADTPG KVRALGAKAV HPDPTDRTTP TTAAVCVYPD
MVAVAKEAVA GSGVKVASVA TAFPAGRAAL DVKLADVREA VAAGADEIDM VIDRGAFLAG
RYLKVYDEIV AVKEACGTSA RLKVIFETGE LSTYDNIRRA SWLGMLAGAD FIKTSTGKVA
VNATPANTLL MLEAVRDFRA QTGVQVGVKP AGGIRTSKDA VKFLVVVNET AGADWLDNHW
FRFGASSLLN DLLMQRQKLA TGRYSGPDYV TVD
//
