ID A0A285E9R9_9ACTN Unreviewed; 337 AA.
AC A0A285E9R9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN06893097_102479 {ECO:0000313|EMBL:SNX95775.1};
OS Geodermatophilus sabuli.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1564158 {ECO:0000313|EMBL:SNX95775.1, ECO:0000313|Proteomes:UP000219514};
RN [1] {ECO:0000313|EMBL:SNX95775.1, ECO:0000313|Proteomes:UP000219514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46844 {ECO:0000313|EMBL:SNX95775.1,
RC ECO:0000313|Proteomes:UP000219514};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OBDO01000002; SNX95775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285E9R9; -.
DR OrthoDB; 6579831at2; -.
DR Proteomes; UP000219514; 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:UP000219514}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 35561 MW; 3F9A78DBE7C507EC CRC64;
MTHVLDPDAV TAETPPRREP LAPYRDVTRS DAAFRAFLHG LPGVDQVGAE ARVAVLGTRS
IKTTAKAWAI DTAISMVDLT TLEGADTPGK VRSLAAKARR PDPGDPSCPQ VAAVCVYGDL
AGVASEALAG SGVHTAAVAT AFPSGRASRA VKLADVRDAV TNGADEIDMV IDRGAFLAGR
YLDVYDEIVA VKEACARPDG QGRAHLKVIL ETGELVTLDA VRRASWLAML AGGDFIKTST
GKVSPAATLP VCLVMLEAVR DFRAATGRQV GVKPAGGIRN TKDAVKHLVL VNEVAGPDWL
SPDWFRFGAS SLLNDLLLQR QKLRTGHYSG PDHVTID
//