ID A0A3B3QFX0_9TELE Unreviewed; 318 AA.
AC A0A3B3QFX0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000004659.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000004659.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3QFX0; -.
DR STRING; 1676925.ENSPKIP00000004659; -.
DR Ensembl; ENSPKIT00000028645.1; ENSPKIP00000004659.1; ENSPKIG00000021666.1.
DR GeneTree; ENSGT00390000007878; -.
DR OrthoDB; 1330179at2759; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000261540; Unplaced.
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 GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
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 Schiff base {ECO:0000256|PIRSR:PIRSR001357-50}.
FT ACT_SITE 218
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
FT ACT_SITE 254
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
SQ SEQUENCE 318 AA; 35090 MW; 55B799F7E1812197 CRC64;
MPARNPGIDL DLEWVSKVRV NQQAVLRRAQ QIQARKQGKK QWQAAWLLKA VTCIDLTTLA
GDDTPSNVHR LCMKAMQPIR HDLLENMDMH DKGITTAAVC VYPARVADAV KSLKAANSSI
SVASVATGFP AGQTALKTRL EEVRMAVEDG AREIDIVINR SLALTGQWQA LYQEIHQFRE
ACGEAHMKTI LAVGELGTFT NVYKASVVAM MAGSDFIKTS TGKESVNATY PVAVVMVRAI
RDYFLRTGHK VGFKPAGGIR TSKDSLVWLT LMKEELGDEW LCPALFRLGA STLLADIERQ
IYHYVTGRYA APYELPLA
//
