ID A0A384B5E6_BALAS Unreviewed; 275 AA.
AC A0A384B5E6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DERA {ECO:0000313|RefSeq:XP_007194865.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007194865.1};
RN [1] {ECO:0000313|RefSeq:XP_007194865.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007194865.1};
RG RefSeq;
RL Submitted (JAN-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 RefSeq; XP_007194865.1; XM_007194803.2.
DR AlphaFoldDB; A0A384B5E6; -.
DR CTD; 51071; -.
DR OrthoDB; 1330179at2759; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000261681; 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 Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 2.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Schiff base {ECO:0000256|PIRSR:PIRSR001357-50}.
FT ACT_SITE 175
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
FT ACT_SITE 211
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
SQ SEQUENCE 275 AA; 30528 MW; 51E3C6C79E9D82B0 CRC64;
MSAHQRGTEF DLSWISKIQV NQPAVLRRAE QIQARRPVKK EWQAAWLLKA VTFIDLTTLS
GDDTSSNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPACVCDAV KALKAAGCDI
PVASVATGFP AGQTHLKTRL EEIRLAVEDG ASEIDVVINR TLVLTGQWEG SDFIKTSTGK
ETVNATFPVA IVMLRAIRDF FWKTGNKIGF KPAGGIRSAK DSLAWLSLIK EELGDEWLKP
ELFRIGASTL LADIERQIYH HVTGRYAAYH DLPMS
//
