ID A0A0V1C9Z4_TRIBR Unreviewed; 327 AA.
AC A0A0V1C9Z4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
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};
DE Flags: Fragment;
GN Name=Dera {ECO:0000313|EMBL:KRY46148.1};
GN ORFNames=T03_11183 {ECO:0000313|EMBL:KRY46148.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY46148.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY46148.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY46148.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY46148.1}.
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DR EMBL; JYDI01000305; KRY46148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1C9Z4; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000054653; 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 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 SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT NON_TER 327
FT /evidence="ECO:0000313|EMBL:KRY46148.1"
SQ SEQUENCE 327 AA; 37201 MW; 5668D9EB7C9B7E85 CRC64;
MLTVDYFRMS VVQRMANLSA TDFDLSNITY GSEVLHNLGY YMKSIAEEAE RINTEEKIDI
IKKLISFTDL TSLNATDSFE TVKKLIDRAT QPLALSLLND SETCCASVCI YPYYVKDAVA
FRNFACALGR SFVSIVTVAG AFPSGMYKLI TKVHECREAK EDGADEIDVV INRGLVATRN
WRVVQRVGSD EKRDRFADFD ENHLVDRGYR IFYGHLCGSY GSSFIKSSTG KEKLNSTVPG
SLVICLAIRS FFLRYKRQVG FKAAGGIKTA QEAIVYYVLV KQILGERWLS REYFRIGASE
LLDDLYLHDA REMQHHRPTF FERLVRL
//
