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Database: UniProt
Entry: K2N3M9_TRYCR
LinkDB: K2N3M9_TRYCR
Original site: K2N3M9_TRYCR 
ID   K2N3M9_TRYCR            Unreviewed;       274 AA.
AC   K2N3M9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
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};
GN   ORFNames=MOQ_006916 {ECO:0000313|EMBL:EKF29307.1}, MOQ_006980
GN   {ECO:0000313|EMBL:EKF29246.1};
OS   Trypanosoma cruzi marinkellei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF29246.1, ECO:0000313|Proteomes:UP000007350};
RN   [1] {ECO:0000313|EMBL:EKF29246.1, ECO:0000313|Proteomes:UP000007350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|EMBL:EKF29246.1,
RC   ECO:0000313|Proteomes:UP000007350};
RX   PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA   Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA   Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA   Andersson B.;
RT   "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT   with the bat-restricted subspecies T. cruzi marinkellei.";
RL   BMC Genomics 13:531-531(2012).
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   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00010936}.
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:EKF29246.1}.
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DR   EMBL; AHKC01013712; EKF29246.1; -; Genomic_DNA.
DR   EMBL; AHKC01013550; EKF29307.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2N3M9; -.
DR   EnsemblProtists; EKF29246; EKF29246; MOQ_006980.
DR   EnsemblProtists; EKF29307; EKF29307; MOQ_006916.
DR   OrthoDB; 202625at2759; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000007350; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   HAMAP; MF_00114; DeoC_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR028581; DeoC_typeI.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889:SF1; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007350}.
SQ   SEQUENCE   274 AA;  29470 MW;  B900ABF6394EEC35 CRC64;
     MTDLRMTERP GFTGKLNEKI LERVRFLAGE LQIPDLESKF PHLKVTDGSW RPPLPGDDVN
     LAAYIDHTQL KQEASKADIV KLCEESNQYK FYAVCVNSSR VKLCVEKLRG TGIKTGGSCG
     FPLGACSTAT KVAEAKTMVQ EGAEDMDMVL NVGALKDKDY RYVLEDIKAV LAVCPPHVTT
     KVIFETCLLT EEEIIDCAII SVVAGASFVK TSTGFNSGGG ATPEAIDVML AVVGKAAKVK
     ASGGVRDRCT ALQYVKAGVS RLGTSRSIDI VTCK
//
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