ID A0A0F4YFR8_TALEM Unreviewed; 391 AA.
AC A0A0F4YFR8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, 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=T310_9279 {ECO:0000313|EMBL:KKA17102.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA17102.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA17102.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA17102.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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 -!- 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:KKA17102.1}.
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DR EMBL; LASV01000713; KKA17102.1; -; Genomic_DNA.
DR RefSeq; XP_013323714.1; XM_013468260.1.
DR AlphaFoldDB; A0A0F4YFR8; -.
DR STRING; 1408163.A0A0F4YFR8; -.
DR GeneID; 25321219; -.
DR OrthoDB; 202625at2759; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000053958; 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 InterPro; IPR024491; Se_SelK/SelG.
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 Pfam; PF10961; SelK_SelG; 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:UP000053958}.
FT REGION 61..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 41873 MW; B86D4A22B2141324 CRC64;
MSAPSSSRPY VSGGQMLQSP PLSVRVIRFF ESIYIFLGLY FVSLFSLDPY TAAQSSQFNV
ARPQNKPNTR PRWGGGSYGG GYGGGGGPGG SGGPRRIGRV DDIRGPECRS CHLENHLYLH
WTMSAQVAPP TTDADWATLI STTKDGLPES EVVYPTPAPS SIAKTIDHTQ LDPSVRLEQI
TALCEEARKY NFATVCVRFP NVARAVDLLK DTDIGVSCVI GFPEGTQKTA DKVEEAKSAV
QRGASELDMV MNWPLLQQGK YTEVYDDVHA VRKAAPSPTK LKVILETSQL SRDEVIAGCV
ISSMAGADFV KTSTGYKGEG ASVENVRLMR ETVDLIGKGC KVKASGGIRS AERCIAMLKS
GADRIGASAG VRIMQELGGN IEAASTPQGN F
//
