ID A0A0A1TT50_9HYPO Unreviewed; 261 AA.
AC A0A0A1TT50;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=VHEMI10341 {ECO:0000313|EMBL:CEJ94832.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ94832.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ94832.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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}.
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DR EMBL; CDHN01000007; CEJ94832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1TT50; -.
DR STRING; 1531966.A0A0A1TT50; -.
DR HOGENOM; CLU_053595_0_2_1; -.
DR OrthoDB; 202625at2759; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000039046; 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 PIRSF; PIRSF001357; 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:UP000039046};
KW Schiff base {ECO:0000256|PIRSR:PIRSR001357-50}.
FT ACT_SITE 163
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
FT ACT_SITE 202
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
SQ SEQUENCE 261 AA; 28172 MW; 2928775F20D1EF7C CRC64;
MAPQTISVSL PKLAKVIDHS LLHPTMTDAQ VRSGLELSRK YNVATACVKP YSVPLAREVL
AGSQVGICAV VGFPHGNSVA AVKITETQDA LAAGATEIDM VVNIGKVLSG EWEYVEHEIQ
AINRVTVAKG AILKVIFEND FLEDTHIIKL CEICTRQEVA FVKTSTGYGF VKQPDGMYTY
KGATIPHLKL MRQHSGPNVQ IKAAGGVRTL DDFLYVMSLG VTRVGASATE AIMNEAAARG
LTDEDKEFEV KEKESTTSGS Y
//
