DEOC_MYCA1
ID DEOC_MYCA1 Reviewed; 223 AA.
AC A0QLL2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114};
DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
GN Name=deoC {ECO:0000255|HAMAP-Rule:MF_00114}; OrderedLocusNames=MAV_4672;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00114}.
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:0000255|HAMAP-Rule:MF_00114};
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. {ECO:0000255|HAMAP-
CC Rule:MF_00114}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00114}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00114}.
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DR EMBL; CP000479; ABK67136.1; -; Genomic_DNA.
DR RefSeq; WP_011726185.1; NC_008595.1.
DR PDB; 3NG3; X-ray; 2.15 A; A/B/C/D=1-223.
DR PDBsum; 3NG3; -.
DR AlphaFoldDB; A0QLL2; -.
DR SMR; A0QLL2; -.
DR PRIDE; A0QLL2; -.
DR EnsemblBacteria; ABK67136; ABK67136; MAV_4672.
DR KEGG; mav:MAV_4672; -.
DR HOGENOM; CLU_053595_0_0_11; -.
DR OMA; KRGIGNE; -.
DR OrthoDB; 1227369at2; -.
DR UniPathway; UPA00002; UER00468.
DR EvolutionaryTrace; A0QLL2; -.
DR Proteomes; UP000001574; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
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; -; 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 PANTHER; PTHR10889; PTHR10889; 1.
DR PANTHER; PTHR10889:SF1; PTHR10889:SF1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR TIGRFAMs; TIGR00126; deoC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Schiff base.
FT CHAIN 1..223
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_1000015324"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 158
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3NG3"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:3NG3"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:3NG3"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:3NG3"
SQ SEQUENCE 223 AA; 21723 MW; 33A436559EB7FC1A CRC64;
MTPTRAQLAA FVDHTLLKPE ATAADVAALV TEAAELGVYA VCVSPPMVPA AVQAGAGVRV
ASVAGFPSGK HVSAVKAHEA ALAVASGAAE IDMVIDVGAA LAGDLDGVRA DIAAVRGAVG
GAVLKVIVES SALLALADEH TLVRVCRAAE DAGADFVKTS TGFHPSGGAS VRAVALMAEA
VGGRLGVKAS GGIRTAADAL AMLDAGATRL GLSGTRAVLD GLG
