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DEOC_STRP1
ID   DEOC_STRP1              Reviewed;         223 AA.
AC   Q99Y51; Q48WS2;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 145.
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};
GN   OrderedLocusNames=SPy_1867, M5005_Spy1585;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34581.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52203.1; -; Genomic_DNA.
DR   RefSeq; NP_269860.1; NC_002737.2.
DR   AlphaFoldDB; Q99Y51; -.
DR   SMR; Q99Y51; -.
DR   STRING; 1314.HKU360_01706; -.
DR   PaxDb; Q99Y51; -.
DR   EnsemblBacteria; AAK34581; AAK34581; SPy_1867.
DR   KEGG; spy:SPy_1867; -.
DR   KEGG; spz:M5005_Spy1585; -.
DR   PATRIC; fig|160490.10.peg.1619; -.
DR   HOGENOM; CLU_053595_0_2_9; -.
DR   OMA; KQYLDST; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000000750; 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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..223
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_0000057274"
FT   ACT_SITE        91
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        153
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        182
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   223 AA;  24007 MW;  94E65FEB92692F75 CRC64;
     MEVKDILKTV DHTLLATTAT WPEIQTILDD AMAYETASAC IPASYVKKAA EYVSGKLAIC
     TVIGFPNGYS TTAAKVFECQ DAIQNGADEI DMVINLTDVK NGDFDTVEEE IRQIKAKCQD
     HILKVIVETC QLTKEELIEL CGVVTRSGAD FIKTSTGFST AGATFEDVEV MAKYVGEGVK
     IKAAGGISSL EDAKTFIALG ASRLGTSRII KIVKNEATKT DSY
 
 
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