DEOC_BACSU
ID DEOC_BACSU Reviewed; 223 AA.
AC P39121;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 143.
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, ECO:0000269|PubMed:8550462};
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, ECO:0000303|PubMed:8550462};
GN Name=deoC {ECO:0000255|HAMAP-Rule:MF_00114};
GN Synonyms=dra {ECO:0000303|PubMed:8550462}; OrderedLocusNames=BSU39420;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=168;
RX PubMed=8550462; DOI=10.1128/jb.178.2.424-434.1996;
RA Saxild H.H., Andersen L.N., Hammer K.;
RT "Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction
RT by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded
RT DeoR repressor protein.";
RL J. Bacteriol. 178:424-434(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8867804; DOI=10.1093/dnares/2.6.295;
RA Yoshida K., Fujimyra M., Yanai N., Fujita Y.;
RT "Cloning and sequencing of a 23-kb region of the Bacillus subtilis genome
RT between the iol and hut operons.";
RL DNA Res. 2:295-301(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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 ECO:0000269|PubMed:8550462}.
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 ECO:0000269|PubMed:8550462};
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 -!- INDUCTION: Induced by deoxyadenosine and thymidine. Repressed by DeoR
CC and glucose. {ECO:0000269|PubMed:8550462}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00114}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57662.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X82174; CAA57662.1; ALT_INIT; Genomic_DNA.
DR EMBL; D45912; BAA08337.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15978.2; -; Genomic_DNA.
DR PIR; A69619; A69619.
DR RefSeq; NP_391821.2; NC_000964.3.
DR RefSeq; WP_003244069.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39121; -.
DR SMR; P39121; -.
DR STRING; 224308.BSU39420; -.
DR jPOST; P39121; -.
DR PaxDb; P39121; -.
DR PRIDE; P39121; -.
DR EnsemblBacteria; CAB15978; CAB15978; BSU_39420.
DR GeneID; 938608; -.
DR KEGG; bsu:BSU39420; -.
DR PATRIC; fig|224308.179.peg.4267; -.
DR eggNOG; COG0274; Bacteria.
DR InParanoid; P39121; -.
DR OMA; MNACIPP; -.
DR PhylomeDB; P39121; -.
DR BioCyc; BSUB:BSU39420-MON; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IBA:GO_Central.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IBA:GO_Central.
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 Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..223
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057224"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 152
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT CONFLICT 204..223
FT /note="GASAGVSIVKGENASGGDNY -> APAQAFLS (in Ref. 1;
FT CAA57662 and 2; BAA08337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 23261 MW; E54930DF6DB8E497 CRC64;
MSLANIIDHT ALKPHTQKAD ILKLIEEAKT YKFASVCVNP TWVELAAKEL KGTGVDVCTV
IGFPLGANTT ETKAFETKDA ISKGATEVDM VINIAALKDK EDDVVEADIR GVVEAVAGKA
LVKVIIETCL LTDEEKERAC RLAVSAGADF VKTSTGFSTG GATKEDIALM RKTVGPDIGV
KASGGVRTKE DVDTMVEAGA SRIGASAGVS IVKGENASGG DNY
