DEOC_VIBCH
ID DEOC_VIBCH Reviewed; 259 AA.
AC Q9KPL7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00592};
DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00592};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
GN Name=deoC {ECO:0000255|HAMAP-Rule:MF_00592}; OrderedLocusNames=VC_2350;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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_00592}.
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_00592};
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_00592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00592}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305}.
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DR EMBL; AE003852; AAF95493.1; -; Genomic_DNA.
DR PIR; F82087; F82087.
DR RefSeq; NP_231980.1; NC_002505.1.
DR RefSeq; WP_001292544.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KPL7; -.
DR SMR; Q9KPL7; -.
DR STRING; 243277.VC_2350; -.
DR DNASU; 2613146; -.
DR EnsemblBacteria; AAF95493; AAF95493; VC_2350.
DR GeneID; 57740961; -.
DR KEGG; vch:VC_2350; -.
DR PATRIC; fig|243277.26.peg.2237; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_3_1_6; -.
DR OMA; MNACIPP; -.
DR BioCyc; VCHO:VC2350-MON; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000000584; Chromosome 1.
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_00592; DeoC_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR023649; DeoC_typeII.
DR PANTHER; PTHR10889; PTHR10889; 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..259
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057305"
FT ACT_SITE 102
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT ACT_SITE 200
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
SQ SEQUENCE 259 AA; 27959 MW; 2876B07AC6527C73 CRC64;
MSELKVAALR ALKLMDLTTL NDNDTDAKVI QLCHDAKSPV GNTAAICIYP RFIPIAKKTL
REQGTPEIRI ATVTNFPHGN DDIEIAVAET KAAVAYGADE VDVVFPYRAL IAGNEQVGFD
LVKQCKAACG DKVLLKVIIE TGELKQEALI KKASQICIEA GADFIKTSTG KVPVNATPEY
ARMMLEVIRD MGVAKTVGFK PAGGVRTAED AQQYLAMADE ILGGDWADSR HYRFGASSLL
TNLLNTLEVT DQKADPAAY
