DEOC_SHEHH
ID DEOC_SHEHH Reviewed; 257 AA.
AC B0TQ91;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Shal_3136;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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_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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000931; ABZ77683.1; -; Genomic_DNA.
DR RefSeq; WP_012278208.1; NC_010334.1.
DR PDB; 5C6M; X-ray; 1.76 A; A/B/C/D=1-257.
DR PDBsum; 5C6M; -.
DR AlphaFoldDB; B0TQ91; -.
DR SMR; B0TQ91; -.
DR STRING; 458817.Shal_3136; -.
DR EnsemblBacteria; ABZ77683; ABZ77683; Shal_3136.
DR KEGG; shl:Shal_3136; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_3_1_6; -.
DR OMA; MNACIPP; -.
DR OrthoDB; 1227369at2; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000001317; 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_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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Schiff base.
FT CHAIN 1..257
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_1000082419"
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 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:5C6M"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:5C6M"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:5C6M"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:5C6M"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5C6M"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:5C6M"
SQ SEQUENCE 257 AA; 27082 MW; 40C6A6DAA78C3A79 CRC64;
MSDLKKAAQQ AISLMDLTTL NDDDTDQKVI ELCHKAKTPA GDTAAICIYP RFIPIARKTL
NEIGGDDIKI ATVTNFPHGN DDIAIAVLET RAAVAYGADE VDVVFPYRAL MEGNETVGFE
LVKACKEACG EDTILKVIIE SGVLADPALI RKASELSIDA GADFIKTSTG KVAVNATLEA
AEIMMTVISE KNPKVGFKPA GGVKDAAAAA EFLGVAARLL GDDWATPATF RFGASSLLTN
LLHTLELADA PQGAQGY
