DEOC_ALKHC
ID DEOC_ALKHC Reviewed; 224 AA.
AC Q9KD67;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
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}; Synonyms=dra;
GN OrderedLocusNames=BH1352;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(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_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, ECO:0000305}.
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DR EMBL; BA000004; BAB05071.1; -; Genomic_DNA.
DR PIR; H83818; H83818.
DR RefSeq; WP_010897517.1; NC_002570.2.
DR PDB; 6D33; X-ray; 2.50 A; A/B/C/D/E/F=1-224.
DR PDB; 6MSW; X-ray; 2.17 A; A/B/C/D/E/F=1-224.
DR PDBsum; 6D33; -.
DR PDBsum; 6MSW; -.
DR AlphaFoldDB; Q9KD67; -.
DR SMR; Q9KD67; -.
DR STRING; 272558.10173968; -.
DR EnsemblBacteria; BAB05071; BAB05071; BAB05071.
DR KEGG; bha:BH1352; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_0_2_9; -.
DR OMA; MNACIPP; -.
DR OrthoDB; 1227369at2; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000001258; 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; Reference proteome; Schiff base.
FT CHAIN 1..224
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057223"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 155
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:6MSW"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:6MSW"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:6MSW"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:6MSW"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6MSW"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:6MSW"
SQ SEQUENCE 224 AA; 23362 MW; 5CC79183BB424502 CRC64;
MSRSIAQMID HTLLKPNTTE DQIVKLCEEA KEYSFASVCV NPTWVALAAQ LLKDAPDVKV
CTVIGFPLGA TTPEVKAFET TNAIENGATE VDMVINIGAL KDKQYELVGR DIQAVVKAAE
GKALTKVIIE TSLLTEEEKK AACELAVKAG ADFVKTSTGF SGGGATAEDI ALMRKVVGPN
LGVKASGGVR DLSDAKAMID AGATRIGASA GVAIVNGERS EGSY
