DEOC_AQUAE
ID DEOC_AQUAE Reviewed; 219 AA.
AC O66540;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
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}; OrderedLocusNames=aq_148;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06495.1; -; Genomic_DNA.
DR PIR; A70314; A70314.
DR RefSeq; NP_213100.1; NC_000918.1.
DR RefSeq; WP_010880038.1; NC_000918.1.
DR PDB; 1MZH; X-ray; 2.00 A; A/B=1-219.
DR PDBsum; 1MZH; -.
DR AlphaFoldDB; O66540; -.
DR SMR; O66540; -.
DR STRING; 224324.aq_148; -.
DR EnsemblBacteria; AAC06495; AAC06495; aq_148.
DR KEGG; aae:aq_148; -.
DR PATRIC; fig|224324.8.peg.124; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_0_2_0; -.
DR InParanoid; O66540; -.
DR OMA; MNACIPP; -.
DR OrthoDB; 1227369at2; -.
DR UniPathway; UPA00002; UER00468.
DR EvolutionaryTrace; O66540; -.
DR Proteomes; UP000000798; 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 3D-structure; Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..219
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057220"
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 150
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 179
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:1MZH"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:1MZH"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1MZH"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:1MZH"
SQ SEQUENCE 219 AA; 24182 MW; 7CFC455A136AB827 CRC64;
MIDVRKYIDN AALKPHLSEK EIEEFVLKSE ELGIYAVCVN PYHVKLASSI AKKVKVCCVI
GFPLGLNKTS VKVKEAVEAV RDGAQELDIV WNLSAFKSEK YDFVVEELKE IFRETPSAVH
KVIVETPYLN EEEIKKAVEI CIEAGADFIK TSTGFAPRGT TLEEVRLIKS SAKGRIKVKA
SGGIRDLETA ISMIEAGADR IGTSSGISIA EEFLKRHLI
