ID A6BLT1_9GAMM Unreviewed; 257 AA.
AC A6BLT1;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00592};
DE Short=DERA {ECO:0000256|HAMAP-Rule:MF_00592};
DE EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00592};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00592};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00592};
DE Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00592};
GN Name=deoC {ECO:0000256|HAMAP-Rule:MF_00592,
GN ECO:0000313|EMBL:BAF64742.1};
OS Shewanella livingstonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=150120 {ECO:0000313|EMBL:BAF64742.1};
RN [1] {ECO:0000313|EMBL:BAF64742.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ac10 {ECO:0000313|EMBL:BAF64742.1};
RX PubMed=17526788; DOI=10.1128/AEM.00824-07;
RA Miyake R., Kawamoto J., Wei Y.L., Kitagawa M., Kato I., Kurihara T.,
RA Esaki N.;
RT "Construction of a low-temperature protein expression system using a cold-
RT adapted bacterium, Shewanella sp. strain Ac10, as the host.";
RL Appl. Environ. Microbiol. 73:4849-4856(2007).
RN [2] {ECO:0000313|EMBL:BAF64742.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ac10 {ECO:0000313|EMBL:BAF64742.1};
RX PubMed=17618403; DOI=10.1007/s00792-007-0098-6;
RA Kawamoto J., Kurihara T., Kitagawa M., Kato I., Esaki N.;
RT "Proteomic studies of an Antarctic cold-adapted bacterium, Shewanella
RT livingstonensis Ac10, for global identification of cold-inducible
RT proteins.";
RL Extremophiles 11:819-826(2007).
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:0000256|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:0000256|ARBA:ARBA00000764, ECO:0000256|HAMAP-
CC 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.
CC {ECO:0000256|ARBA:ARBA00004816, ECO:0000256|HAMAP-Rule:MF_00592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00592}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009473, ECO:0000256|HAMAP-
CC Rule:MF_00592}.
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DR EMBL; AB284104; BAF64742.1; -; Genomic_DNA.
DR AlphaFoldDB; A6BLT1; -.
DR UniPathway; UPA00002; UER00468.
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; Aldolase class I; 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 NCBIfam; TIGR00126; deoC; 1.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00592};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00592};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00592}.
FT ACT_SITE 102
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00592"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00592"
FT ACT_SITE 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00592"
SQ SEQUENCE 257 AA; 27655 MW; 63CAC33501EE64E8 CRC64;
MTDLKKAAQR GIELMDLTTL NDDDTDQKVI DLCHKAKSPA GNTAAICIYP RFIPIARKTL
NELDCEDIKI ATVTNFPHGN DDIAIAVLET RAAVAYGADE VDVVFPYRAL MDGNETVGFE
MVKACKEECG DDAILKVIIE SGVLKDPALI RKASELAIDA GADFIKTSTG KVPVNATLEA
AEIMLTVISE KNRNVGFKPA GGVRDAAQTA EFLDLAARIL GDDWVTPQTF RFGASSLLNS
LLHTLDLVDA PKPTSGY
//
