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Database: UniProt
Entry: A0A1G8WPD3_9FIRM
LinkDB: A0A1G8WPD3_9FIRM
Original site: A0A1G8WPD3_9FIRM 
ID   A0A1G8WPD3_9FIRM        Unreviewed;       227 AA.
AC   A0A1G8WPD3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE            Short=DERA {ECO:0000256|HAMAP-Rule:MF_00114};
DE            EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00114};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE            Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
GN   Name=deoC {ECO:0000256|HAMAP-Rule:MF_00114};
GN   ORFNames=SAMN04487760_11624 {ECO:0000313|EMBL:SDJ79927.1};
OS   Lachnospiraceae bacterium G41.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1200749 {ECO:0000313|EMBL:SDJ79927.1, ECO:0000313|Proteomes:UP000199016};
RN   [1] {ECO:0000313|EMBL:SDJ79927.1, ECO:0000313|Proteomes:UP000199016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G41 {ECO:0000313|EMBL:SDJ79927.1,
RC   ECO:0000313|Proteomes:UP000199016};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|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:0000256|ARBA:ARBA00000764, ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-
CC       Rule:MF_00114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00114}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00010936, ECO:0000256|HAMAP-
CC       Rule:MF_00114}.
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DR   EMBL; FNEU01000016; SDJ79927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8WPD3; -.
DR   STRING; 1200749.SAMN04487760_11624; -.
DR   OrthoDB; 9778711at2; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000199016; Unassembled WGS sequence.
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_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   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889:SF1; 2-DEOXY-D-RIBOSE 5-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00114};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00114};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199016};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT   ACT_SITE        99
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        161
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        190
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   227 AA;  24871 MW;  D33298104D7F26EB CRC64;
     MDIKEILSKV DHTLLAVDAT WDQIKTICDD AVKYQTASVC IPAVYVKRAS EYIKEEAAEQ
     HLPNVKVCTV IGFPNGYSTT AVKCMEAREA IENGADEIDM VIHVGALKDK KYDDILKDIK
     SVKTACEDKV LKVIIETCLL TDEEKIKMCE IVNESGADYI KTSTGFSKGG ATKEDVALFA
     KYVKAPVKIK AAGGIASLED AEDFIKLGAD RLGTSRIVKI VKSMEEK
//
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