ID W1F384_ECOLX Unreviewed; 256 AA.
AC W1F384;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=5-keto-4-deoxy-D-glucarate aldolase {ECO:0000256|HAMAP-Rule:MF_01291};
DE Short=KDGluc aldolase {ECO:0000256|HAMAP-Rule:MF_01291};
DE Short=KDGlucA {ECO:0000256|HAMAP-Rule:MF_01291};
DE EC=4.1.2.20 {ECO:0000256|HAMAP-Rule:MF_01291};
DE AltName: Full=2-dehydro-3-deoxy-D-glucarate aldolase {ECO:0000256|HAMAP-Rule:MF_01291};
DE AltName: Full=2-keto-3-deoxy-D-glucarate aldolase {ECO:0000256|HAMAP-Rule:MF_01291};
DE AltName: Full=5-dehydro-4-deoxy-D-glucarate aldolase {ECO:0000256|HAMAP-Rule:MF_01291};
DE AltName: Full=Alpha-keto-beta-deoxy-D-glucarate aldolase {ECO:0000256|HAMAP-Rule:MF_01291};
GN Name=garL {ECO:0000256|HAMAP-Rule:MF_01291};
OS Escherichia coli ISC7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1432555 {ECO:0000313|EMBL:CDL28849.1, ECO:0000313|Proteomes:UP000019199};
RN [1] {ECO:0000313|EMBL:CDL28849.1, ECO:0000313|Proteomes:UP000019199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISC7 {ECO:0000313|EMBL:CDL28849.1,
RC ECO:0000313|Proteomes:UP000019199};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of both 5-keto-
CC 4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and
CC tartronic semialdehyde. {ECO:0000256|HAMAP-Rule:MF_01291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate +
CC pyruvate; Xref=Rhea:RHEA:10268, ChEBI:CHEBI:15361, ChEBI:CHEBI:57978,
CC ChEBI:CHEBI:58098; EC=4.1.2.20; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01291};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydro-4-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate +
CC pyruvate; Xref=Rhea:RHEA:27726, ChEBI:CHEBI:15361, ChEBI:CHEBI:42819,
CC ChEBI:CHEBI:57978; Evidence={ECO:0000256|HAMAP-Rule:MF_01291};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01291};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01291};
CC -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation; D-
CC glycerate from galactarate: step 2/3. {ECO:0000256|HAMAP-
CC Rule:MF_01291}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01291}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01291}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL28849.1}.
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DR EMBL; CBWN010000138; CDL28849.1; -; Genomic_DNA.
DR AlphaFoldDB; W1F384; -.
DR SMR; W1F384; -.
DR UniPathway; UPA00565; UER00630.
DR Proteomes; UP000019199; Unassembled WGS sequence.
DR GO; GO:0008672; F:2-dehydro-3-deoxyglucarate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046392; P:galactarate catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR HAMAP; MF_01291; KDGluc_aldolase; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR017648; GarL.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR03239; GarL; 1.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF4; 5-KETO-4-DEOXY-D-GLUCARATE ALDOLASE; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01291, ECO:0000313|EMBL:CDL28849.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01291};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01291}.
FT DOMAIN 20..245
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
FT SITE 75
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
FT SITE 89
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01291"
SQ SEQUENCE 256 AA; 27399 MW; A363593FFB171401 CRC64;
MNNDVFPNKF KAALAAKQVQ IGCWSALSNP ISTEVLGLAG FDWLVLDGEH APNDISTFIP
QLMALKGSAS APVVRVPTNE PVIIKRLLDI GFYNFLIPFV ETKEEAEQAV ASTRYPPEGI
RGVSVSHRAN MFGTVADYFA QSNKNITILV QIESQQGVDN VDAIAATEGV DGIFVGPSDL
AAALGHLGNA SHPDVQKAIQ HIFNRASAHG KPSGILAPVE ADARRYLEWG ATFVAVGSDL
GVFRSATQKL ADTFKK
//
