GARL_ECO8A
ID GARL_ECO8A Reviewed; 256 AA.
AC B7M032;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=5-keto-4-deoxy-D-glucarate aldolase {ECO:0000255|HAMAP-Rule:MF_01291};
DE Short=KDGluc aldolase {ECO:0000255|HAMAP-Rule:MF_01291};
DE Short=KDGlucA {ECO:0000255|HAMAP-Rule:MF_01291};
DE EC=4.1.2.20 {ECO:0000255|HAMAP-Rule:MF_01291};
DE AltName: Full=2-dehydro-3-deoxy-D-glucarate aldolase {ECO:0000255|HAMAP-Rule:MF_01291};
DE AltName: Full=2-keto-3-deoxy-D-glucarate aldolase {ECO:0000255|HAMAP-Rule:MF_01291};
DE AltName: Full=5-dehydro-4-deoxy-D-glucarate aldolase {ECO:0000255|HAMAP-Rule:MF_01291};
DE AltName: Full=Alpha-keto-beta-deoxy-D-glucarate aldolase {ECO:0000255|HAMAP-Rule:MF_01291};
GN Name=garL {ECO:0000255|HAMAP-Rule:MF_01291}; OrderedLocusNames=ECIAI1_3274;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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:0000255|HAMAP-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:0000255|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:0000255|HAMAP-
CC Rule:MF_01291};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01291};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01291};
CC -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation; D-
CC glycerate from galactarate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_01291}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_01291}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01291}.
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DR EMBL; CU928160; CAR00088.1; -; Genomic_DNA.
DR RefSeq; WP_001058227.1; NC_011741.1.
DR AlphaFoldDB; B7M032; -.
DR SMR; B7M032; -.
DR GeneID; 66672975; -.
DR KEGG; ecr:ECIAI1_3274; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; NEGWMVK; -.
DR UniPathway; UPA00565; UER00630.
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; -; 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 Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR03239; GarL; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..256
FT /note="5-keto-4-deoxy-D-glucarate aldolase"
FT /id="PRO_1000140407"
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01291"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01291"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01291"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01291"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01291"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01291"
FT SITE 75
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01291"
FT SITE 89
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000255|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
