ID A0A085AAS3_9ENTR Unreviewed; 256 AA.
AC A0A085AAS3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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,
GN ECO:0000313|EMBL:KFC07318.1};
GN ORFNames=GTGU_01908 {ECO:0000313|EMBL:KFC07318.1};
OS Trabulsiella guamensis ATCC 49490.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC07318.1, ECO:0000313|Proteomes:UP000028630};
RN [1] {ECO:0000313|EMBL:KFC07318.1, ECO:0000313|Proteomes:UP000028630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC07318.1,
RC ECO:0000313|Proteomes:UP000028630};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFC07318.1}.
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DR EMBL; JMTB01000063; KFC07318.1; -; Genomic_DNA.
DR RefSeq; WP_038156146.1; NZ_JMTB01000063.1.
DR AlphaFoldDB; A0A085AAS3; -.
DR eggNOG; COG3836; Bacteria.
DR OrthoDB; 86160at2; -.
DR UniPathway; UPA00565; UER00630.
DR Proteomes; UP000028630; 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:KFC07318.1};
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; 27453 MW; CA8D7FE6B5985EFA CRC64;
MNNDIFPNKF KAALAAQQIQ IGCWSALANP ISTEVLGLAG FDWLVLDGEH APNDVTTFIP
QLMALKGSTS APVVRVPTNE PVIIKRLLDI GFYNFLIPFV ETEEEAVRAV ASTRYPPEGI
RGVSVSHRAN MFGTVADYFA QSNRNITVLV QIESQTGVDN VDAIAATPGV DGIFVGPSDL
AAALGHLGNA SHPDVQKCIQ HIFARAKAHE KPSGILAPVD ADARRYLEWG ATFVAVGSDL
GVFRSATQKL ADAFKK
//
