GARL_SALPA
ID GARL_SALPA Reviewed; 256 AA.
AC Q5PCB8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=SPA3118;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78948.1; -; Genomic_DNA.
DR RefSeq; WP_001057712.1; NC_006511.1.
DR AlphaFoldDB; Q5PCB8; -.
DR SMR; Q5PCB8; -.
DR EnsemblBacteria; AAV78948; AAV78948; SPA3118.
DR KEGG; spt:SPA3118; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; NEGWMVK; -.
DR UniPathway; UPA00565; UER00630.
DR Proteomes; UP000008185; Chromosome.
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_0000353155"
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; 27307 MW; E2626337BDB7A1FC CRC64;
MNNAIFPNKF KAALAAQQVQ IGCWSALASP ITTEVLGLAG FDWLVLDGEH APNDVSTLIP
QLMALKGSAS APVVRVPTNE PVIIKRMLDI GFYNFLIPFV ETQEEAARAV ASTRYPPEGI
RGVSVSHRAN MFGTVPDYFA QSNKNITIIV QIESQLGVDN VDAIAATEGV DGIFVGPSDL
AAALGHLGNA SHPDVQQTIQ HIFARAKAHG KPCGILAPVE ADARRYLEWG ATFVAVGSDL
GAFRASTQKL ADTFKK
