ID   GARL_ECOL5              Reviewed;         256 AA.
AC   Q0TCY1;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=5-keto-4-deoxy-D-glucarate aldolase;
DE            Short=KDGluc aldolase;
DE            Short=KDGlucA;
DE            EC=4.1.2.20;
DE   AltName: Full=5-dehydro-4-deoxy-D-glucarate aldolase;
DE   AltName: Full=2-keto-3-deoxy-D-glucarate aldolase;
DE   AltName: Full=2-dehydro-3-deoxy-D-glucarate aldolase;
DE   AltName: Full=Alpha-keto-beta-deoxy-D-glucarate aldolase;
GN   Name=garL; OrderedLocusNames=ECP_3216;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of both 5-
CC       keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to
CC       pyruvate and tartronic semialdehyde (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-dehydro-4-deoxy-D-glucarate = pyruvate +
CC       tartronate semialdehyde.
CC   -!- CATALYTIC ACTIVITY: 2-dehydro-3-deoxy-D-glucarate = pyruvate +
CC       tartronate semialdehyde.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-galactaric acid
CC       degradation; D-glyceric acid from D-galactaric acid: step 2/3.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers (By similarity).
CC   -!- SIMILARITY: Belongs to the hpcH/hpaI aldolase family. KDGluc
CC       aldolase subfamily.
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DR   EMBL; CP000247; ABG71198.1; -; Genomic_DNA.
DR   RefSeq; YP_671099.1; -.
DR   SMR; Q0TCY1; 4-256.
DR   GeneID; 4188537; -.
DR   GenomeReviews; CP000247_GR; ECP_3216.
DR   KEGG; ecp:ECP_3216; -.
DR   HOGENOM; Q0TCY1; -.
DR   OMA; Q0TCY1; QRSNRYG.
DR   BioCyc; ECOL362663:ECP_3216-MON; -.
DR   GO; GO:0008672; F:2-dehydro-3-deoxyglucarate aldolase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   GO; GO:0019582; P:D-galactarate catabolic process; IEA:HAMAP.
DR   GO; GO:0019394; P:glucarate catabolic process; IEA:HAMAP.
DR   HAMAP; MF_01291; -; 1.
DR   InterPro; IPR017648; Dehyd-dGlucarate-aldolase_GarL.
DR   InterPro; IPR005000; HpcH_HpaI.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   ProDom; PD001009; Pyruvate_kinase; 1.
DR   TIGRFAMs; TIGR03239; GarL; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lyase; Magnesium; Metal-binding.
FT   CHAIN         1    256       5-keto-4-deoxy-D-glucarate aldolase.
FT                                /FTId=PRO_0000353150.
FT   ACT_SITE     50     50       Proton acceptor (By similarity).
FT   METAL       153    153       Magnesium (By similarity).
FT   METAL       179    179       Magnesium (By similarity).
FT   BINDING     151    151       Substrate (By similarity).
FT   BINDING     178    178       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     179    179       Substrate (By similarity).
FT   SITE         75     75       Transition state stabilizer (By
FT                                similarity).
FT   SITE         89     89       Increases basicity of active site His (By
FT                                similarity).
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
//