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GARL_ECOUT
ID   GARL_ECOUT              Reviewed;         256 AA.
AC   Q1R6L1;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=UTI89_C3557;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE09003.1; -; Genomic_DNA.
DR   RefSeq; WP_001058227.1; NC_007946.1.
DR   AlphaFoldDB; Q1R6L1; -.
DR   SMR; Q1R6L1; -.
DR   EnsemblBacteria; ABE09003; ABE09003; UTI89_C3557.
DR   GeneID; 66672975; -.
DR   KEGG; eci:UTI89_C3557; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; NEGWMVK; -.
DR   UniPathway; UPA00565; UER00630.
DR   Proteomes; UP000001952; 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_0000353145"
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
 
 
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