ID   GCL_ECO57               Reviewed;         593 AA.
AC   P0AEP8; P30146; P77126;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Glyoxylate carboligase;
DE            EC=4.1.1.47;
DE   AltName: Full=Tartronate-semialdehyde synthase;
GN   Name=gcl; OrderedLocusNames=Z0661, ECs0568;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the condensation of two molecules of glyoxylate to
CC       give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glyoxylate + H(+) = 2-hydroxy-3-oxopropanoate + CO2;
CC         Xref=Rhea:RHEA:10136, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57978; EC=4.1.1.47;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Organic acid metabolism; glycolate degradation; 3-phospho-D-
CC       glycerate from glycolate: step 2/4.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG54863.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33991.1; -; Genomic_DNA.
DR   PIR; C85550; C85550.
DR   PIR; H90699; H90699.
DR   RefSeq; NP_308595.1; NC_002695.1.
DR   RefSeq; WP_001096881.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AEP8; -.
DR   SMR; P0AEP8; -.
DR   STRING; 155864.EDL933_0592; -.
DR   EnsemblBacteria; AAG54863; AAG54863; Z0661.
DR   EnsemblBacteria; BAB33991; BAB33991; ECs_0568.
DR   GeneID; 66671197; -.
DR   GeneID; 915770; -.
DR   KEGG; ece:Z0661; -.
DR   KEGG; ecs:ECs_0568; -.
DR   PATRIC; fig|386585.9.peg.676; -.
DR   eggNOG; COG3960; Bacteria.
DR   HOGENOM; CLU_013748_1_2_6; -.
DR   OMA; TLMGWGA; -.
DR   UniPathway; UPA00864; UER00831.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009028; F:tartronate-semialdehyde synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0046296; P:glycolate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009436; P:glyoxylate catabolic process; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR006397; Glyox_carbo_lig.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 1.
DR   PANTHER; PTHR18968:SF14; PTHR18968:SF14; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR01504; glyox_carbo_lig; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Reference proteome; Thiamine pyrophosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..593
FT                   /note="Glyoxylate carboligase"
FT                   /id="PRO_0000090833"
SQ   SEQUENCE   593 AA;  64732 MW;  EF35ECC43B7C62E7 CRC64;
     MAKMRAVDAA MYVLEKEGIT TAFGVPGAAI NPFYSAMRKH GGIRHILARH VEGASHMAEG
     YTRATAGNIG VCLGTSGPAG TDMITALYSA SADSIPILCI TGQAPRARLH KEDFQAVDIE
     AIAKPVSKMA VTVREAALVP RVLQQAFHLM RSGRPGPVLV DLPFDVQVAE IEFDPDMYEP
     LPVYKPAASR MQIEKAVEML IQAERPVIVA GGGVINADAA ALLQQFAELT SVPVIPTLMG
     WGCIPDDHEL MAGMVGLQTA HRYGNATLLA SDMVFGIGNR FANRHTGSVE KYTEGRKIVH
     IDIEPTQIGR VLCPDLGIVS DAKAALTLLV EVAQEMQKAG RLPCRKEWVA DCQQRKRTLL
     RKTHFDNVPV KPQRVYEEMN KAFGRDVCYV TTIGLSQIAA AQMLHVFKDR HWINCGQAGP
     LGWTIPAALG VCAADPKRNV VAISGDFDFQ FLIEELAVGA QFNIPYIHVL VNNAYLGLIR
     QSQRAFDMDY CVQLAFENIN SSEVNGYGVD HVKVAEGLGC KAIRVFKPED IAPAFEQAKA
     LMAQYRVPVV VEVILERVTN ISMGSELDNV MEFEDIADNA ADAPTETCFM HYE