GCL_ECOLI
ID GCL_ECOLI Reviewed; 593 AA.
AC P0AEP7; P30146; P77126; Q2MBS1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glyoxylate carboligase;
DE EC=4.1.1.47;
DE AltName: Full=Tartronate-semialdehyde synthase;
GN Name=gcl; OrderedLocusNames=b0507, JW0495;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31.
RC STRAIN=K12;
RX PubMed=8440684; DOI=10.1016/s0021-9258(18)53559-6;
RA Chang Y.-Y., Wang A.-Y., Cronan J.E. Jr.;
RT "Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia
RT coli glyoxylate carboligase. An enzyme of the acetohydroxy acid synthase-
RT pyruvate oxidase family.";
RL J. Biol. Chem. 268:3911-3919(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Catalyzes the condensation of two molecules of glyoxylate to
CC give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
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.
CC -!- INDUCTION: By glyoxylate.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40260.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L03845; AAA23864.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40260.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73609.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76285.1; -; Genomic_DNA.
DR PIR; JT0742; JT0742.
DR RefSeq; NP_415040.1; NC_000913.3.
DR RefSeq; WP_001096881.1; NZ_STEB01000007.1.
DR PDB; 2PAN; X-ray; 2.70 A; A/B/C/D/E/F=1-593.
DR PDBsum; 2PAN; -.
DR AlphaFoldDB; P0AEP7; -.
DR SMR; P0AEP7; -.
DR BioGRID; 4263336; 2.
DR DIP; DIP-48112N; -.
DR IntAct; P0AEP7; 6.
DR STRING; 511145.b0507; -.
DR PaxDb; P0AEP7; -.
DR PRIDE; P0AEP7; -.
DR EnsemblBacteria; AAC73609; AAC73609; b0507.
DR EnsemblBacteria; BAE76285; BAE76285; BAE76285.
DR GeneID; 66671197; -.
DR GeneID; 945394; -.
DR KEGG; ecj:JW0495; -.
DR KEGG; eco:b0507; -.
DR PATRIC; fig|1411691.4.peg.1770; -.
DR EchoBASE; EB1542; -.
DR eggNOG; COG3960; Bacteria.
DR HOGENOM; CLU_013748_1_2_6; -.
DR InParanoid; P0AEP7; -.
DR OMA; TLMGWGA; -.
DR PhylomeDB; P0AEP7; -.
DR BioCyc; EcoCyc:GLYOCARBOLIG-MON; -.
DR BioCyc; MetaCyc:GLYOCARBOLIG-MON; -.
DR BRENDA; 4.1.1.47; 2165.
DR UniPathway; UPA00864; UER00831.
DR EvolutionaryTrace; P0AEP7; -.
DR PRO; PR:P0AEP7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009028; F:tartronate-semialdehyde synthase activity; IDA:EcoCyc.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc.
DR GO; GO:0046296; P:glycolate catabolic process; IMP:EcoCyc.
DR GO; GO:0009436; P:glyoxylate catabolic process; IMP:EcoCyc.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Magnesium;
KW Reference proteome; Thiamine pyrophosphate.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8440684"
FT CHAIN 2..593
FT /note="Glyoxylate carboligase"
FT /id="PRO_0000090832"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2PAN"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2PAN"
FT TURN 238..242
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 322..338
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:2PAN"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 446..451
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 456..461
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 511..517
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 531..545
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 549..555
FT /evidence="ECO:0007829|PDB:2PAN"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:2PAN"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:2PAN"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:2PAN"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:2PAN"
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
