(data stored in ACNUC7421 zone)

SWISSPROT: B7UKI5_ECO27

ID   B7UKI5_ECO27            Unreviewed;       593 AA.
AC   B7UKI5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:CAS07989.1};
GN   Name=gcl {ECO:0000313|EMBL:CAS07989.1};
GN   OrderedLocusNames=E2348C_0441 {ECO:0000313|EMBL:CAS07989.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07989.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07989.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; FM180568; CAS07989.1; -; Genomic_DNA.
DR   RefSeq; WP_001339222.1; NC_011601.1.
DR   EnsemblBacteria; CAS07989; CAS07989; E2348C_0441.
DR   KEGG; ecg:E2348C_0441; -.
DR   HOGENOM; HOG000258449; -.
DR   KO; K01608; -.
DR   OMA; WGAIPDD; -.
DR   BioCyc; ECOL574521:E2348C_RS02315-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009028; F:tartronate-semialdehyde synthase activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR011766; TPP_enzyme-bd_C.
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;
DR   PRODOM; B7UKI5.
DR   SWISS-2DPAGE; B7UKI5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Ligase {ECO:0000313|EMBL:CAS07989.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        4    172       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      193    329       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      393    553       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   593 AA;  64774 MW;  4F31860363D3A85F CRC64;
     MAKMRAVDAA MYVLEKEGIT TAFGVPGAAI NPFYSAMRKH GGIRHILARH VEGASHMAEG
     YTRATAGNIG VCLGTSGPAG TDMITALYSA SADSIPILCI TGQAPRARLH KEDFQAVDIE
     AIAKPVSKMA VTVREAALVP RVLQQAFHLM RSGRPGPVLV DLPFDVQVAE IEFDPDMYEP
     LPVYKPAASR MQIEKAVKML IQAERPVIVA GGGVINADAA ALLQQFAELT SVPVIPTLMG
     WGCIPDDHEL MAGMVGLQTA HRYGNATLLA SDMVFGIGNR FANRHTGSVE KYTEGRKIVH
     IDIEPTQIGR VLCPDLGIVS DAKAALTLLV EVAQEMQKAG RLPCRKEWVA DCQQRKRTLL
     RKTHFDNVPV KPQRVYEEMN KAFGRDVCYV TTIGLSQIAA AQMLHVFKDR HWINCGQAGP
     LGWTIPAALG VCAADPERNV VAISGDFDFQ FLIEELAVGA QFNIPYIHVL VNNAYLGLIR
     QSQRAFDMDY CVQLAFENIN SSEVNGYGVD HVKVAEGLGC KAIRVFKPED IAPAFEQAKI
     LMAQYRVPVV VEVILERVTN ISMGSELDNV MEFEDIADNA ADAPTETCFM HYE
//

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