(data stored in SCRATCH zone)

SWISSPROT: C8U2I9_ECO10

ID   C8U2I9_ECO10            Unreviewed;       593 AA.
AC   C8U2I9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:BAI29347.1};
GN   Name=gcl {ECO:0000313|EMBL:BAI29347.1};
GN   OrderedLocusNames=ECO103_0480 {ECO:0000313|EMBL:BAI29347.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29347.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29347.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AP010958; BAI29347.1; -; Genomic_DNA.
DR   RefSeq; WP_001298998.1; NC_013353.1.
DR   EnsemblBacteria; BAI29347; BAI29347; ECO103_0480.
DR   KEGG; eoh:ECO103_0480; -.
DR   HOGENOM; HOG000258449; -.
DR   KO; K01608; -.
DR   OMA; WGAIPDD; -.
DR   BioCyc; ECOL585395:ECO103_RS02510-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U2I9.
DR   SWISS-2DPAGE; C8U2I9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Ligase {ECO:0000313|EMBL:BAI29347.1};
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;  64760 MW;  F4B1C0DC6B00ECB7 CRC64;
     MAKMRAVDAA MYVLEKEGIT TAFGVPGAAI NPFYSAMRKH GGIRHILARH VEGASHMAEG
     YTRATAGNIG VCLGTSGPAG TDMITALYSA SADSIPILCI TGQAPRARLH KEDFQAVDIE
     AIAKPVSKMA VTVREAALVP RVLQQAFHLM RSGRPGPVLV DLPFDVQVAE IEFDPDMYEP
     LPVYKPAASR MQIEKAVEML IQAKRPVIVA GGGVINADAA ALLQQFAELT SVPVIPTLMG
     WGCIPDDHEL MAGMVGLQTA HRYGNATLLA SDMVFGIGNR FANRHTGSVE KYTEGRKIVH
     IDIEPTQIGR VLCPDLGIVS DAKAALTLLV EVAQEMQKAG RLPCRKEWVA ECQQRKRTLL
     RKTHFDNVPV KPQRVYEEMN KAFGRDVCYV TTIGLSQIAA AQMLHVFKDR HWINCGQAGP
     LGWTIPAALG VCAADPERKV VAISGDFDFQ FLIEELAVGA QFNIPYIHVL VNNAYLGLIR
     QSQRAFDMDY CVQLAFENIN SSEVNGYGVD HVKVAEGLGC KAIRVFKPED IAPAFEQAKA
     LMAQYRVPVV VEVILERVTN ISMGSELDNV MEFEDIADNA ADAPTETCFM HYE
//

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