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Database: UniProt
Entry: B4EBH7_BURCJ
LinkDB: B4EBH7_BURCJ
Original site: B4EBH7_BURCJ 
ID   B4EBH7_BURCJ            Unreviewed;       591 AA.
AC   B4EBH7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:CAR52250.1};
DE            EC=4.1.1.47 {ECO:0000313|EMBL:CAR52250.1};
GN   Name=gcl {ECO:0000313|EMBL:CAR52250.1};
GN   ORFNames=BCAL1949 {ECO:0000313|EMBL:CAR52250.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR52250.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR52250.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AM747720; CAR52250.1; -; Genomic_DNA.
DR   RefSeq; WP_006485953.1; NC_011000.1.
DR   AlphaFoldDB; B4EBH7; -.
DR   GeneID; 56558429; -.
DR   KEGG; bcj:BCAL1949; -.
DR   eggNOG; COG3960; Bacteria.
DR   HOGENOM; CLU_013748_1_3_4; -.
DR   OMA; TLMGWGA; -.
DR   BioCyc; BCEN216591:G1G1V-2143-MONOMER; -.
DR   Proteomes; UP000001035; Chromosome 1.
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:0009436; P:glyoxylate catabolic process; IEA:InterPro.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
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_TPP-bd.
DR   NCBIfam; TIGR01504; glyox_carbo_lig; 1.
DR   PANTHER; PTHR18968:SF14; GLYOXYLATE CARBOLIGASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CAR52250.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   591 AA;  63985 MW;  B606E7CE8241E4BF CRC64;
     MAKMRAVDAA VLVLEKEGIQ TAFGVPGAAI NPFYSAMRKS GGISHVLARH VEGASHMAEG
     FTRAAPGNIG VCIGTSGPAG TDMITGLYSA SADSIPILAI TGQAPRARLY KEDFQAVDIE
     SIAKPVTKWA VTVREPALVP RVFQQAFHLM RSGRPGPVLV DLPIDVQLAE IEFDIDTYEP
     LPVYKPAATR AQIEKALTML NDADKPLIVS GGGVLNAAAE DLLVQFAETV GVPVIPTLMS
     WGAIADDHPL MAGMVGLQTS HRYGNATMLA SDFVLGIGNR WANRHTGSVE VYTKGRKFVH
     VDIEPTQIGR VFGPDLGIVS DAKAALELFV AVAQEWKAAG KLKDRSAWVA DCQERKRTLQ
     RKTHFDNVPV KPQRVYEEMN KVFGRDTCYV STIGLSQIAA AQFLHVFKAR NWINCGQAGP
     LGWTIPAALG VRAADPSRPI VALSGDYDFQ FMIEELAAGA QFKLPYVHVV VNNSYLGLIR
     QAQRAFDMDY CVQLAFDNVN APELNGYGVD HVAVAEGLGC KALRVFKPEE IEPALRQAQT
     LAEEFSVPVV VEVILERVTN ISMGTEIDAI NEFEDLAEKA EHAPTAISML D
//
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