ID   Q0BEQ2_BURCM            Unreviewed;       591 AA.
AC   Q0BEQ2;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:ABI87371.1};
GN   OrderedLocusNames=Bamb_1815 {ECO:0000313|EMBL:ABI87371.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI87371.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000440; ABI87371.1; -; Genomic_DNA.
DR   RefSeq; WP_011657072.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BEQ2; -.
DR   GeneID; 69544018; -.
DR   KEGG; bam:Bamb_1815; -.
DR   PATRIC; fig|339670.21.peg.3144; -.
DR   eggNOG; COG3960; Bacteria.
DR   Proteomes; UP000000662; Chromosome 1.
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   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   Ligase {ECO:0000313|EMBL:ABI87371.1};
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;  63862 MW;  28045EE7BB75ADBD CRC64;
     MAKMRAVDAA VLVLEKEGIQ TAFGVPGAAI NPFYSAMRKS GGISHVLARH VEGASHMAEG
     FTRAAPGNIG VCIGTSGPAG TDMITGLYSA SADSIPILAI TGQAPRARLY KEDFQAVDIE
     SIAKPVTKWA VTVREPALVP RVFQQAFHLM RSGRPGPVLV DLPIDVQLAE IEFDIDTYEP
     LPVYKPAASR AQIEKALAML NDADKPLIVS GGGVLNAAAE DLLVQFAETI GVPVIPTLMS
     WGAIPDDHPL MAGMVGLQTS HRYGNATMLA SDFVLGIGNR WANRHTGSVE VYTKGRKFVH
     VDIEPTQIGR VFGPDLGIVS DAKAALELFV AVAQEWKAAG KLKDRSAWVS ECQARKRTLQ
     RKTHFDNVPV KPQRVYEEMN KVFGRDTCYV STIGLSQIAA AQFLHVFKAR NWINCGQAGP
     LGWTIPAALG VRAADPTRPI VALSGDYDFQ FMIEELAAGA QFKLPYVHVV VNNSYLGLIR
     QAQRAFDMDY CVQLAFDNVN APELNGYGVD HVAVAEGLGC KALRVSKPEE IEPALKQAQA
     LAQEFSVPVV VEVILERVTN ISMGTEIDAI NEFEELAEKA EHAPTAISML D
//