ID C5AFD4_BURGB Unreviewed; 591 AA.
AC C5AFD4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:ACR28541.1};
GN OrderedLocusNames=bglu_1g13920 {ECO:0000313|EMBL:ACR28541.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR28541.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR28541.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR28541.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(2009).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001503; ACR28541.1; -; Genomic_DNA.
DR RefSeq; WP_015875435.1; NC_012724.2.
DR AlphaFoldDB; C5AFD4; -.
DR STRING; 626418.bglu_1g13920; -.
DR GeneID; 58134950; -.
DR KEGG; bgl:bglu_1g13920; -.
DR PATRIC; fig|626418.3.peg.4173; -.
DR eggNOG; COG3960; Bacteria.
DR HOGENOM; CLU_013748_1_3_4; -.
DR Proteomes; UP000002187; 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:ACR28541.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002187};
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; 63903 MW; 8C4C6619B9A090B0 CRC64;
MAKMRAVDAA VLVLEKEGIQ TAFGVPGAAI NPFYSALRKS GAIGHVLARH VEGASHMAEG
YTRAAPGNIG VCIGTSGPAG TDMITGLYSA WADSIPILAI TGQAPRARLY KEDFQAVDIE
SIAKPVTKWA VTVREPALVP RVFQQAFHLM RSGRPGPVLI DLPIDVQLAE IEFDIDTYAP
LPAYKPAATR AQIEAALTML DEAERPLIVS GGGVLNAAAE DLLVEFAELL GVPVIPTLMS
WGAIPDDHPL MAGMVGLQTS HRYGNATLLA SDFVLGIGNR WANRHTGSVE VYTKGRRFVH
VDIEPTQIGR VFGPDLGIVS DAKAALELFV AAAREWKAAG RLKDRGAWVA DCQQRKRTLQ
RKTHFDDVPV KPQRVYEEMN KAFGRNTCYV STIGLSQIAA AQFLHVYQAR NWINCGQAGP
LGWTIPAALG VRAADPGRPI VALSGDYDFQ FMIEELAVGA QFKLPYVHVV VNNAYLGLIR
QAQRAFDMDY CVQLAFENVN APELGSYGVD HVAVAEGLGC KALRVTRPEQ IAPAFEQAKQ
LIAEFGVPVV VEVILERVTH IAMGAELDAV NEFEPLAERP EHAPTAISLL D
//
