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
//