ID B4E9J5_BURCJ Unreviewed; 534 AA.
AC B4E9J5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:CAR53096.1};
GN ORFNames=BCAL2796 {ECO:0000313|EMBL:CAR53096.1};
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:CAR53096.1, ECO:0000313|Proteomes:UP000001035};
RN [1] {ECO:0000313|EMBL:CAR53096.1, 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; CAR53096.1; -; Genomic_DNA.
DR RefSeq; WP_012492843.1; NC_011000.1.
DR AlphaFoldDB; B4E9J5; -.
DR KEGG; bcj:BCAL2796; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_4; -.
DR BioCyc; BCEN216591:G1G1V-3097-MONOMER; -.
DR Proteomes; UP000001035; Chromosome 1.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF133; BENZOYLFORMATE DECARBOXYLASE; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 534 AA; 56883 MW; 375A781A0C7DC544 CRC64;
MSGHPPPSAS ITVRDAVVDL LRQFGIDRVF GNPGSTELPM FRDFPDDFRY VLGLHEAVVV
GMADGHAQAT GNAAVVNLHS AAGVGNAMGN LFTAFKNRTP LIVTAGQQAR AILPFDPFLG
ATQAAELPKP YVKWSIEPAR AQDVPAAIAR AYRIAMQEPR GPVFVSIPVD DWDQPAERLP
RRDVSSIVRP DPDALARLGD ALDAARRPAF VVGAAVDRAG AWDDVVRLAE RHRARVYVAP
MSGRCSFPED HPLFAGFLPA IREKIIARLD GHDLVFAFGA PAFTYHIEGF GPHVPPGATL
VQLVDDPGVA AWTPSGDAVV GNLRLAARDL LARPAPPERP MPAARAPRVR VDAPAAGERM
SVAFALQTLA DVRDASDIVV EEAPSARPVM QEHLPFTRSG TFYTMDSGGL GYGMPAAVGV
ALAQPGRRVI GLIGDGSSLY SIQALWSAAQ LKLPITFVIL NNRRYAALQD FAPVFGFGPG
DPVQGTELPD LDFVALAQGM GCRGVRVAEA AKLRDTLTDA LRAATPVVVE VEIA
//