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Database: UniProt
Entry: E1TEQ8_BURSG
LinkDB: E1TEQ8_BURSG
Original site: E1TEQ8_BURSG 
ID   E1TEQ8_BURSG            Unreviewed;       387 AA.
AC   E1TEQ8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:ADN60213.1};
GN   OrderedLocusNames=BC1003_4279 {ECO:0000313|EMBL:ADN60213.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN60213.1};
RN   [1] {ECO:0000313|EMBL:ADN60213.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN60213.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002218; ADN60213.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1TEQ8; -.
DR   STRING; 640512.BC1003_4279; -.
DR   KEGG; bgf:BC1003_4279; -.
DR   eggNOG; COG0028; Bacteria.
DR   eggNOG; COG4032; Bacteria.
DR   HOGENOM; CLU_042853_0_0_4; -.
DR   OMA; YMLGSYT; -.
DR   OrthoDB; 9785953at2; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0033980; F:phosphonopyruvate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:InterPro.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR017684; Phosphono-pyrv_decarboxylase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR03297; Ppyr-DeCO2ase; 1.
DR   PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:ADN60213.1}.
FT   DOMAIN          5..114
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          240..346
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   387 AA;  40741 MW;  BE1C52AF4A095158 CRC64;
     MIEAAQFVEA ARERGFDWYA GVPCSYLTPF INYVLQDESL HYVSAANEGD AVALIAGVAL
     GARNGRRGIT MMQNSGLGNA VSPLTSLTWT FRLPQLLIVT WRGQPGVADE PQHALMGPVT
     PAMLDTMEIP WETFPTQAEA IGPALDRAIA HMDQTGRPYA LVMQKGSVAP YELKAGPAGA
     RRVPAAARSQ FGSVAASDLA SRHDALKKVI AHTPLESTVV LASTGFCGRE LYAIDDRPNQ
     LYMVGSMGCV TPFALGLALA RPDLHVVALD GDGAALMRMG AFATLGAYGP SNLTHVLLDN
     GAHDSTGGQA TVSPQVSFAG VAAACGYASA VESDDPAVLD QLFESAPLEG PRFARLAIRR
     GTPDGLPRPT ITPPDVKARL MRHIGAG
//
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