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Database: UniProt
Entry: A0A1H7TUE3_9BURK
LinkDB: A0A1H7TUE3_9BURK
Original site: A0A1H7TUE3_9BURK 
ID   A0A1H7TUE3_9BURK        Unreviewed;       399 AA.
AC   A0A1H7TUE3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:SEL88185.1};
GN   ORFNames=SAMN05192542_11693 {ECO:0000313|EMBL:SEL88185.1};
OS   Paraburkholderia caballeronis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=416943 {ECO:0000313|EMBL:SEL88185.1, ECO:0000313|Proteomes:UP000199120};
RN   [1] {ECO:0000313|Proteomes:UP000199120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOAJ01000016; SEL88185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7TUE3; -.
DR   STRING; 416943.SAMN05445871_4718; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000199120; Unassembled WGS sequence.
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:SEL88185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199120}.
FT   DOMAIN          6..112
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          242..348
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   399 AA;  41901 MW;  641252A323C71667 CRC64;
     MIDASQFVEA ARARGFDWYA GVPCSYLTPF INYVLQDPSL HYVSAANEGD AVALTAGIAL
     AGKRGITMMQ NSGLGNAVSP LTSLTWTFRL PQLLIVTWRG QPGVSDEPQH ALMGPVTPQM
     LDTMEIPWET FPTEADAIGP ALDRALAHMD STGRPYALVM QKGSVAPYEL KDGAAPARHA
     HVAAQTRFGG GVGVEANELP SRRDALERVI AATPADSTVV LASTGFCGRE LYALDDRANQ
     LYMVGSMGCV TPFALGFALA RPDLNVVALD GDGAALMRMG AFATLGAYGP SNLTHVLLDN
     GAHDSTGGQA TVSPQVSFAG VAAACGYADA IESDDLAVLD DVLAAARERR AGASGFAGTR
     FVRIAIRRGT PDGLPRPTIT PPDVKTRLMR HIGAEQGAH
//
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