ID Q3JGT8_BURP1 Unreviewed; 393 AA.
AC Q3JGT8;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=3-phosphonopyruvate decarboxylase {ECO:0000313|EMBL:ABA52889.1};
DE EC=4.1.1.- {ECO:0000313|EMBL:ABA52889.1};
GN Name=ppd {ECO:0000313|EMBL:ABA52889.1};
GN OrderedLocusNames=BURPS1710b_A2064 {ECO:0000313|EMBL:ABA52889.1};
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA52889.1, ECO:0000313|Proteomes:UP000002700};
RN [1] {ECO:0000313|EMBL:ABA52889.1, ECO:0000313|Proteomes:UP000002700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b {ECO:0000313|EMBL:ABA52889.1,
RC ECO:0000313|Proteomes:UP000002700};
RA Woods D.E., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000125; ABA52889.1; -; Genomic_DNA.
DR RefSeq; WP_004530031.1; NC_007435.1.
DR AlphaFoldDB; Q3JGT8; -.
DR EnsemblBacteria; ABA52889; ABA52889; BURPS1710b_A2064.
DR GeneID; 56531043; -.
DR KEGG; bpm:BURPS1710b_A2064; -.
DR HOGENOM; CLU_042853_0_0_4; -.
DR Proteomes; UP000002700; Chromosome II.
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 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; 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 SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ABA52889.1};
KW Pyruvate {ECO:0000313|EMBL:ABA52889.1}.
FT DOMAIN 239..347
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 393 AA; 41022 MW; 1F0F156BF9EE3B28 CRC64;
MIEAAQFVEA ARARGFDWYA GVPCSYLTPF INYVLQDPAL HYVSAANEGD AVALVAGATL
GGRRGIAMMQ NSGLGNAVSP LTSLTWTFRL PQLLIVTWRG QPGVPDEPQH ALMGPITPAM
LDTMEIPWET FPTQADAIGP ALDRAIAHMD ATGRPYALVM QKGSVAPHAL EHASMPERRA
HAAARATPGA AAPSAWPTRH DALARIVART PADSTVVLAS TGFCGRELYA LDDRPNQLYM
VGSMGCVTPL ALGLALARPD LTVVALDGDG AALMRMGAFA TLGAYGPPNL VHLLLDNGAH
ESTGGQATVS QYVSFAGIAA ACGYATAIEG DDLGVLDAAL DAARAGEQAV EHGGAHFARL
SIRTGVPDGL PRPTVTPVDV KTRLMRHIGA MPA
//