ID   PPD_STRHY               Reviewed;         401 AA.
AC   Q54271;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Phosphonopyruvate decarboxylase;
DE            EC=4.1.1.82;
GN   Name=bcpC;
OS   Streptomyces hygroscopicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX   PubMed=10786631; DOI=10.1016/s0167-4781(99)00249-3;
RA   Nakashita H., Kozuka K., Hidaka T., Hara O., Seto H.;
RT   "Identification and expression of the gene encoding phosphonopyruvate
RT   decarboxylase of Streptomyces hygroscopicus.";
RL   Biochim. Biophys. Acta 1490:159-162(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphonopyruvate + H(+) = CO2 + phosphonoacetaldehyde;
CC         Xref=Rhea:RHEA:20768, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:58383, ChEBI:CHEBI:71402; EC=4.1.1.82;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; bialaphos biosynthesis.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; D37809; BAA07055.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q54271; -.
DR   SMR; Q54271; -.
DR   KEGG; ag:BAA07055; -.
DR   BRENDA; 4.1.1.82; 6043.
DR   UniPathway; UPA00197; -.
DR   GO; GO:0033980; F:phosphonopyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR017684; Phosphono-pyrv_decarboxylase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR03297; Ppyr-DeCO2ase; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Decarboxylase; Lyase; Thiamine pyrophosphate.
FT   CHAIN           1..401
FT                   /note="Phosphonopyruvate decarboxylase"
FT                   /id="PRO_0000090841"
FT   REGION          382..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  41629 MW;  E83FF3C135758463 CRC64;
     MISASDMLAG LTGLGVTTVA GVPCSYLTPL INRVISDRAT RYLTVTQEGE AAAVAAGSWL
     GGGLGCAITQ NSGLGNMTNP LTSLLHPARI PAVVISTWRG RPGEKDEPQH HLMGRVTGDL
     FGLCDMEWSL LPDTPDALRG EFDVCREALA RRELPYGFLL PQGVIADEPL DEEAPRSRAG
     RLVRHARTGP SDAAPTRVAA LERLLAELPP AAAVVSTTGK TSRELYTLDD RDQHFYMVGA
     MGSAATVGLG VALHTPRPVV VVDGDGSALM RLGSLATVAA HAPGNLVHLI LDNGVHDSTG
     GQRTLSSAVD LPAVAAACGY RAVHACGSLD DLTTALAGAL ATDGPTLIHL PIRPGSLAAL
     GRPKVQPHEV ARRFREFATE PWPASAVGSG TRAAAGSAGD R