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 24-JAN-2024, entry version 82.
DE RecName: Full=Phosphonopyruvate decarboxylase {ECO:0000303|PubMed:9127192};
DE Short=PnPy decarboxylase {ECO:0000303|PubMed:9127192};
DE EC=4.1.1.82 {ECO:0000269|PubMed:9127192};
GN Name=bcpC {ECO:0000303|PubMed:10786631};
OS Streptomyces hygroscopicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; 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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=E26;
RX PubMed=9127192;
RA Nakashita H., Watanabe K., Hara O., Hidaka T., Seto H.;
RT "Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P
RT bond formation: discovery of phosphonopyruvate decarboxylase which
RT catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate.";
RL J. Antibiot. 50:212-219(1997).
CC -!- FUNCTION: Involved in the biosynthesis of phosphinothricin tripeptide
CC (PTT), also known as bialaphos (BA), a natural-product antibiotic and
CC potent herbicide (PubMed:9127192). Catalyzes the decarboxylation of
CC phosphonopyruvate (PnPy) to generate phosphonoacetaldehyde (PnAA)
CC (PubMed:9127192). {ECO:0000269|PubMed:9127192}.
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 Evidence={ECO:0000269|PubMed:9127192};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20769;
CC Evidence={ECO:0000269|PubMed:9127192};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:9127192};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9127192};
CC -!- PATHWAY: Secondary metabolite biosynthesis; bialaphos biosynthesis.
CC {ECO:0000269|PubMed:9127192, ECO:0000305|PubMed:10786631}.
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:0000287; F:magnesium ion binding; IEA:UniProt.
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 CDD; cd03371; TPP_PpyrDC; 1.
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; 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.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Decarboxylase; Lyase; Magnesium;
KW 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
//
