ID   PPD_STRVT               Reviewed;         397 AA.
AC   O86938; D9XF41; Q5IW37;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Phosphonopyruvate decarboxylase;
DE            EC=4.1.1.82;
GN   Name=ppd; ORFNames=SSQG_01038 {ECO:0000312|EMBL:EFL30520.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=591159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=9673017; DOI=10.1111/j.1574-6968.1998.tb13039.x;
RA   Schwartz D., Recktenwald J., Pelzer S., Wohlleben W.;
RT   "Isolation and characterization of the PEP-phosphomutase and the
RT   phosphonopyruvate decarboxylase genes from the phosphinothricin tripeptide
RT   producer Streptomyces viridochromogenes Tu494.";
RL   FEMS Microbiol. Lett. 163:149-157(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=15616300; DOI=10.1128/aac.49.1.230-240.2005;
RA   Blodgett J.A., Zhang J.K., Metcalf W.W.;
RT   "Molecular cloning, sequence analysis, and heterologous expression of the
RT   phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces
RT   viridochromogenes DSM 40736.";
RL   Antimicrob. Agents Chemother. 49:230-240(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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: Antibiotic biosynthesis; phosphinothricin biosynthesis.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; X65195; CAJ14045.1; -; Genomic_DNA.
DR   EMBL; AY632421; AAU00072.1; -; Genomic_DNA.
DR   EMBL; GG657757; EFL30520.1; -; Genomic_DNA.
DR   RefSeq; WP_003988635.1; NZ_GG657757.1.
DR   AlphaFoldDB; O86938; -.
DR   SMR; O86938; -.
DR   STRING; 591159.ACEZ01000045_gene2947; -.
DR   PRIDE; O86938; -.
DR   EnsemblBacteria; EFL30520; EFL30520; SSQG_01038.
DR   eggNOG; COG0028; Bacteria.
DR   eggNOG; COG4032; Bacteria.
DR   HOGENOM; CLU_042853_0_0_11; -.
DR   OrthoDB; 1219810at2; -.
DR   BioCyc; MetaCyc:MON-15035; -.
DR   BRENDA; 4.1.1.82; 6116.
DR   UniPathway; UPA00168; -.
DR   Proteomes; UP000004184; Unassembled WGS sequence.
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; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..397
FT                   /note="Phosphonopyruvate decarboxylase"
FT                   /id="PRO_0000090842"
SQ   SEQUENCE   397 AA;  41054 MW;  178CC70C702FE398 CRC64;
     MIGAADLVAG LTGLGVTTVA GVPCSYLTPL INRVISDPAT RYLTVTQEGE AAAVAAGAWL
     GGGLGCAITQ NSGLGNMTNP LTSLLHPARI PAVVITTWRG RPGEKDEPQH HLMGRITGDL
     LDLCDMEWSL IPDTTDELHT AFAACRASLA HRELPYGFLL PQGVVADEPL NETAPRSATG
     QVVRYARPGR SAARPTRIAA LERLLAELPR DAAVVSTTGK SSRELYTLDD RDQHFYMVGA
     MGSAATVGLG VALHTPRPVV VVDGDGSVLM RLGSLATVGA HAPGNLVHLV LDNGVHDSTG
     GQRTLSSAVD LPAVAAACGY RAVHACTSLD DLSDALATAL ATDGPTLVHL AIRPGSLDGL
     GRPKVTPAEV ARRFRAFVTT PPAGTATPVH AGGVTAR