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Database: UniProt
Entry: A0A066YUZ4_9ACTN
LinkDB: A0A066YUZ4_9ACTN
Original site: A0A066YUZ4_9ACTN 
ID   A0A066YUZ4_9ACTN        Unreviewed;       376 AA.
AC   A0A066YUZ4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:KDN81921.1};
GN   ORFNames=KCH_63600 {ECO:0000313|EMBL:KDN81921.1};
OS   Kitasatospora cheerisanensis KCTC 2395.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN81921.1, ECO:0000313|Proteomes:UP000027178};
RN   [1] {ECO:0000313|EMBL:KDN81921.1, ECO:0000313|Proteomes:UP000027178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN81921.1,
RC   ECO:0000313|Proteomes:UP000027178};
RA   Nam D.H.;
RT   "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDN81921.1}.
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DR   EMBL; JNBY01000128; KDN81921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066YUZ4; -.
DR   PATRIC; fig|1348663.4.peg.6153; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_042853_0_0_11; -.
DR   Proteomes; UP000027178; 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   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:KDN81921.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027178}.
FT   DOMAIN          13..112
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          230..345
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   376 AA;  39084 MW;  F6526D6948CAFC5F CRC64;
     MSGEQGGGLD PAAVVDAFRT AGLGPYFGVP CSFLGPMISV LQADHPEEYL AAANEGEAVA
     VASGAHLAGR RPVVIMQNSG LGNAVNPLTS LCHTLRIPVL LLVTWRGEPG HPDEPQHRLM
     GALTRDLLTA MGVRHEIFPS DPAELAPALE RARRHMDEEG LPFAFVVPKG ALRPSRPAAA
     APAPAAGLML RAEAIAHIVA EAGPDALLVA TTGKTARELE NDWDRSGNLY VVGSMGCASS
     IGLGVALGAP RRKVVVLDGD GAALMRLEAM ATIGHRAPGN LVHVVLDNEA YESTGGQPTA
     SAGIDFGAIA AACGYRSRSD VRGAEPLRRA VARIDSQPGP HFVRVRIRPG SDPALGRPSL
     TPPEARARFM AEVGAA
//
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