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Database: UniProt
Entry: A0A1H2TWA8_9PSEU
LinkDB: A0A1H2TWA8_9PSEU
Original site: A0A1H2TWA8_9PSEU 
ID   A0A1H2TWA8_9PSEU        Unreviewed;       375 AA.
AC   A0A1H2TWA8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:SDW47998.1};
GN   ORFNames=SAMN05421504_101702 {ECO:0000313|EMBL:SDW47998.1};
OS   Amycolatopsis xylanica.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=589385 {ECO:0000313|EMBL:SDW47998.1, ECO:0000313|Proteomes:UP000199515};
RN   [1] {ECO:0000313|EMBL:SDW47998.1, ECO:0000313|Proteomes:UP000199515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 202699 {ECO:0000313|EMBL:SDW47998.1,
RC   ECO:0000313|Proteomes:UP000199515};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNON01000001; SDW47998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2TWA8; -.
DR   STRING; 589385.SAMN05421504_101702; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000199515; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 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   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:SDW47998.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199515}.
FT   DOMAIN          16..117
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"
FT   REGION          349..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  38852 MW;  A3251E005A4E7381 CRC64;
     MTSATLRAPA EPLAAVAVAD ALLGAGFGPF YGVPCSFLGP LIQVLQDQHP GLYQAAGNEG
     EAVALAAGAR LAGRLPVVIL QNSGLGNGVN PLTSLCHTLR IPVLLLITWR GRPGHPDEPQ
     HELMGRITPD LLAAMEIRSE LFPANLADLP AALSTSAEHL KTGKSFAFIV PKGTLAPLPA
     EPRADDGLAL RAEAIAATVQ ASDPATLLVA TTGKTARELE RDWDRDGNLY VVGSMGCAAS
     VGLGVALNAP DRFVTVIDGD GAVLMRMEAM ATIGRSAATR FTHVVLDNEA YESTGGQLTH
     SAGVDFAGIA AACGYRSHVD VSGMAELGAA VRRAQADPGP HFIRVRIRPG SDPKLGRPAL
     TPPEAAARFA RAARA
//
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