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
//