ID A0A0P7B609_9HYPO Unreviewed; 399 AA.
AC A0A0P7B609;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phosphonopyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK830_g9298 {ECO:0000313|EMBL:KPM37283.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM37283.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM37283.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM37283.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPM37283.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKCW01000171; KPM37283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B609; -.
DR STRING; 78410.A0A0P7B609; -.
DR OrthoDB; 2694079at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000050424}.
FT DOMAIN 13..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 259..333
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 399 AA; 43190 MW; C85141FF8F1CBAFA CRC64;
MATLDPRLFY EQALVGNGIT HAFGVPDSCL KGFLSYLYDT KKSPEHIVTA SEGAAIGLAA
GYYLSTKNLA VAYMQNSGLA NSLNPLQSLA AKEVFGIPLL LLVGWRGKPG EHDEPEHLLA
GPRTLETLES QGFPYEVLPD TLEAVAGAVA RLIKAAREGN TPVALVVPNH RFAAYSPEGG
QSNGLWQPPV TNLAKLTARP EDWRSSEGDL PLSREHAMRI ILKRLYPADV TVSSVGGNSR
EIYKVRKENN EDLSRAFLSI GAMGHTYPLA FGVQIGHSKG RVVCVEGDGS FLMHVGNVAV
LAAQASDKLV HVVVHNGIHC STGSQPIPIN TNNLLSLAGS LPYKQKFFVD SAEGLIQAFE
WAEKTTLIVV VVNQHVSKDL PRPSEHPFEL RDSFISHFT
//
