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Database: UniProt
Entry: C9LX28_SELS3
LinkDB: C9LX28_SELS3
Original site: C9LX28_SELS3 
ID   C9LX28_SELS3            Unreviewed;       381 AA.
AC   C9LX28;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:EEX76588.1};
DE            EC=4.1.1.82 {ECO:0000313|EMBL:EEX76588.1};
GN   Name=aepY {ECO:0000313|EMBL:EEX76588.1};
GN   ORFNames=SELSPUOL_02115 {ECO:0000313|EMBL:EEX76588.1};
OS   Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX76588.1, ECO:0000313|Proteomes:UP000003505};
RN   [1] {ECO:0000313|EMBL:EEX76588.1, ECO:0000313|Proteomes:UP000003505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35185 / DSM 20758 / VPI D19B-28
RC   {ECO:0000313|Proteomes:UP000003505};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) 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:EEX76588.1}.
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DR   EMBL; ACKP02000048; EEX76588.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9LX28; -.
DR   STRING; 546271.Selsp_0558; -.
DR   eggNOG; COG0028; Bacteria.
DR   Proteomes; UP000003505; 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:0032923; P:organic phosphonate biosynthetic process; IEA:InterPro.
DR   CDD; cd03371; TPP_PpyrDC; 1.
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   Lyase {ECO:0000313|EMBL:EEX76588.1};
KW   Pyruvate {ECO:0000313|EMBL:EEX76588.1}.
FT   DOMAIN          15..126
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          237..351
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   381 AA;  40995 MW;  4F9FECF519AB61F2 CRC64;
     MSGSQKEDVM QATEFLDILG ADFFVGVPDS QLRALCDALM ERYGNHAPHV IAANEGTAAG
     IAAGHYLATG RSPLVYLQNS GEGNIVNALA SLLHEKAYAI PLIFVIGWRG EPGVKDEPQH
     AYQGEVTLPL LELLQVEHFV LAKETRGEDV SDAMERFRSS LENGRSVAFV VRKGALTHDT
     KVSYKNGYAL RREEAIRTIL DAADESDVFV STTGKASREL FELREERGEG HERDFLTIGS
     MGHSSSIALG IALEKKGRRT WCLDGDGAFL MHMGAAAVIA AAKPSNFCHV VLNNEAHESV
     GGMPTAASSI DFPALARALG YAAARRAKDG EELAAALEEM KGQAGPCFLE VRCAVGSRAD
     LGRPTIPPKA NKLAMMRFLS L
//
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