ID A0A0F0C944_9CLOT Unreviewed; 375 AA.
AC A0A0F0C944;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:KJJ70353.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:KJJ70353.1};
GN Name=mdlC {ECO:0000313|EMBL:KJJ70353.1};
GN ORFNames=CLFS41_29220 {ECO:0000313|EMBL:KJJ70353.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ70353.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ70353.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ70353.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-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:KJJ70353.1}.
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DR EMBL; JYHN01000061; KJJ70353.1; -; Genomic_DNA.
DR RefSeq; WP_045092697.1; NZ_JYHN01000061.1.
DR AlphaFoldDB; A0A0F0C944; -.
DR PATRIC; fig|1609975.3.peg.3139; -.
DR Proteomes; UP000033604; Unassembled WGS sequence.
DR GO; GO:0050695; F:benzoylformate decarboxylase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:KJJ70353.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604}.
FT DOMAIN 5..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 229..344
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 375 AA; 40941 MW; 261DB18EB33D1A38 CRC64;
MLDQNLVLDE LKKNGVTFFT GVPDSYLNGF CNHILKNAPD RTIIAANEGN AIGIASGYYF
ASKEIPLVYM QNSGMGNTVN PLVSLADEHV YAVPMLLLIG WRGRPGTGDW PQHELQGEIT
PGLLDIMHIP YTVLEDDNGK IGDVLAAAVS YARENRKPYA LIAPKGVMAG EKTDNRDDRY
PMNREEAIEI ILDHLPSETI YAATTGRATR ELFFLREKRK EGKDHDFLNV GAMGHTSSVA
LGIALEKKDR KVVCLDGDSA VMMHLGAMTM VSKLDVPNFI HIVLNNGAHE SVGGQPSAGH
LVDLTGIAQA CGYRTIGKPV GTREELIKAL DDLKNSGQAS FIDVRIHKGL SGKLPPLDFL
HKEAVDGLIY ELNKD
//