ID A0A222VWG0_9PSEU Unreviewed; 526 AA.
AC A0A222VWG0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:SDC89210.1};
GN ORFNames=DES30_104315 {ECO:0000313|EMBL:PWV78578.1},
GN SAMN05421630_104314 {ECO:0000313|EMBL:SDC89210.1};
OS Prauserella marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=530584 {ECO:0000313|EMBL:SDC89210.1, ECO:0000313|Proteomes:UP000199494};
RN [1] {ECO:0000313|EMBL:SDC89210.1, ECO:0000313|Proteomes:UP000199494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5506 {ECO:0000313|EMBL:SDC89210.1,
RC ECO:0000313|Proteomes:UP000199494};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWV78578.1, ECO:0000313|Proteomes:UP000246674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45268 {ECO:0000313|EMBL:PWV78578.1,
RC ECO:0000313|Proteomes:UP000246674};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; QGTN01000004; PWV78578.1; -; Genomic_DNA.
DR EMBL; FMZE01000004; SDC89210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222VWG0; -.
DR STRING; 530584.SAMN05421630_104314; -.
DR KEGG; pmad:BAY61_28120; -.
DR OrthoDB; 2443624at2; -.
DR Proteomes; UP000199494; Unassembled WGS sequence.
DR Proteomes; UP000246674; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF133; BENZOYLFORMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199494};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..105
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 377..516
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 526 AA; 55647 MW; 72C14203A75379B8 CRC64;
MGTVRDVTRE LLREWGLTTV FGNPGTTEIP FLTDWPSDFR YVLGLQESVV VAMADGYAQA
ARRPAVVNLH SAGGVGHALG SVFTAYRNRS PLIILAGQQT RSLLPEDPFL GATDAAVFPQ
PYVKWSCEPA RAEDVPAALS RAYHVATQPP YGPVFVSVPA DDWDVETAPI TARPRIPGFA
ADPDVLAELV SAIDAAVAPA IVVGSAVDQD GVVDEVIALA ERTRAAVYES PMSSRCSFPE
DHPSFLGFLV PERIALSETL SSHDLVIVLG APAFTYHVYR GEAETALPPM YVVSDDEQVL
ARAPQGIGVR ATVGLAVRAL VERAGAVTRP SPRALVRPPQ PAESTPVSGS YVYSVLAEML
PDDAVVVEEA PSHRNALHDH LPIRSCDMGF LAGASGTLGY ALPAAIGVGI ARPERKVVAV
LGDGSSMYSI QALWTAVTEQ VPVTFVVLDN SQYAAVRILG EAMGGAKLPG VDLGGIDFVA
LANGMGCATY QAEQPAELKA AFAAAFADLR PNLVHVRVDP SPEKIY
//
