ID A0A117V293_9SPHN Unreviewed; 521 AA.
AC A0A117V293;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:KUR76443.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:KUR76443.1};
GN ORFNames=AQZ49_12300 {ECO:0000313|EMBL:KUR76443.1};
OS Novosphingobium sp. FSW06-99.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR76443.1, ECO:0000313|Proteomes:UP000061032};
RN [1] {ECO:0000313|EMBL:KUR76443.1, ECO:0000313|Proteomes:UP000061032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR76443.1,
RC ECO:0000313|Proteomes:UP000061032};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KUR76443.1}.
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DR EMBL; LLZQ01000017; KUR76443.1; -; Genomic_DNA.
DR RefSeq; WP_067615961.1; NZ_KQ954256.1.
DR AlphaFoldDB; A0A117V293; -.
DR STRING; 1739113.AQZ49_12300; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000061032; Unassembled WGS sequence.
DR GO; GO:0050695; F:benzoylformate decarboxylase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:KUR76443.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..108
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 375..517
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 521 AA; 54498 MW; B640DBE52B695218 CRC64;
MTAPHTVRQA TVALLDALGM TTVFGNPGST ELPLFRDFPA HFRYVLGLQE SVVIGMADGY
AQATRRAALV NLHSAAGLGH GLGNLFTAFR NQTPLVVTAG QQARAILPHD PFLFAERATE
FPRPYVKYAI EPARAADVPG AILRAWHIAM TPPCGPVFVS VPVDDWDRVC APVTVTMMAR
QIGGDAALLD ALADALAAAR RPAIVVGAGV ARDDAWAQTV SLAEAHNAAV FVAPMAARNG
FPENHRLFQG FLPAFREAIV AALDGHDLIL VLGAPVFTYH AEGAGPHVPP GAGVWQLVDD
PAAASALPVG TAIVTSLRPA LDALLRAPAP VRPAPPLRRI VPPAPGGRLR ADQALALLAA
HRPPGSVVVE EAPSHRATMQ THLPMVAPDS FYTTASGGLG HGLPAAIGVA LGRPGTRVIA
LLGDGSSMYA IQGLWTAARL DLPISFVVLN NARYQALHSF AEMFGLGIVP GTDLGGLDFA
GLAQAQGVDA VRVDTADDWD AALARSFATP RPTLIEVVLD R
//
