ID A0A1C6MJA6_9ACTN Unreviewed; 554 AA.
AC A0A1C6MJA6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:SCK18883.1};
GN ORFNames=H181DRAFT_01331 {ECO:0000313|EMBL:SCK18883.1};
OS Streptomyces sp. WMMB 714.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1286822 {ECO:0000313|EMBL:SCK18883.1, ECO:0000313|Proteomes:UP000182206};
RN [1] {ECO:0000313|Proteomes:UP000182206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMB 714 {ECO:0000313|Proteomes:UP000182206};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FMHJ01000003; SCK18883.1; -; Genomic_DNA.
DR RefSeq; WP_045863278.1; NZ_FMHJ01000003.1.
DR AlphaFoldDB; A0A1C6MJA6; -.
DR STRING; 1286822.GCA_000964305_01329; -.
DR OrthoDB; 2443624at2; -.
DR Proteomes; UP000182206; 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:UP000182206};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 333..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 57643 MW; 332CD092D2C0BCEF CRC64;
MQTVREAALE VMRRYGLTTV FANPGSTEVP FLAGLPDDIR FVLALHEGSV VGAATGYALA
RDAPALALLH TTAGLGNAVG ALSTARVNKA PLVVIVGQQD RRHLVQEPFL AGRLEQLAGD
YPVTTETPPR AQDVPGALAR AVHAARTMRG PALVIVPMDD WARPAESLPL PAPEELRLPA
AADTAAAGEV AALLGSASAP ALVVGAGADH PVTWEALTAL AGRLDCDVWQ ESFGARAGFP
QDHPRFAGHL PADRPRLRAV LAPYDLVLTV GAPVFRQYPY ESGALTGPGT RLALVTDDPA
EARRAPVELA VVARLPAFCE ALADAAGADG VAEPAAGGGP SAGVAGAGRA PQRRRPRRER
PAPPPPPAEG GPLRAAHVLA ELARLLPPET VLVEETPSSR PDLHALVPAR RPLGFLSAAM
GALGFALPAA VGVRMGAPER PVVAVVGDGS SLYQIQALWT AAHYRVGVLF VVLANGRYAI
MDRLAEKAGR SAPWPAFEEV GIAAAARALG CPARRVSDHA MLRAELEGLL PELADRSGPL
VLEVEVAADE HFQP
//
