ID A0A1C6V1N2_9ACTN Unreviewed; 531 AA.
AC A0A1C6V1N2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:SCL60218.1};
GN ORFNames=GA0070603_2974 {ECO:0000313|EMBL:SCL60218.1};
OS Micromonospora chersina.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL60218.1, ECO:0000313|Proteomes:UP000198605};
RN [1] {ECO:0000313|EMBL:SCL60218.1, ECO:0000313|Proteomes:UP000198605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL60218.1,
RC ECO:0000313|Proteomes:UP000198605};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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; FMIB01000002; SCL60218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6V1N2; -.
DR STRING; 47854.GA0070603_2974; -.
DR OrthoDB; 2443624at2; -.
DR Proteomes; UP000198605; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 390..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..103
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..519
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 328..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 55630 MW; D101F3B9E71C1624 CRC64;
MATVRDTTYD LLRALGLTTV FGNPGSTEEP FLADFPADFR YVHALQEASA MAMADGYAQA
TGRPAHVNLH TAPGIGNGMG NLVTAWHNKT PLIVTAGQQT REMLLIEPRL ANPRAVELTQ
PYVKWAHEPA RAQDVPAAFM RAYASAVQPP AGPVFLSLPM DDWAQPADPP PQVRTVATRI
APDPDRLRGF AATLAAARAP ALVLGAAVDR ADAWPAAVAL AERLAAPVWA APAPERAVFP
EGHPQFRGVL PYAIGPLAEA LHGHDTVLVV GAPVFRYYPH VPGDYLPADA QLLHVTDDPD
EAARAPVGES LLGDAGLAMA GLVELLPPAD RPAPPARDAP APPEATDPPS ADAVFAALAA
QWPADGVLVQ ESPSNLAALR RRLRIDRPRS YFTMASGGLG FGLPAAVGIA LAERDTGRGR
PVVAVVGDGS FHYSVQALWT AAQLGLPLAV VVPVNRQYAI LKAFAELKHT PGVPALDLPG
LDVTAVARGY GCAAEVVESP DRLGPALAAA LAADRPTVLP VPISTDVPRI L
//
