ID A0A3N1MD86_9PROT Unreviewed; 558 AA.
AC A0A3N1MD86;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:ROQ01045.1};
GN ORFNames=EDC65_0217 {ECO:0000313|EMBL:ROQ01045.1};
OS Stella humosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Stellaceae; Stella.
OX NCBI_TaxID=94 {ECO:0000313|EMBL:ROQ01045.1, ECO:0000313|Proteomes:UP000278222};
RN [1] {ECO:0000313|EMBL:ROQ01045.1, ECO:0000313|Proteomes:UP000278222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5900 {ECO:0000313|EMBL:ROQ01045.1,
RC ECO:0000313|Proteomes:UP000278222};
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 (NOV-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 -!- 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:ROQ01045.1}.
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DR EMBL; RJKX01000011; ROQ01045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1MD86; -.
DR Proteomes; UP000278222; 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:UP000278222};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..107
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 410..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 59049 MW; EA50BCB48C81A6E4 CRC64;
MPTMTGKRAF LELLKQEGVD VLFGNPGTTE LPLMDALAAE ADIRYVLGLQ EAVVMGMADG
YAQASGKLAV VNLHVAPGLG NAMGMLYDAQ KAASPILVTA GQHEQSFNVT EPILWADLPT
MARPLVKWST EVHRLADLPR IVHRAAKTAM APPTGPVFLS LPGDILNDEA EIDLMAVTRV
APRIRADLDA IEAAAELLVR ADRPMLVAGD AVAQSRAHDE LAELAELLGA PVYLEGVSST
ASFPTSHPLH RGPMGRLSPV LRKLLGQYDT MFSVGGDLFT LSLPSDVEPI PEGLVTIHLD
LDPWELGKNY PARVAMLGDP KATLPEITAA VRRRLDDGRR AAMERRGAEM RARIADERAA
LAAKARADAG KSPVQALALL EAIGRVLPPD AVVIEEALSS AGGIRDLIRS DDPQSFFGLR
GGGIGWGLPA AVGAKVALPG RPVVAIVGDG SAMYSCQALW TAARYRLGVV FVILNNSSYR
ILKQRVNALR GHAAQTGTYV GMDLEDPAID FQALARSMGV ASNVARTVAE ATDLITAGIA
SGKPTLVEVT LDRSLGLG
//
