ID A0A438AHS9_9RHOB Unreviewed; 532 AA.
AC A0A438AHS9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:RVV98228.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:RVV98228.1};
GN ORFNames=EKE94_10415 {ECO:0000313|EMBL:RVV98228.1};
OS Mesobaculum littorinae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mesobaculum.
OX NCBI_TaxID=2486419 {ECO:0000313|EMBL:RVV98228.1, ECO:0000313|Proteomes:UP000285908};
RN [1] {ECO:0000313|EMBL:RVV98228.1, ECO:0000313|Proteomes:UP000285908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M0103 {ECO:0000313|EMBL:RVV98228.1,
RC ECO:0000313|Proteomes:UP000285908};
RA Li F.;
RT "Mesobaculum littorinae gen. nov., sp. nov., isolated from Littorina scabra
RT that represents a novel genus of the order Rhodobacteraceae.";
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:RVV98228.1}.
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DR EMBL; RQXX01000003; RVV98228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438AHS9; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000285908; 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; 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 Lyase {ECO:0000313|EMBL:RVV98228.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000285908};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 532 AA; 56483 MW; 2ECBC23A23766787 CRC64;
MHPTGRSDHG VTVAEAVFAF MRQAGIDRIF GNPGSTELPM FVDLPKDFDY VLGLQESIVI
GMADAYAQIT DNAAFVNLHS AAGLGHAMGN LYTAFRNRAP LIVSTGQQVR ELLPGDPFLF
NEAPAEMAAP YVKWAVEPAR AEDVPAAIQR AYFTAMTPPR GPVLVSVPLD DWARRTHPLP
PRGMRFGLGA DPERLAELGR DIDAAQEVAI VVGPGVDADR AWREVQDLAE KIQAKVWVAP
MASRAGFPEN HQNFAGFLPA RQPALSDCLS GADLVLVLGA PVFTYHFPGT PEHLPPDTKL
WLVTDDPRQA AGALTGTAML ADIRLAARGL AANCSPRPPL TGPARHVPRV AVPDRITDAY
LYQVLTDLRD PGSIVVEEAP TARDALHDHF PITRPAGFFA TASGGLGYGL PAAVGAALTR
PGKTVIAPMG DGSSMYSIQA LWSAAEHDAD VFFVILNNGG YGALKGIAKL GQGRDVAGCE
IGHLDFVSIA QAQGVPARRC DDPAALPGIV KEMLAQTGPR LLEVIQTPPA AT
//
