ID A0A1I3G492_9GAMM Unreviewed; 528 AA.
AC A0A1I3G492;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:SFI18308.1};
GN ORFNames=SAMN04487959_12523 {ECO:0000313|EMBL:SFI18308.1};
OS Halomonas xianhensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=442341 {ECO:0000313|EMBL:SFI18308.1, ECO:0000313|Proteomes:UP000199040};
RN [1] {ECO:0000313|EMBL:SFI18308.1, ECO:0000313|Proteomes:UP000199040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6848 {ECO:0000313|EMBL:SFI18308.1,
RC ECO:0000313|Proteomes:UP000199040};
RA de Groot N.N.;
RL Submitted (OCT-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; FOPY01000025; SFI18308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3G492; -.
DR STRING; 442341.SAMN04487959_12523; -.
DR Proteomes; UP000199040; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:UP000199040};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..108
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..521
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 528 AA; 56823 MW; B0B1F2F9F70587CE CRC64;
MPTVHSVTYQ LLRRQGLNVV FGNPGSNELP FLKDFPEDFQ YVLGLHEGVV VGMADGYALA
SRRPVLVNLH AAAGTGNAMG ALTNAWYSHS PLVLTAGQQA RSMIGVESML ANVDAPSLPR
PLVKWSYEPA CPEDVPRALS QAIHMANLPA KGPVYVSIPH DDWGREVEED AALVARRDVH
HASTPSDAQL AGLAERLNQA RNPVMIVGPE VDAEHANALA VELAERLRMP AWVAPSASRC
PFPTRHACFR GVLPAAIAGI SSKLDGHDLI LVIGAPVFRY HQYAPGRYLP QGAELIHLTS
DVQEAARAPM GDALVGGLRA TLEKLLPTLT QSERAMPEPL PLPQPMADEP GRLAPESVFD
ALNELAPKDA IFVKESTSTV TAFWQRVEMR HPDSYFFPAA GGLGFGLPAA VGVQLARPER
QVIAVIGDGS ANYAISALWS AAQYGVPVVF IILRNDTYGA LRWFSRMLDA EDAPGLDVPG
LDFCSLARGY GVDAVCTDTR DAFENALRQA LNATKPMLIE VPTTTIEP
//
