ID A0A3A1P245_9SPHN Unreviewed; 512 AA.
AC A0A3A1P245;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:RIV83004.1};
DE EC=4.1.1.7 {ECO:0000313|EMBL:RIV83004.1};
GN ORFNames=D2V17_14495 {ECO:0000313|EMBL:RIV83004.1};
OS Aurantiacibacter xanthus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1784712 {ECO:0000313|EMBL:RIV83004.1, ECO:0000313|Proteomes:UP000265366};
RN [1] {ECO:0000313|EMBL:RIV83004.1, ECO:0000313|Proteomes:UP000265366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2015396 {ECO:0000313|EMBL:RIV83004.1,
RC ECO:0000313|Proteomes:UP000265366};
RA Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA Xu X.-W.;
RT "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT sediment.";
RL Submitted (AUG-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:RIV83004.1}.
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DR EMBL; QXFM01000114; RIV83004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1P245; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000265366; 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:RIV83004.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265366};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..101
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 184..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..509
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 512 AA; 53526 MW; 9A4401E06C154395 CRC64;
MTNVREAAYR VFEHFGVDRL FGNPGSTELP MLKGMPFPYV MGLNEAVVMG MADGFARASG
KPALVNLHSS AGTGHSLGNL FTAWKNNAPI VVTAGQQARS ILPFDPFLGA ERPTEFPRPY
VKFAIEPARA EDVPLALARA FAVALTPPMG PVFVSIPVDD WERECEMPAL PDLTLRTFPD
PAGIAKIAAM LDGAKNPALV LGTGVANAGG WDAAIALAEK TGVSVWAAPY AAREVFPETH
PQFAGFLNAW RDQIRDALGA HDAILVVGAP VFTYHVEGSG PHWPEGAALM ALSDDPNHLA
NLPGGGGVLG DPAAALAMLA EAAKARPFSG TSHQLIDPEP DMTAPYVLKR IAALRPDNAV
IVEEAPTARG PEHVTLPITR KGGFYTCASG GLGHSLPAAV GVALGQPDKV VAVLGDGSAM
YTIQGLFTAF QEKANVSFVV LNNSAYAALT GFSSEFGMNH VPGCDLTGLD FAKLAEGLGV
PSKPVDSVDA LDAALGWSMA ESGPTLLDVR IK
//
