ID A0A0G9MZ78_9SPHN Unreviewed; 512 AA.
AC A0A0G9MZ78;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Benzoylformate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AAW00_10300 {ECO:0000313|EMBL:KLE34583.1};
OS Aurantiacibacter luteus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE34583.1, ECO:0000313|Proteomes:UP000053464};
RN [1] {ECO:0000313|EMBL:KLE34583.1, ECO:0000313|Proteomes:UP000053464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA37 {ECO:0000313|EMBL:KLE34583.1,
RC ECO:0000313|Proteomes:UP000053464};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter luteus KA37.";
RL Submitted (APR-2015) 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:KLE34583.1}.
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DR EMBL; LBHB01000002; KLE34583.1; -; Genomic_DNA.
DR RefSeq; WP_047004230.1; NZ_LBHB01000002.1.
DR AlphaFoldDB; A0A0G9MZ78; -.
DR STRING; 1581420.AAW00_10300; -.
DR PATRIC; fig|1581420.6.peg.2111; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000053464; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000053464};
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 373..508
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 512 AA; 53791 MW; 422A45FA0E6A9C85 CRC64;
MTNVREAAFA VFDHFGVDRL FGNPGSTELP MLKGLPFPYV MGLNEAVVVG MADGYARASG
RPALVNLHSA AGTGHSLGNL FTAWKNNAPV VVTAGQQARS ILPFDPFLYA ERPSEFPRPY
VKFAIEPARA EDVPLALARA FAAALTPPMG PVFVSIPVDD WERTCDLPDL PVLTLCPVPS
ATGIESLAAL LDQAENPALV LGTGVANAGG WACAVRLAEK CGAHVYAAPY AARETFPEDH
PQFAGFLPAW RDRIREMLAP HDAILVFGAS VFTYHVEGEG PHWPPHATLG ALSDDPAHLS
NLPGGIGVLG DVEDGLAQLA HRTNVRPFVG EPRTMAAPEA AMTSAHVLAQ IAALRPEGAI
IVEEAPTARG PMHDHLPILR EGGFYTCASG GLGYGLPGAV GVAMAQADKV IAVLGDGGAM
YTIQGLFTAW QEQLPVSFVV LNNGAYAALT SFSGEFGMNH VPGCDLAGLD FVSLARGMGL
EALRVDSVDD LDAALEWSFA AGGPTLLDLR IA
//
