ID A0A171KQ30_9BURK Unreviewed; 544 AA.
AC A0A171KQ30;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Benzoylformate decarboxylase {ECO:0000313|EMBL:KKO70997.1};
GN ORFNames=AAV32_13500 {ECO:0000313|EMBL:KKO70997.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO70997.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO70997.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO70997.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
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:KKO70997.1}.
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DR EMBL; LBNE01000010; KKO70997.1; -; Genomic_DNA.
DR RefSeq; WP_068373203.1; NZ_LBNE01000010.1.
DR AlphaFoldDB; A0A171KQ30; -.
DR STRING; 206506.AAV32_13500; -.
DR PATRIC; fig|206506.3.peg.2866; -.
DR Proteomes; UP000078084; 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:0044281; P:small molecule 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 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:UP000078084};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..105
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 58306 MW; 38417913A2551055 CRC64;
MSDKTIRDVT FQLLRDLGLT TMFGNPGSTE ETFLKNFPED FRYIQTLHES SAVGAADGFA
QATRRPAIVN VHTSAGLSNA MSNILTASQN KTPLIITAGN QTRDMLLMEP WLTNVEPSLL
PKPWVKWSYE PVRAEDVPAA FMRAYAMAMQ PPAGPVFLSI PLDDWDKRAA GPAVVRSVTT
RIAPDPDRIA EFAQALSRAS NPALIYGSAI ARGDGWQQAI ALAEKLQAHV YAAPASERPP
FPETHPLYSG GLPFAIGPLS RKLKGHDLAI VIGAPVFRYY PYVEGDYLPE GLRLLHITDD
PSESGRAPVG DSLLGDAVLS LEALEKLVAG RSAPATPVTR QPHGLAPHPA ASVETAGQGE
TLSALTLFQA LRAATPAETV LVEESPSNLG ELHTAWPVDR PDSFYTFASG SLGWNLPASV
GLALAERDSG RNRPVLAIIG DGSFQYSIQG LWTAVQHELP ILFVVPRNGQ YGILKSFAEL
EQTPGVPGLD LPGLDFVALA NGYGAHGVRA TTTDEIRAVC TEAFSRKGPT VLEVPVLPTI
PPLL
//