ID Q0BCD6_BURCM Unreviewed; 535 AA.
AC Q0BCD6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:ABI88187.1};
GN OrderedLocusNames=Bamb_2631 {ECO:0000313|EMBL:ABI88187.1};
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI88187.1, ECO:0000313|Proteomes:UP000000662};
RN [1] {ECO:0000313|Proteomes:UP000000662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) 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; CP000440; ABI88187.1; -; Genomic_DNA.
DR RefSeq; WP_011657775.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BCD6; -.
DR GeneID; 69543173; -.
DR KEGG; bam:Bamb_2631; -.
DR PATRIC; fig|339670.21.peg.2270; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000000662; Chromosome 1.
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; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 13..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 535 AA; 56941 MW; FEE398CBD8A468C0 CRC64;
MSGTPSQSAA PITVRDAVID LFRQFGIDRV FGNPGSTELP MFRDFPADFR YVLGLQEAVV
VGMADGHAQA TGNAAVVNLH SAAGVGNAMG NLFTAFRNRT PLIVTAGQQA RAILPFDPFL
GATQAAEMPK PYVKWSIEPA RAQDVPAAIA RAYRIAMQEP RGPVFVSIPV DDWDQPAELL
PRRDVSSVVR PDPDALARLG DALDAARRPA LVVGAAVDRA GAWDDVVRLA ERHRASVYAA
PMSGRCSFPE DHPLFAGFLP AIREKIVARL DGHDLVFAFG APAFTYHVEG FGPHVPPGAT
LVQLVDDPGV AAWTPSGDAV VGNLRLAARD LLARPAPAER PMPAPRPPRP RAEAPAAGER
MSVAFALQTL AELRDAHDIV VEEAPSARPV MQTHLPFTRS GTFYTMDSGG LGYGMPAAVG
VALARPGRRV IALIGDGSSL YSVQALWSAA QQKLPITFVI LNNRRYAALQ EFASVFGFGP
DDPVQGTDLP DLDFVALAQG MGCRGIRVTD AARLRDTLTD ALRAGTPVVV DVEVA
//
