ID E1TF04_BURSG Unreviewed; 587 AA.
AC E1TF04;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:ADN60234.1};
GN OrderedLocusNames=BC1003_4300 {ECO:0000313|EMBL:ADN60234.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN60234.1};
RN [1] {ECO:0000313|EMBL:ADN60234.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN60234.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP002218; ADN60234.1; -; Genomic_DNA.
DR AlphaFoldDB; E1TF04; -.
DR STRING; 640512.BC1003_4300; -.
DR KEGG; bgf:BC1003_4300; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_4; -.
DR OrthoDB; 2254214at2; -.
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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 32..141
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 223..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 416..568
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 63223 MW; CBAB4A3379B2B82A CRC64;
MSAVVSSLNP VTGSTTAEDT LKQKTRNAGV VSGGHLVAKA LKNEGVDTIF TLCGGHIIDI
YDGCVDEGIR IIDVRHEQVA AHAADGYARQ TGKLGCVVTT AGPGCTNAVT GIATAFRSES
PVLHIGGQGA LTQHKMGSLQ DLPHVDMMAP ITKFAASVSS TERVADMISM AARECFNGAP
GPAYLEIPRD VLDREVELTR AVVPQPGHYR ASAKSIGDPR DTEKLADILV NSERPAILYG
QQVWTARGHE EAIALLRGLD IPGYFNGASR GLLPPGDPHH FDRTRSQAFA NADVLIVVGT
PFDFRMGYGK RISKELTLVQ IDMDYRTVGK NRDIDLGLVG DPGAILAAVL QAASGRLKDD
KRQARRKWMA QLQDAEATAT EKLMPLFKSN NTPIHPYRVA YELNEFLSDD TIYIGDGGDV
VTISAQAVRP RRPGQWMDPG ALGSLGVGTG FALAAKVAHP HKEVLCYYGD GSFGMTAFDM
ETANRFGAPY LAVIGNNSAM NQIRYGQLAK YGDERGNVGN LLSDVPFSKF AEMLGGYGEE
VRDPAQIASA LQRAREAIHR TGRSAVVNIW VDPREYAPGT KNQTMYK
//
