ID B1TEN4_9BURK Unreviewed; 608 AA.
AC B1TEN4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Thiamine pyrophosphate protein TPP binding domain protein {ECO:0000313|EMBL:EDT37969.1};
GN ORFNames=BamMEX5DRAFT_6250 {ECO:0000313|EMBL:EDT37969.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT37969.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT37969.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT37969.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-2008) 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:EDT37969.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABLK01000349; EDT37969.1; -; Genomic_DNA.
DR RefSeq; WP_006761987.1; NZ_ABLK01000349.1.
DR AlphaFoldDB; B1TEN4; -.
DR PATRIC; fig|396597.7.peg.1209; -.
DR Proteomes; UP000004814; 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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 3..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..545
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 608 AA; 65205 MW; 8F940280D07645FC CRC64;
MATVADFIVE RLYDWGVRRV YGYPGDGING FFGALSRAEG KIEFIQARHE EMAAFMASAH
AKFTGELGVC VATSGPGATH LVTGLYDARL DHMPVLAIVG QQARAALGGH YQQEVDLPAL
LKDVAGAFVQ LAVVPAQVRH LVDRAVRIAL GARTVTALVL PSDLQELDYA PPKRAHGTVH
SGVGYTPPKV VPYADDLQRA ADVLNAGKKV AMLVGAGALH ATDEVIAVAD RLGAGAAKAL
LGKAALPDDL PWVTGSIGLL GTKPSYALMT ECDTLLVVGS GFPYSEFLPK EGQARGVQID
LKADMLSLRY PMEVNLVGDS AETLRALLPL LKERGDTGWR DRIAKWNADW RETLAARAAA
KASAGRGVNP QRAFTELSPR LPDDVILTSD SGSCANWYAR DLMMRRGMMG SLSGGLASMG
AAVPYAIAAK FAYPVRPVIA MVGDGAMQMN NMAELITVAK YWRQWPDPRW ICMVLNNEDL
NQVTWEQRVM EGDPKFDASQ QIPNVPYSRF ASLLGLKGIY VDDPEQLGAA WDDALASDRP
VVLEVKSDPE VPPLPPHVTL QQAKHFAETL VKGDPREANV IVETARQVLS AVLPGNGEHG
GKGGKKGA
//
