ID   A0A0J1CP06_9BURK        Unreviewed;       600 AA.
AC   A0A0J1CP06;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KLU22387.1};
GN   ORFNames=EOS_30790 {ECO:0000313|EMBL:KLU22387.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22387.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU22387.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
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:KLU22387.1}.
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DR   EMBL; AEJF01000180; KLU22387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1CP06; -.
DR   PATRIC; fig|908627.4.peg.6865; -.
DR   Proteomes; UP000035963; 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; cd00568; TPP_enzymes; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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          27..136
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          230..336
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          434..581
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   600 AA;  64589 MW;  C7799A3EA070DFFF CRC64;
     MRDGEIQLTV SAQIVLETMG SLAPSSVSKT VVKSLESAKI DHVFLVPGKL IYPLLEAIDE
     SPSIRAIVGA HETGSAFMAD GYARASRKFG VCIGISGPGT MNFVPGMAAA HADQIPMLYI
     AGGVSSQAEG KGAFQDATLS GIFESGVVKN LVENVIELKN KENIQAEMRR ATDGLNWMRR
     ARSFISIPID VQKQEVLSGQ DAARQLYDHG EFNVREVPAS RAVLDALCKQ YLLKSKRVAF
     LIGSRGNDAE TAKVLLEVAE KFHIPVATTL SGKGAFPEDH VLALGIYGFS GHSRAAHVIN
     SDGLDALVVF GSDLNQRDSM NWSKKLAAGK ELIIFDDSFD PPAMGHIGHG SIFSGIGATF
     RVLSKTDTDS SADFPKVLET RKAWVAEVIQ TPLYDDQFEQ VSAGVSGGDR SLYPGDVVKR
     LCQLLPKDSN VVVDSGAHRI FMAHYWLSSG IGNYFSSSSL APMGWAIAAG IGIKLAAPER
     PCVVVTGDGC MLMHGMEIQT AARYRVKMIY VVLNNSAHGA IHIDAISKGS ISEQFTKLPR
     HDWTAFASSL GVAARMVEHL DELEDVLSEA SRYNGPFLIE VMTGVFPAPN RYYAECAACS
//