ID   A0A158KNY3_9BURK        Unreviewed;       564 AA.
AC   A0A158KNY3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:SAL82459.1};
GN   ORFNames=AWB68_06527 {ECO:0000313|EMBL:SAL82459.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL82459.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-2016) 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; FCON02000120; SAL82459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158KNY3; -.
DR   OrthoDB; 2254214at2; -.
DR   Proteomes; UP000054770; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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          14..129
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          201..339
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          396..542
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   564 AA;  60694 MW;  9E7B8F0612E7C4DD CRC64;
     MASAVASSDS PQTTGARLVV DALVTHGVER VFCVPGESFL AVLDSLHDET AQIQTIVCRH
     EAGAANMAEA VGKLTGRPGI AIVTRGPGAT HASIGVHTAF QDSTPMILLI GQCAREHMDR
     EAFQEIDYRR MFGQMAKWVA QIDDPRRVPE YMSHAFHVAT SGRPGPVVLA LPEDMLSEAC
     AAVPGAPRYQ RVAAAPAPGQ IERLQAMLSA AQRPFVIAGG SGWTEAATQD FARFVEQWQL
     PVGCAFRFQD TLNNEHPNYA GDVGLGINPA LAARIREADL LLVIGPRLGE STTGGYTLLD
     IPKTKQTLIH IHQGAEELGR VYSADLPIVS GMPEIASALA ALAPPSTIPW SGAADAAHAA
     YVEWRKPKPM LGDVQLGEIM RQLSERLPAD SIITNGAGNY ATWLHRHYAY RHFRSQVAPT
     SGAMGYGVPA AIAAKSLYPE RTVIAFAGDG CFMMSSHEIA TAMQYRLAVI FIVVNNAQYG
     TIRMHQERHY PNRVHGTGLT NPDFPAFARS FGAHGEIVAT TAEFMPAFER AVSSGLPAVI
     EIRIPQDQST PGATLDQIRE QGKK
//