ID A0A069PJE9_9BURK Unreviewed; 567 AA.
AC A0A069PJE9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KDR40054.1};
GN ORFNames=BG61_27970 {ECO:0000313|EMBL:KDR40054.1};
OS Caballeronia glathei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR40054.1, ECO:0000313|Proteomes:UP000027466};
RN [1] {ECO:0000313|EMBL:KDR40054.1, ECO:0000313|Proteomes:UP000027466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR40054.1,
RC ECO:0000313|Proteomes:UP000027466};
RA Liu X.Y., Li C.X., Xu J.H.;
RT "Draft Genome Sequences of Four Burkholderia Strains.";
RL Submitted (MAR-2014) 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:KDR40054.1}.
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DR EMBL; JFHC01000047; KDR40054.1; -; Genomic_DNA.
DR RefSeq; WP_035937209.1; NZ_JFHC01000047.1.
DR AlphaFoldDB; A0A069PJE9; -.
DR STRING; 60547.GCA_000751215_05166; -.
DR Proteomes; UP000027466; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000027466};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 567 AA; 60953 MW; 8E4020547A3BE680 CRC64;
MAPSAAPSSD STQTTGARLV VDALLTHGVE RVFCVPGESF LAVLDSLHDE TARIQTIVCR
HEAGAANMAE AVGKLTGRPG VAIVTRGPGA THASIGVHTA FQDSTPMILL IGQCAREHMD
REAFQEIDYR RMFGQMAKWV AQIDDPRRVP EYLSHAFHVA TSGRPGPVVL ALPEDMLSEA
CPAVPGAPRY QRVAAAPAPA QTERLREMLA AARKPFVIAG GSGWTDSATR DFARFAEQWQ
LPVGCAFRFQ DTLDNEHPNY AGDVGLGINP ALAARIRDAD LLLVIGPRLG ESTTGGYTLL
DIPKTKQTLV HIHQGAEELG RVYSADLPIV SGMPEIASAL AALAPPASIA WAGSAAAAHD
AYLEWRKPKP MLGDVQLGEI MRELSERLPA DSIVTNGAGN YATWLHRHYS YRHFRSQVAP
TSGAMGYGVP AAIAAKSLYP GRTVVAFAGD GCFMMSSHEL ATAMQYGLAV IFIVVNNAQY
GTIRMHQERH YPDRVHGTGL TNPDFVAYAR SFGAHGELVE STAQFMPAFE RAAASGLPAV
IEIRIPQDQS TPGATLDQVR EQGRKLR
//