ID A0A1D9H617_9BURK Unreviewed; 584 AA.
AC A0A1D9H617;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:AOY95333.1};
GN ORFNames=BKK79_26535 {ECO:0000313|EMBL:AOY95333.1};
OS Cupriavidus sp. USMAA2-4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY95333.1, ECO:0000313|Proteomes:UP000178101};
RN [1] {ECO:0000313|EMBL:AOY95333.1, ECO:0000313|Proteomes:UP000178101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY95333.1,
RC ECO:0000313|Proteomes:UP000178101};
RA Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT "Complete genome sequences of three Cupriavidus strains isolated from
RT various Malaysian environments.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; CP017749; AOY95333.1; -; Genomic_DNA.
DR RefSeq; WP_071039259.1; NZ_CP017749.1.
DR AlphaFoldDB; A0A1D9H617; -.
DR STRING; 876364.BKK79_26535; -.
DR KEGG; cuu:BKK79_26535; -.
DR Proteomes; UP000178101; Chromosome 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000178101};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 20..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..342
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..556
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 584 AA; 63302 MW; CAE3FA28744B2FBB CRC64;
MSTDNSTQAP RLQAAPTERN GGQILIDQLI IQGVKRVFLV PGESYLPCID ALYDHQDKIQ
PIVCRQESGA GYMAEAHGKL TGEPGICFVT RGPGATNASI AVHTAYQDST PMILFVGQVG
NDFAEREAFQ EIDYRRMFGQ MAKWVAQIDR TERIPEFIAR AFAVATSGRP GPVVLALPED
TLWGKASVPD VPRYRRAHAA PTPDAMDELA RLLAAAERPF LLLGGSGWTP QAARSMEGFA
ERFGLPVGVA WRRLECFDNH HPNFAGHVGW GMPESLRRRV QQADLLIAVG TRMGEATSEG
YSVIASPLPQ QRLVHVYPDA GELGRVFHPT LPIVADAPSF AAAVDRLAPA RERTGSGAAY
QARRAHEAHE EYLAGQEPKA APGKLNLNKV ACHVRDHLPA DACLTVGAGN YALYPHAYHR
FRGVGTSLAP TVGSMGYGLP AAIAAKLEDP RRTVVCFAGD GCFQMNLQEL GVAMQYRVGI
VVLVFNNGIW GTIRAHQERE FPGRTVALGF DNPEFSELAR AYRGYGEIVD SDAAFGPAFE
RALAFANAER LPALLELRYD PDGIAPGMTL SGIRADALAR QSEA
//
