ID V2GNA8_9BURK Unreviewed; 577 AA.
AC V2GNA8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:ESH92412.1};
GN ORFNames=B551_0221690 {ECO:0000313|EMBL:ESH92412.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESH92412.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESH92412.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) 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:ESH92412.1}.
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DR EMBL; AMPR02000436; ESH92412.1; -; Genomic_DNA.
DR AlphaFoldDB; V2GNA8; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000053474; 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 Reference proteome {ECO:0000313|Proteomes:UP000053474};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 33..149
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 416..561
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 61101 MW; 3745A3C961CEBD36 CRC64;
MTQPTADLRS SLSVSSPGSP DPAAATQPLP PRSGGRILVD ALRIHGAERV FCVPGESFLD
VLDALHDQPA IDLIVCKHEG AAANMAEADG KLTGRPGICF VTRGPGATHA SVGVHIAAQD
STPMILFVGQ IGREQRGREA FQEVDYAAMF GGMAKWVAEI DDPARIPELV ARAFQVATSG
RPGPVVLALP EDVLDGDAVC RDTGAYRPVV ASPSAADAAT LAGLLAAAQR PLVIAGGANW
RDEDAAAFAR FVHAWDLPVA CAFRRQDVLD NRDPHYVGHL SLGVNPRLAE RVRGADLIVA
FGTRLGDVAT DGYTLLEPPR PRQRLVHIHA DAAELGRVYQ PELAIHAGIG PGAAMLAGMP
APSTVRWREW TAAARADHQG FVAPAAPHAD ATGVDMTAVV DHLNRTLPDD AIVTNGAGNY
AVWLHRYFAY RRPRTQLAPT CGAMGYGLPA AISAKLRHPE RTVVCFAGDG CFQMYPQELT
TAAAVGANVV VLVVNNGMYG TIRMHQERRY PGRVSGTGIV NPDFVALAQA CGAWAERLTS
ADGFADAFAR ACAAGRPALL ELCTDPRQIT PAMRLKP
//
