ID A0A086WD84_9BURK Unreviewed; 589 AA.
AC A0A086WD84;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KFI07734.1};
GN ORFNames=JN27_09235 {ECO:0000313|EMBL:KFI07734.1};
OS Massilia sp. BSC265.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1549812 {ECO:0000313|EMBL:KFI07734.1, ECO:0000313|Proteomes:UP000028843};
RN [1] {ECO:0000313|EMBL:KFI07734.1, ECO:0000313|Proteomes:UP000028843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSC265 {ECO:0000313|EMBL:KFI07734.1,
RC ECO:0000313|Proteomes:UP000028843};
RA Kellom M., Bailey A., Poret-Peterson A., Noonan K., Raymond J.;
RT "Draft Genome of Massilia consociata BSC265, Isolated from Biological Soil
RT Crust of Moab, Utah.";
RL Submitted (AUG-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:KFI07734.1}.
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DR EMBL; JPXI01000029; KFI07734.1; -; Genomic_DNA.
DR RefSeq; WP_036247049.1; NZ_JPXI01000029.1.
DR AlphaFoldDB; A0A086WD84; -.
DR STRING; 1549812.JN27_09235; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000028843; 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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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:UP000028843};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 63180 MW; 3B7722DE649385CE CRC64;
MATVGDFLLE RLRQWGVRRI FGYPGDGING IMAAFGRQQA VEFVQTRHEE MAAFMACGHA
KFTGEVGVCL ATSGPGAIHL LNGLYDAKLD HQAVVAIVGQ QKRAALGAHY QQEVDLTTLF
KDVAGEYVQM AASTGQVRHL VDRAVRIALS ERCVTCIILP NDLQEEDAVP CPPREHGYTF
SGVGAASRAL VPPEDALRCA AAILNAGSKV AILAGAGAQG AHDELAEVAE LLGAGVAKAL
LGKAVLADGL PFVTGSVGII GTRASNAMLQ DCDTLLMVGS SFPYAEFLPP EGQARAVQVD
IDGRMLGLRY PMEANLQGDA KATLRALIPH LERKQDRSWR ERIEHDAAAS RRELLDKALE
PATPVNPQRV FTELSPRLPD GVVLAGDSGS VAAWYALHLE VRPGMLASLS GTLATMGSAV
PYALAAKLAH PDRPVIALAG DGAMQMTGIN GLMSVAWHWK QRGWTNPAFV VLVLNNRDLN
FVTWEQRGMQ GEPKFQPSQQ LPDFSYAEYA RMLGLDGERV DDPEQLGAAW ERALACDKPF
VLEAVVDPNI PPLPPQTVEQ QRRQYEEAIA KGDAEAGDVR RGADAQGGS
//
