ID A0A098U487_9BURK Unreviewed; 595 AA.
AC A0A098U487;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KGF79349.1};
GN ORFNames=IA69_24585 {ECO:0000313|EMBL:KGF79349.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF79349.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF79349.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF79349.1,
RC ECO:0000313|Proteomes:UP000029701};
RA Fida T.T., Spain J.C.;
RT "Identification of Arachidin-3 degrading bacteria in the peanut
RT rhizosphere.";
RL Submitted (JUL-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:KGF79349.1}.
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DR EMBL; JPQD01000034; KGF79349.1; -; Genomic_DNA.
DR RefSeq; WP_036238339.1; NZ_JPQD01000034.1.
DR AlphaFoldDB; A0A098U487; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000029701; 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; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 595 AA; 65031 MW; 9214A2EC040EB450 CRC64;
MSKSVGDFFV ERLYEWGVRT IFGYPGDGIN GVLGALDRAE GKIQFIQVRH EEMAAFMAAA
HAKFTGEPGV CLSTGGPGAA HMVTGLYDAK CDHVPVLAIC GQAPSTARGA HYQQELNLDR
LFQDVADYVY EASQPSQVRH LLDRAMRTAL GRNGVSVLVL PNDLQEKPYE DPPRKHGSVF
SGIGYAKPRV VPYEADLQRA ADVLNAGSKV AILVGAGALQ ATDEVIAVAE RLKAGCAKAL
LGKAALPDHL PWVTGSIGIL GTKASWELMS DCDTLLLIGT GFPYAEFLPK EGKARAVQID
IDPTMLSMRF PAEVNLHGDS AETLRLLLPL LKEKTDTDWR AKIEKEVRES YKTLEERALA
SANPINPQRV CYELSPLLAR DAIVTSDSGS CANWYARDLK VQRGQMYSLS GGLASMGAAV
PYAIAAKFAH PDRPVIALVG DGAMQMNNMA ELITVAKYWK RWKDPRWIVC VFNNQDLNQV
TWEQRVMEGN PKFEATQQIP DVPYHRFGEL IGLKGIFCND PDKVGEAWRE ALAADRPVVL
EFKTDPEVPP LPSHITLEQA RHFMTTIVKG DPSEGSMLAG VAKQVLSTIL PGDKK
//