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Database: UniProt
Entry: A0A0F2PYR7_9FIRM
LinkDB: A0A0F2PYR7_9FIRM
Original site: A0A0F2PYR7_9FIRM 
ID   A0A0F2PYR7_9FIRM        Unreviewed;       528 AA.
AC   A0A0F2PYR7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Thiamine pyrophosphate-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VR69_03400 {ECO:0000313|EMBL:KJS17792.1};
OS   Peptococcaceae bacterium BRH_c4b.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS17792.1, ECO:0000313|Proteomes:UP000033446};
RN   [1] {ECO:0000313|EMBL:KJS17792.1, ECO:0000313|Proteomes:UP000033446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS17792.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS17792.1}.
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DR   EMBL; LADO01000013; KJS17792.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2PYR7; -.
DR   STRING; 1629717.VR69_03400; -.
DR   PATRIC; fig|1629717.3.peg.2312; -.
DR   Proteomes; UP000033446; 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   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   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..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          188..312
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          373..518
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   528 AA;  57338 MW;  091ADC6C0A611E85 CRC64;
     MGQTVAQLLL KLLAQWGVKN IYGVSGDAIL PFMDALGKQE EIKFISTANE QGASFMACGE
     ARVTGRPGVC LATEGPGAIN LLNGVADAYR DGVPMLIITG QVETSKLSTN TKQYFEQQQL
     FAPVTGLTTL LTRPESAAET LKVAFEKATG DSVPCHISVP KDIFLSPVKD YNIPDLGYPC
     PPGISGNIAE AIKAMDYCHK PIIITGKAAI AYKDTVFQLA CRIGAGIIPA QGARGIFPDT
     EDILLGGLGE AHIPPLLQQS DCILLIGASP YEHKFIPAHV TVLQIDTRPQ NIAHHLRAFA
     LTGDVALILM ELFEGLSKKI PDSNWQNEIK KHHDNRLEMI RSEANLSGKP ISPRKVVSLL
     NDVLPEDAVI AIDSGEFMHW FDRSFIAKSQ KVIISDYWRC MGSGLPIGLG AKVASPGKKV
     IVLTGDGCFI MTMQEIITAV RYSLPVVVII FNNSNYLLEK HRMQKKGMIP FGVDVRTPDF
     ALIAKACGAE GIRLEEPDML KDALGKAVAL DRPAVIDIIV MDEMPRFI
//
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