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
//