ID   A0A124IJ43_9PROT        Unreviewed;       544 AA.
AC   A0A124IJ43;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Thiamine pyrophosphate-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=APF80_04965 {ECO:0000313|EMBL:KUO58445.1};
OS   Alphaproteobacteria bacterium BRH_c36.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1734406 {ECO:0000313|EMBL:KUO58445.1, ECO:0000313|Proteomes:UP000053382};
RN   [1] {ECO:0000313|EMBL:KUO58445.1, ECO:0000313|Proteomes:UP000053382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c36 {ECO:0000313|EMBL:KUO58445.1};
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 (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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:KUO58445.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LOEV01000124; KUO58445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IJ43; -.
DR   STRING; 1734406.APF80_04965; -.
DR   Proteomes; UP000053382; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 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.
PE   3: Inferred from homology;
FT   DOMAIN          3..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          380..525
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   544 AA;  56988 MW;  AACC65EC2215149B CRC64;
     MKRGADLLVD TLARAGVTRI FSLSGNQIMP IYDACIDAGI TIHHTRHEAS AVFMADAWAQ
     LTGQIGVALV TAAPGFANAM GALFTALQSE SPVLLLSGDS PRTQDGRGAF QELDQIAVST
     PITKLSARLT TVDYVAEETA EAIRVALSGR PGPVHLALPF DVVQATIETP TPLQPDALAP
     VAGRVAPEDM EALKEALAAA ERPIILVGPS LNRTRGGSVF GELESTLGVP LLAIESPRGL
     NDPALGRLGT ALTKADLIVS LGKRIDYTLA LGNSDKVGGE QKWIVVDVDR KERGIAALNL
     KDRLLLSIAA DPRAVVTALS SQPAEASDQS GWQSEVASLT SERSYDGAPA PAHGAISPWA
     LCAAVQRQID SSPQSVLICD GGEFGQWAQA VCSARERLIN GPSAAIGGML CYALGARCAR
     PDATIFALMG DGTVGFQFAE FETAVREKLP FVVVIGNDAC WNAEHQIQMR EYGPERLIGC
     QLSDARYDLA AAGLGGHGEY VTDVRDLDAA LARARASGLP ACVNVRIRGE PAPTISSGPA
     VSAH
//