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Database: UniProt
Entry: D3F2F9_CONWI
LinkDB: D3F2F9_CONWI
Original site: D3F2F9_CONWI 
ID   D3F2F9_CONWI            Unreviewed;       582 AA.
AC   D3F2F9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding protein {ECO:0000313|EMBL:ADB52225.1};
GN   OrderedLocusNames=Cwoe_3808 {ECO:0000313|EMBL:ADB52225.1};
OS   Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS   100937 / ID131577).
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB52225.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|EMBL:ADB52225.1, ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RX   PubMed=21304704;
RA   Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Mavromatis K., Ivanova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chain P.,
RA   Meincke L., Sims D., Brettin T., Detter J.C., Rohde M., Goeker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.-P.,
RA   Hugenholtz P.;
RT   "Complete genome sequence of Conexibacter woesei type strain (ID131577).";
RL   Stand. Genomic Sci. 2:212-219(2010).
RN   [2] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) 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, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP001854; ADB52225.1; -; Genomic_DNA.
DR   RefSeq; WP_012935276.1; NC_013739.1.
DR   AlphaFoldDB; D3F2F9; -.
DR   STRING; 469383.Cwoe_3808; -.
DR   KEGG; cwo:Cwoe_3808; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_0_11; -.
DR   OMA; YEATHEC; -.
DR   OrthoDB; 4959782at2; -.
DR   Proteomes; UP000008229; Chromosome.
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:UP000008229};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          8..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          197..322
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          385..530
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   582 AA;  61937 MW;  ED6BFE6B3B511348 CRC64;
     MAPRASGTVA EQFVTVLRQA GVERIYGVVG DSLNPIVDAV RRTDGIDWVH VHNEEAGAFA
     AGAEAQLTGR LAVCAGSSGP GNLHLIQGLF DAHRSGAPVL ALASHIPSAQ VGTLFFQETH
     PERLFQECSH YCELVSRAEQ MPRVLRIAIQ TALGRGGVSV VAMPGDLANE DVANATGESV
     LAAPCATVVP SDDQVIALAD AINRAGSVTL FCGAGVRDAH AEVMALAGKV HSPVGHALGG
     KEWIQFDNPY DVGMSGLLGY GACHEASNEA DLLVLLGTDF PYDNFLPQAH TAQVDRDPAK
     LGRRTLVDFP VHGDVAATIA KLLPLLEQKT DRTFLDTMLR RHAARLEKVV DAYTRNVEKH
     VPIHPEYAAA MLDELAADDA IFTVDTGMNN VWAARYLTPN GRRRVIGSWR HGTMANALPQ
     AIGAQLAHPG RQVVSLSGDG GLSMLLGELL TVRIHNLPLN VVVFNNASLG MVKLEMLVGG
     IPDWQTDHEP HDFAAIARAI GIDAIRIEDP AQVRDGLADG LSRPGPTLIE LVTDSNALSM
     PPNITAEQIK GFAIAASKMV VEGGVGRMID LARSNLRNIP RP
//
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