GenomeNet

Database: UniProt
Entry: D3F5K6_CONWI
LinkDB: D3F5K6_CONWI
Original site: D3F5K6_CONWI 
ID   D3F5K6_CONWI            Unreviewed;       571 AA.
AC   D3F5K6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Thiamine pyrophosphate protein TPP binding domain protein {ECO:0000313|EMBL:ADB50673.1};
GN   OrderedLocusNames=Cwoe_2248 {ECO:0000313|EMBL:ADB50673.1};
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:ADB50673.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|EMBL:ADB50673.1, 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   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; CP001854; ADB50673.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3F5K6; -.
DR   STRING; 469383.Cwoe_2248; -.
DR   KEGG; cwo:Cwoe_2248; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_11; -.
DR   OMA; NGFHPHA; -.
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; cd00568; TPP_enzymes; 1.
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; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          22..142
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          213..343
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          406..545
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  58014 MW;  EE100506D8FFD4CC CRC64;
     MSAPASSGGE AASQPAPPPA SSGGEALVQA LEQLGVTCAF GLPGVHNLPA WAALARSPIR
     LVGVRHEQTA AYAADGYARA SGRLGVALTT TGPGAANALG ATGEAWASHS PVLVIATDIP
     TTLRRAGAYR GVLHETRDQA AMFEPVVKRT YVCHAADHIA PLVQAAAAHA LHAPSGPVYV
     QIPTDLLSAP VGRALAPPAP APPRAPADPA ALRRAVELLD DAERVLIWAG GGAVAAGAGS
     ALALLAERLA APVIETYGGR ALLGGHPCAV GLPPHLPHAG ELWDRADVVL AVGSDFDGMT
     TQNWLQPQPR CLIAVNVDPV GAAENYPPDV ALIGDARTTC EALAAAVSAA PPAAVDALAA
     DLASRRAAAD AFVAADEPQA AELLGTLAAV LDEDDVVVAD MCIPGYWTAA LHRFAQPRKL
     AYPVGWGTLG FAFPASIGTA LAGAGRALCV CGDGGFLFAA GELATLAQER IPLTLLIVDD
     GAYGMLRYDQ RHAGQEVFGV ELESPDFVAW ARACGIAATA VDGVGAPLAD ALRSALADPS
     PTVVVARASL DPPPTTSPRW YRRAAVPPPT A
//
DBGET integrated database retrieval system