GenomeNet

Database: UniProt
Entry: A0A1M5WXF9_9CLOT
LinkDB: A0A1M5WXF9_9CLOT
Original site: A0A1M5WXF9_9CLOT 
ID   A0A1M5WXF9_9CLOT        Unreviewed;       274 AA.
AC   A0A1M5WXF9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:SHH92237.1};
GN   ORFNames=SAMN02745196_01939 {ECO:0000313|EMBL:SHH92237.1};
OS   Clostridium collagenovorans DSM 3089.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121306 {ECO:0000313|EMBL:SHH92237.1, ECO:0000313|Proteomes:UP000184526};
RN   [1] {ECO:0000313|EMBL:SHH92237.1, ECO:0000313|Proteomes:UP000184526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3089 {ECO:0000313|EMBL:SHH92237.1,
RC   ECO:0000313|Proteomes:UP000184526};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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; FQXP01000006; SHH92237.1; -; Genomic_DNA.
DR   RefSeq; WP_072831817.1; NZ_FQXP01000006.1.
DR   AlphaFoldDB; A0A1M5WXF9; -.
DR   STRING; 1121306.SAMN02745196_01939; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000184526; Unassembled WGS sequence.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR049557; Transketolase_CS.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184526};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..271
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
SQ   SEQUENCE   274 AA;  29761 MW;  B769D4BA229EE5D3 CRC64;
     MKTNIEELQR IAKLIRKDIV EMLTESASGH PGGSLSAADI LTTLYFREMN VDTKNPKAAD
     RDRFVLSKGH AAPVLYAALA EKGFFDKSEL MNLRKINSIL QGHPNMNYVP GVDMSTGSLG
     QGVSAAVGMA LAGKIDKKDY RVYSLLGDGE LGEGQVWEAA MSAAHYKLNN LTIFIDFNGL
     QIDGKIEDVM NPNPIADKFV AFGWNVLSID GHNFEEIINA IEIARNTTDK PTAIVCKTIK
     GKGVSFMENE AGWHGSAPSK EQCKQALAEI GGEN
//
DBGET integrated database retrieval system