ID   A0A0J8D4L8_CLOCY        Unreviewed;       276 AA.
AC   A0A0J8D4L8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Transketolase N-terminal section {ECO:0000313|EMBL:KMT21110.1};
DE            EC=2.2.1.1 {ECO:0000313|EMBL:KMT21110.1};
GN   ORFNames=CLCY_1c03440 {ECO:0000313|EMBL:KMT21110.1};
OS   Clostridium cylindrosporum DSM 605.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT21110.1, ECO:0000313|Proteomes:UP000036756};
RN   [1] {ECO:0000313|EMBL:KMT21110.1, ECO:0000313|Proteomes:UP000036756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 605 {ECO:0000313|EMBL:KMT21110.1,
RC   ECO:0000313|Proteomes:UP000036756};
RA   Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT   "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT   HC-1 (DSM 605).";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KMT21110.1}.
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DR   EMBL; LFVU01000028; KMT21110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8D4L8; -.
DR   STRING; 1121307.CLCY_1c03440; -.
DR   PATRIC; fig|1121307.3.peg.709; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000036756; Unassembled WGS sequence.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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:UP000036756};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMT21110.1}.
FT   DOMAIN          12..271
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
SQ   SEQUENCE   276 AA;  29819 MW;  5A95006653FCCB51 CRC64;
     MPRDINELTS VATEIRKDIV TMLTESASGH PGGSLSAADI LTALYFGEMN IDPKNPKCED
     RDRFVLSKGH AAPVLYAALA ERGFMAKEEL MTLRKIDSNL QGHPNMNDTP GVDMSTGSLG
     QGLSAANGMA LAGKLDNKSY RVYAYLGDGE LQEGQVWEAA MTSAHYKLDN LTAFVDYNGL
     QIDGNTTDVM NVEPIANKFE AFGWHVISIN GHSFEEIFKA IDEAKSTKGK PTMIVAKTVK
     GKGVSFMENQ AGWHGNAPSK EQCEEALKEL GGVING
//