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Database: UniProt
Entry: L1QFL0_9CLOT
LinkDB: L1QFL0_9CLOT
Original site: L1QFL0_9CLOT 
ID   L1QFL0_9CLOT            Unreviewed;       273 AA.
AC   L1QFL0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Transketolase, thiamine diphosphate binding domain protein {ECO:0000313|EMBL:EKY26470.1};
GN   ORFNames=HMPREF0216_01966 {ECO:0000313|EMBL:EKY26470.1};
OS   Clostridium celatum DSM 1785.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY26470.1, ECO:0000313|Proteomes:UP000010420};
RN   [1] {ECO:0000313|EMBL:EKY26470.1, ECO:0000313|Proteomes:UP000010420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY26470.1,
RC   ECO:0000313|Proteomes:UP000010420};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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:EKY26470.1}.
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DR   EMBL; AMEZ01000055; EKY26470.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1QFL0; -.
DR   STRING; 545697.HMPREF0216_01966; -.
DR   PATRIC; fig|545697.3.peg.1934; -.
DR   eggNOG; COG3959; Bacteria.
DR   HOGENOM; CLU_009227_4_1_9; -.
DR   Proteomes; UP000010420; 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:UP000010420};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          15..264
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
SQ   SEQUENCE   273 AA;  29999 MW;  532C47F690190B2E CRC64;
     MDKMNKEMLI SKSKDIRTNI IEMLYESKSG HPGGSLSCAD ILTYLYYEKM NVDVNNPKDE
     NRDRFVLSKG HAAPALYSVL AEKGFFDKEE LKNLRKLGAM LQGHPDAKKI PGVDVSTGSL
     GQGVSNAVGM ALGLKYKKST AKVYTVLGDG ELQEGLVWEA TMAASHYKLD NLVVIIDNNG
     LQIDGNNEDV MGVSPLDEKF KSFGFNVVTC NGHDFDEIHE AMNITDRIEG KPSIIIAQTI
     KGKGVSFMEN EAGWHGQAPN KEQTEKALID INN
//
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