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
//