ID A0A285QXF7_9ACTN Unreviewed; 237 AA.
AC A0A285QXF7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:SOB84752.1};
GN ORFNames=SAMN06272789_5013 {ECO:0000313|EMBL:SOB84752.1};
OS Streptomyces sp. 1331.2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB84752.1, ECO:0000313|Proteomes:UP000219030};
RN [1] {ECO:0000313|Proteomes:UP000219030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA Varghese N., Submissions S.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; OBMJ01000001; SOB84752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285QXF7; -.
DR Proteomes; UP000219030; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000219030}.
FT DOMAIN 31..220
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
SQ SEQUENCE 237 AA; 24850 MW; 3A3909BE0B1BBA16 CRC64;
MTTNATAETP TESRFEDLPA LMGLMTGDEK HGPAATSTLD ALWVLYDRVL RVSPAGAGAQ
DRDRFLLSKG HGPMAYYAVL AAKGFIDPAV LPSFGGYDSP LGHHPDRTLI PGVEIASGSL
GHGLPLAVGT ALGLRAQGLT DPAVWVLVGD AEFDEGSNGE AVAFAGAYGL DRLHVVVIDN
SSATHGWRGG IAARFEAEGW SAATVDGRDH EALHRAFTAE HPGRPHVVVA RVEPKDS
//