ID Q8G6C8_BIFLO Unreviewed; 702 AA.
AC Q8G6C8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:AAN24535.1};
GN OrderedLocusNames=BL0716 {ECO:0000313|EMBL:AAN24535.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24535.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN24535.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; AE014295; AAN24535.1; -; Genomic_DNA.
DR RefSeq; NP_695899.1; NC_004307.2.
DR RefSeq; WP_011068109.1; NC_004307.2.
DR AlphaFoldDB; Q8G6C8; -.
DR SMR; Q8G6C8; -.
DR STRING; 206672.BL0716; -.
DR EnsemblBacteria; AAN24535; AAN24535; BL0716.
DR KEGG; blo:BL0716; -.
DR PATRIC; fig|206672.9.peg.415; -.
DR HOGENOM; CLU_009227_0_0_11; -.
DR OrthoDB; 8732661at2; -.
DR PhylomeDB; Q8G6C8; -.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000439};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..556
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 702 AA; 75915 MW; 7D6F2F6CFEB7CA7E CRC64;
MTEFKETELD ERAIKMAKVL SADAVEKAGS GHPGSPISLA PVAYTLYQHF IKHDPNDPNW
EGRDRFILSG GHASLTQYVQ LYFSGYGVTL DDLKNFRGGA ATRTPGHPEY GLTPGIEMTT
GPLGQGFASA IGFAYGERFQ RGLLDPETPK EDSPFYHKIW AICGEGDIEE GISGEAASLA
ANQKLGNLTV IFDANRIQIE GDTNLVLAED VLKRFQAYGW YTDEFSFIQP DGSYKEDIEG
LADVIAKAEK AAPDQPKLIK VHSLIAWPTP GKTNDPSSHG SKLGTEAVAG LKEALGYDPE
ENFHVDEEAL AHARKVAERG LEAHKEWDEK FDAWRKANPD KAALYDRLKA GELPEGFDKA
LDDLEATFEV GKGVATRGAS GSVLNAIAAV MPELWGGSAD LGGSNKTDLK GAATFAPAEC
ATKQWPNCNE FGRQLHFGVR EFTMGCITNG ILLGSHTRPF GGTFFMFSDY ERSAVRLAAL
MEIPNLYIWS HDSVAVGEDG PTHQPVEHLA SFRAIPQLEV IRPADAFETA EAYRYFFEKK
NTLPGAMVLT RQGVPVLAET AAKAKDGVKK GAYVLVDTEG TPDVILMASG SEVQWAVAAA
KTLAGEGVKA RVVSVPSMEW FEEQDAEYKE AVLPAAVKAR VSVEAGVAMP WYKYLGSYGK
PVSIEQFGLQ GDGAQNMIDL GITAEHVVEA AKASIAEVEA AK
//
