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Database: UniProt
Entry: A7A5N6_BIFAD
LinkDB: A7A5N6_BIFAD
Original site: A7A5N6_BIFAD 
ID   A7A5N6_BIFAD            Unreviewed;       702 AA.
AC   A7A5N6;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   Name=tkt {ECO:0000313|EMBL:EDN82874.1};
GN   ORFNames=BIFADO_01156 {ECO:0000313|EMBL:EDN82874.1};
OS   Bifidobacterium adolescentis L2-32.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=411481 {ECO:0000313|EMBL:EDN82874.1, ECO:0000313|Proteomes:UP000003773};
RN   [1] {ECO:0000313|EMBL:EDN82874.1, ECO:0000313|Proteomes:UP000003773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-32 {ECO:0000313|EMBL:EDN82874.1,
RC   ECO:0000313|Proteomes:UP000003773};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDN82874.1, ECO:0000313|Proteomes:UP000003773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-32 {ECO:0000313|EMBL:EDN82874.1,
RC   ECO:0000313|Proteomes:UP000003773};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bifidobacterium adolescentis (L2-32).";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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:EDN82874.1}.
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DR   EMBL; AAXD02000028; EDN82874.1; -; Genomic_DNA.
DR   RefSeq; WP_003809218.1; NZ_DS264455.1.
DR   AlphaFoldDB; A7A5N6; -.
DR   GeneID; 56675072; -.
DR   HOGENOM; CLU_009227_0_0_11; -.
DR   Proteomes; UP000003773; Unassembled WGS sequence.
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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDN82874.1}.
FT   DOMAIN          374..556
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   702 AA;  76085 MW;  7EDFD1B78F44BBE8 CRC64;
     MTEFKETELD ERAIKMAKVL SADAVERAGH GHPGSPVSLA PIAYTLYQHF IKHDPNDPNW
     EGRDRFILSG GHASLTQYVQ LYFSGYGLTL DDLKNFRGGA DTRTPGHPEY GLTPGIEMTT
     GPLGQGFASA IGFAYGQRFQ RGLLDPEAPE GESPFDHNIW VICGEGDIEE GISGEAASLA
     ANQQLGNLTV IFDANRIQIE GDTNLVLAED VLKRFQAYGW YTDEFSFIQP DGSYKEDVEG
     LADTIAKARA AAPNQPKLIK VDTLIAWPTP GKTNDPSSHG SKLGAEAVAG LKKLLGYDPE
     ESFHVDEEAL AHARKVAERG LEAHKEWDEK YNAWRKANPD KAALYDRIKA GELPEGFDKA
     IDDLEATFEV GKNVATRGAS GSTLNAIAAV MPELWGGSAD LGGSNKTDLK GAETFAPAEC
     ATKQWPNCSK YGRQLHFGVR EFTMGTITNG ILLGSHTRPY GGTFFMFSDY ERSAVRLAAL
     MQIPNLYVWS HDSVAVGEDG PTHQPVEHLA SFRAIPQLEV ARPADAYETA EAYRYFFEKK
     NTLPTAMVLT RQGVPVLAET AEKAKDGVKK GAYVLVDTEG TPDVIIMATG SEVQWAVSAA
     KTLAGEGIKA RVVSVPCVEW FEEQDAEYKE AVLPAAVKAR VSVEAGVAMP WYKYLGSYGK
     PVSIEQFGLQ GDGAQNMIDL GITAEHVVEA AKASIAEVEA AK
//
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