ID A0A087DI04_9BIFI Unreviewed; 702 AA.
AC A0A087DI04;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=BSCA_0972 {ECO:0000313|EMBL:KFI95154.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI95154.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI95154.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI95154.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI95154.1}.
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DR EMBL; JGZO01000004; KFI95154.1; -; Genomic_DNA.
DR RefSeq; WP_034535414.1; NZ_JGZO01000004.1.
DR AlphaFoldDB; A0A087DI04; -.
DR STRING; 158787.BSCA_0972; -.
DR eggNOG; COG0021; Bacteria.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000029033; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029033};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFI95154.1}.
FT DOMAIN 374..556
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 702 AA; 76181 MW; C20D362E37236B02 CRC64;
MTEFKETELD ERAIKMAKVL SADAVEKAGS GHPGSLVSLA PVAYTLYQHF IKHDPNDPNW
EGRDRFILSG GHASLTQYVQ LYFSGYGVTL DDLKYFRGGA DTRTPGHPEY GLTPGIEMTT
GPLGQGFASA IGFAYGERFQ RGLLDPDTPK EESPFYHKIW AICGEGDIEE GISGEAASLA
ANQKLGNLTV IFDANRIQIE GDTNLVLAED VLKRFQAYGW YTDEFSFIQP DGSYKEDVEG
LADVIAKAEK AAPDQPKLIK VHSLIAWPTP GKTNDPSSHG SKLGAEAVAG LKKVLGYDPE
ESFHVDEEAL AHARKVAERG LEAHKEWDEK FDAWRKANPD KAALYDRLKA GELPEGFDKA
LDDLEATFEV GKKVATRGAS GSVLNAIAAV MPELWGGSAD LGGSNKTDLK GAATFAPAEC
ATKQWPVCNE FGRQLHFGVR EFTMGCITNG ILLGSHTRPF GGTFFMFSDY ERSAVRLAAL
MEIPNLYIWS HDSVAVGEDG PTHQPVEHLA SFRAIPQLEV IRPADAFETA EAYRYFFEKK
NTLPGAMILT RQGVPVLAET ADKAKDGVRK GAYVLVDTEG TPDVILMASG SEVQWAVEAA
KTLAGKGVKA RVVSVPSMEW FEEQDAEYKE AVLPAAVKAR VSVEAGVAMP WYKYLGTYGK
PVSIEQFGLQ GDGAQNMIDL GITAEHVVEA AEASIAEVEA AK
//