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Database: UniProt
Entry: A0A087DI04_9BIFI
LinkDB: A0A087DI04_9BIFI
Original site: A0A087DI04_9BIFI 
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
//
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