ID E0NEN2_PEDAC Unreviewed; 658 AA.
AC E0NEN2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:EFL96043.1};
GN ORFNames=HMPREF0623_0094 {ECO:0000313|EMBL:EFL96043.1};
OS Pediococcus acidilactici DSM 20284.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL96043.1, ECO:0000313|Proteomes:UP000004470};
RN [1] {ECO:0000313|EMBL:EFL96043.1, ECO:0000313|Proteomes:UP000004470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL96043.1,
RC ECO:0000313|Proteomes:UP000004470};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) 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:EFL96043.1}.
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DR EMBL; AEEG01000002; EFL96043.1; -; Genomic_DNA.
DR RefSeq; WP_004165655.1; NZ_GL397067.1.
DR AlphaFoldDB; E0NEN2; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_9; -.
DR Proteomes; UP000004470; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UP000004470};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFL96043.1}.
FT DOMAIN 347..518
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 658 AA; 71850 MW; B3BA28B6670D46BA CRC64;
MFTKKDIDAV NAIRFLSADM IEKAQSGHPG LPIDAAPMAY TLWEKFLQFN PQDPKWINRD
RFVLSAGHGS AMLYSLLHLN GFDLPLTELK KFRKLGSRTP GHPEYGMTAG VDATTGPLGQ
GLGMAVGMAM AERHLAALVN RPGYPVFNHF TYALVGDGDL MEGVSQEAIN IAGQKQLNKL
IVLYDSNDVS LDGPLSLSTN ENVAQRFKAA NWNYQKVTDG NDLAGLQQAL QQAQTSDRPT
LIEVKTIIGY GTPESGTNKV HGNALGKANL AAMRQFYHWQ AAPFEIAPEI YQHYQEQVAK
KQTAYQAWQT MFQEYQTEFP EVYRQFQDAR LDTTKLNLDD PAWQEPMATR TSNSKIMQQV
ADQNVQLWGG SADLYSSNNT HLDDSKAFDA LHPEQRNVYF GVREFGMATA VNGINLHGNT
RAFGSTFFVF SDYLKAAIRL AAIQQIPAVY IFTHDSIAVG EDGPTHEPIE QLAGLRSIPN
VTVIRPADAH EVLGAWQKIG QITDQPTVLV LTRQKVPLLA QTQTDKVAFG GYTLSPAATA
NPDGILVATG SEVALALQAQ QKLAQEKLNV AVVSMPSVEL FQAQSSDYQA QVLPPNVKVK
IGLEMGSRNG LATVASAVIG IDHFGASGNG TEVVQQAGFT VDNIAEQFKA KLAEAEVK
//
