ID A0A099BXP2_9BACT Unreviewed; 673 AA.
AC A0A099BXP2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KGI60228.1};
GN ORFNames=HMPREF0671_07130 {ECO:0000313|EMBL:KGI60228.1};
OS Prevotella sp. S7 MS 2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI60228.1, ECO:0000313|Proteomes:UP000029732};
RN [1] {ECO:0000313|EMBL:KGI60228.1, ECO:0000313|Proteomes:UP000029732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI60228.1,
RC ECO:0000313|Proteomes:UP000029732};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-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 -!- 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:KGI60228.1}.
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DR EMBL; JRPT01000033; KGI60228.1; -; Genomic_DNA.
DR RefSeq; WP_036898589.1; NZ_JRPT01000033.1.
DR AlphaFoldDB; A0A099BXP2; -.
DR eggNOG; COG0021; Bacteria.
DR Proteomes; UP000029732; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 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; PS00801; TRANSKETOLASE_1; 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:UP000029732};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 353..535
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 673 AA; 73382 MW; D4756CD7A5C58165 CRC64;
MNDKTLMNHA ADNIRILAAS MVEKANSGHP GGAMGGADFI NVLFSEFLVY DPEDPTWTGR
DRFFLDPGHM SPMLYAALAL QGKFTIDELM QFRQWGSPTP GHPELDVKRG IENSSGPLGQ
GHALAAGAAV AEKFLEARLG HTMMQHKVYA YISDGGIEEE ISQGVGRIAG TLGLNNLIMF
YDANEIQLST EYAEVSSEDT EAKYKAWNWN VIKINGNDPD AIREALTIAN QEDSKPTLII
GKTVMGKGAL QNDGSSYERN VKTHGAPLGG DAYRNTINNL GGNPDNPFIV FDDVKELYAN
RKKQLKEIVV IRKQAEAAWA AANPDKAAMM KEWFSGKAPQ VDWSKLEEPK AGSATRVASA
ACLKVLAQQV PNMICASADL SNSDKTDGFL KETHSMKHGD FSGAFFQAGV SELTMADMCI
GMMLHGGVIT AMGTFFVFSD YMKPAIRLAA LMGTPVKFIW SHDAFRVGED GPTHEPVEQE
AQIRLMEKLK NHKGLDSVRV FRPADAKETT VCWQMAMENM STPTALIFSR QGINPLPEGT
NYEEARKGAY IVANSDEDFD VVLLASGSEV STLVEGSNKL KQDGIKVRIV SVPSEGLFRN
QSKEYQESIL PTDAKKFGMT AGLPVTLEGL VGANGKVFGL ESFGFSAPYK VLDEKLGYTG
ENVYNQVKQL LAE
//