ID A0A1J4UA05_9BACT Unreviewed; 773 AA.
AC A0A1J4UA05;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=AUJ23_00970 {ECO:0000313|EMBL:OIO20115.1};
OS Candidatus Magasanikbacteria bacterium CG1_02_32_51.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1805238 {ECO:0000313|EMBL:OIO20115.1, ECO:0000313|Proteomes:UP000181941};
RN [1] {ECO:0000313|EMBL:OIO20115.1, ECO:0000313|Proteomes:UP000181941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_32_51 {ECO:0000313|EMBL:OIO20115.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO20115.1}.
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DR EMBL; MNVC01000012; OIO20115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4UA05; -.
DR STRING; 1805238.AUJ23_00970; -.
DR Proteomes; UP000181941; 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 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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 423..607
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 773 AA; 85074 MW; 0E1A0ECF1A886A84 CRC64;
MSYNLLDKAD FEKFKKNNPS NFQYDFEGGS YLKLQDLELN GLSGIDEEKL NKIATLMREL
IFATVEGSRS GHPGGSSAKV EQFLAMTLGG AMAFDLLDPK NNCRDRVVWS AGHCTPGLYS
GLALFYESLQ KKGIKFDVKK LHAILGKDLS KFRKGGGLPG HAESYTPLSD ISTGPSGHGF
SAAGGLAITH KSSGTGSKVW VFMGDAESEE GMTYEARNIL HTVGADNMIV SLDYNHFGID
GDIDEVLSNK YINNWLGLGW NVIEINGHNI LECVYAYRLT SEKVFANGNP TVVIAHTWKG
KSYGSLENSN KSHGSQVKHD EYIEIENKLN ANNKVSIPGK EGDILSDIES ILSNLDNSLA
TYIVGRLKVA SKKIPNEQKV LVQMKKTLKF VKGGSTRKFK SVTEIERPSK LPAELVFVPE
QKVATRKSSQ VFFEWLMKES AFFWAGAGDL SESVKTDKAE NVYGVINRKN PYGRGIRYGI
AEQNMGMMGA GMTLDRLPGN FAPVSVIGTY AAFTSMMCNG IRVAVINNHL YPEHKGFFIV
LASHDGPEVG EDGPTHQGLY WMSMYSAYPG IKVYKPTDAN ETIEMLFYAM KIGEPIILSV
SRPDVLVLKR GKNACCGQFV PQAKEAVQGA YIFKDYKNNG NNKMCVAVSG AIVLNNLLQI
LPDLEKEKID IKVVVVTSPE LFAEFKKKNK KKADSIFSKE DRKVGVTLHA GWKGFLRDFV
DNDFYSAKGG SASGGEERSI GLETYLASGS VDEVYEMAKL TSLDIKKKIL EIK
//
