ID   A0A1Y1RHR2_9BACT        Unreviewed;       646 AA.
AC   A0A1Y1RHR2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=B6244_06625 {ECO:0000313|EMBL:OQY28621.1};
OS   Candidatus Cloacimonetes bacterium 4572_55.
OC   Bacteria; Candidatus Cloacimonadota.
OX   NCBI_TaxID=1971726 {ECO:0000313|EMBL:OQY28621.1, ECO:0000313|Proteomes:UP000192623};
RN   [1] {ECO:0000313|Proteomes:UP000192623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) 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:OQY28621.1}.
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DR   EMBL; NBMB01000020; OQY28621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1RHR2; -.
DR   STRING; 1971726.B6244_06625; -.
DR   Proteomes; UP000192623; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          336..507
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          233..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  70955 MW;  DCF1C5A5B74741F8 CRC64;
     MIEKSKSGHP GAAMALAPAA YLLYSRFLKH NPKNPDWLNR DRFILSCGHV SVLLYSTLHL
     SGYSISLDDL KNFRQWRSIA AGHPEQGLAP GVETTSGPLG QGCAASVGMA IAETHLADRF
     NTRDHTVVDH HTWVLCSDGD MMEGVSHEAA SLAGHLRLGK LIWIYDDNRV TIDGPTSISL
     SDDTDKRFEA CGWHVQSVQD VNDLPLLAQA MSRAKNETQR PSLIRVRTHI GFGAPNKQDR
     SAAHGSPLGS DETKATKIAY GWDSDEPFHI PTEISNHCLQ AISRGEQAEI DWLATLKQWR
     TANPLLASEW DRTLLGDLPD NWDRDIPLFP PDEKGSGTRI SSWKILNAIA PHIPELIGGS
     ADLAASVKSN MTKCRDFSAE NRGGRNLHFG IREHAMAAIL NGVSLHRGLR PFGSTFLVFS
     DYMRPSIRLA ALMKLPVIYI WSHDAINIGE DGPTHQPVEH LAALRSIPGL TIIRPADANE
     TVAAWRVIIK SRSGPVGLIL TRQNAPTLSE TMGKSEQGVA HGAYILSEPE GDGDLDAIII
     ATGYEVHLAL AAQKKMQDHG TSVRVVSMPS WELFDLQSKD YRERVLPPNT RKLAIEAGVE
     QGWWKYVGDK GDVLCLNRFG ASAPESVVYK KLGFHVDRVI GKITKT
//