ID A0A124FRK9_9BACT Unreviewed; 648 AA.
AC A0A124FRK9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Transketolase domain-containing protein {ECO:0000313|EMBL:KUK59455.1};
GN ORFNames=XD80_0097 {ECO:0000313|EMBL:KUK59455.1};
OS Synergistales bacterium 53_16.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635273 {ECO:0000313|EMBL:KUK59455.1, ECO:0000313|Proteomes:UP000053116};
RN [1] {ECO:0000313|Proteomes:UP000053116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK59455.1}.
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DR EMBL; LGGB01000002; KUK59455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FRK9; -.
DR PATRIC; fig|1635273.3.peg.1699; -.
DR Proteomes; UP000053116; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 330..500
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 648 AA; 70711 MW; 259CF4F8B30179B2 CRC64;
MNALKTKLEG FSEEVSRPEL IEQLREAGRL CRISAITMTS VAGSGHPAGS LSSMEMCLIT
YGVARIGDCK YENAGIDKVV VSHGHISPAV YSVLAFYGYI PTDEVLAFFR KAGSPYQGHV
VRQIPQIAWS TGNLGQGLAA GVGFALAKKT REEDGRIYVL MGDGEQVKGQ VAEARRIARH
YDLSNITVLI DLNNIQISGK TETIMKADVR RLWEADGWEV TDVDGHDPSG LYGALKKASL
SKIPQVLLCH TLMGKGVSFM EGLPDYHGKA LNDEEYVPAI KELGGDPAMI EKYRKRRKEL
PVPSGRLSVP PLATSLEGGK PREYKADDLI DCRSAFGKAL SDIGEANYKK EGKGPLLVFD
CDLADSVKVS EFAKKYPEWF LEMGIQEHAT ATVAGAASIA GCISLWADFG VFGASEAYNQ
QRLNDINDTN LKLALTHVGL DVGEDGETHQ CIDYIGLFRN LFGWKLLVPA DGNQADRMTR
YALTTQGNIC LAMGRSKLPV ITDEDGKPFF GGDYVFRYGK ADLLRNGKDA AIICCGHMVY
RALSAWEKLV RMGISAKVYH FGCPLAIDRE AVLDAAETGL IVTCEDHNRE SGLGSQVATV
LAEERASTRL VRMGVHRYGD SGKSVEVMER MGLSVDDLVR TVSSFLEE
//
