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Database: UniProt
Entry: A0A0S8E3B4_9BACT
LinkDB: A0A0S8E3B4_9BACT
Original site: A0A0S8E3B4_9BACT 
ID   A0A0S8E3B4_9BACT        Unreviewed;       307 AA.
AC   A0A0S8E3B4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=AMJ78_03145 {ECO:0000313|EMBL:KPK42269.1};
OS   Omnitrophica WOR_2 bacterium SM23_29.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK42269.1, ECO:0000313|Proteomes:UP000050824};
RN   [1] {ECO:0000313|EMBL:KPK42269.1, ECO:0000313|Proteomes:UP000050824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_29 {ECO:0000313|EMBL:KPK42269.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK42269.1}.
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DR   EMBL; LJUB01000020; KPK42269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8E3B4; -.
DR   PATRIC; fig|1703776.3.peg.1731; -.
DR   Proteomes; UP000050824; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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   PANTHER; PTHR43825:SF5; HYPOTHETICAL TRANSKETOLASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          1..163
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   307 AA;  34263 MW;  136B6E88A0DC9213 CRC64;
     MRNSVIKTIM NYSKRNNKIF FITGDAGYGV LDKYKENFPD RFLNLGVAEQ NMISFASGLS
     LAGYKVFVYN IIPFVLYRCY EQVRNDICYQ DLPVTLIGVG SGITYAPQGA THYSVEDIAL
     ARTLPNLIIL SPSDSVEAEK CAEFSLRCKS PVYIRIAKSG EPIIHKQGIK SISEPIIVNE
     GSEVGILFHG SIGSEVISAL KCLKRTPKVI SLPMLQPLNF DFLLSNLEGI HTLITVEEHF
     IEGGLGSIIE GWVVKNMLNF RVKKLGIKNE FIHAINNPAG MRNLYGISCN KIIRTVEKAF
     LNFTFKK
//
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