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Database: UniProt
Entry: A0A3M8FQB9_9FLAO
LinkDB: A0A3M8FQB9_9FLAO
Original site: A0A3M8FQB9_9FLAO 
ID   A0A3M8FQB9_9FLAO        Unreviewed;       317 AA.
AC   A0A3M8FQB9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=Transketolase family protein {ECO:0000313|EMBL:RNC80156.1};
GN   ORFNames=ED556_13680 {ECO:0000313|EMBL:RNC80156.1};
OS   Winogradskyella sp.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1883156 {ECO:0000313|EMBL:RNC80156.1, ECO:0000313|Proteomes:UP000278005};
RN   [1] {ECO:0000313|EMBL:RNC80156.1, ECO:0000313|Proteomes:UP000278005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin3 {ECO:0000313|EMBL:RNC80156.1};
RA   Zheng Q., Wang Y., Jiao N.;
RT   "Metagenomics and metaproteomics analyze the interactions between
RT   Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT   Synechococcus culture.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RNC80156.1}.
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DR   EMBL; RHLG01000007; RNC80156.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8FQB9; -.
DR   Proteomes; UP000278005; 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; 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   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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000278005}.
FT   DOMAIN          10..175
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   317 AA;  34106 MW;  54DC1D3F140C8136 CRC64;
     MKTYENTGNK DTRSGFGAGL TELGKTNENV VALCADLTGS LKMDEFKNNH PERFFQVGIA
     EANMIGIAAG MTIGGKVPFT GTFANFSTGR VYDQIRQSVA YSDKNVKICA SHAGITLGED
     GATHQILEDI GLMKMLPGMT VINTCDFNQT KAATLAIAEH HGPVYLRFGR PKVPNFTPEN
     QNFEIGKAVK LTDGNDVTIV ATGHLVWEAL EAAKALDSEG ISAEVINIHT IKPLDSEAII
     QSVSKTKCIV TAEEHNHLGG LGESVARVLS QHQPTPQEYV ATNDTFGESG TPAQLMDKYG
     LNSKAIIEAS KKVIKRK
//
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