ID   A0A220S9M3_9FLAO        Unreviewed;       810 AA.
AC   A0A220S9M3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:ASK29915.1};
GN   ORFNames=CEY12_07265 {ECO:0000313|EMBL:ASK29915.1};
OS   Chryseobacterium sp. T16E-39.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=2015076 {ECO:0000313|EMBL:ASK29915.1, ECO:0000313|Proteomes:UP000198250};
RN   [1] {ECO:0000313|EMBL:ASK29915.1, ECO:0000313|Proteomes:UP000198250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T16E-39 {ECO:0000313|EMBL:ASK29915.1,
RC   ECO:0000313|Proteomes:UP000198250};
RA   Lee S.A., Weon H.-Y.;
RT   "Complete genome of Chryseobacterium sp. T16E-39 isolated from tomato
RT   (Solanum lycopersicum L.) root endosphere.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP022282; ASK29915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A220S9M3; -.
DR   KEGG; chry:CEY12_07265; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000198250; Chromosome.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00676; E1_dh; 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); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          476..650
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   810 AA;  91003 MW;  C2019D202C113BF2 CRC64;
     MQTTYIETQK ISFQDFKNQI LEDYKLGRIS REMSYLGRRE VLTGKAKFGI FGDGKELPQL
     AMAKVFRNGD FRSGYYRDQT FALSVDALTV ESFFAQLYAD TSVEREPASA GRQMNGHFAT
     RSLNEDGSWK NLMAQKNISS DISPTAGQMP RLLGLAQASK IYKSVQFDGS EKFSKDGNEI
     AFGTIGDAST AEGHFWETLN AACALQVPMI VSIWDDGYGI SVPTKNQRAK ADISEMLSGF
     QRKEGENQGC EIIQVKAWDY PALLDAYARA EHFARTESVP VVVHVIEVTQ PQGHSTSGSH
     ERYKNEERLS WEADFDGLVK FKEWILNYSI EIEGKEEVIA TKEELDAIDE EAKKMVKAGQ
     KIAWENYQKT ILDLSKAVLP LVENLKGQNS EIENYITQFN KLVSKAKKDI FHLMRKSLLA
     TRGTNTAERN QLMQKYNEVF EVEKDNYSSH LYSQSQWKAE NIKEVKPVYS DHSEDVDGRV
     VVRNNFDKIF EKYPETLVFG EDAGNIGDVN QGLEGMQEKY GDVRVADTGI REATILGQGI
     GMAMRGLRPI AEIQYLDYIL YCIQGMSDDL ATVQYRTKGG QKAPVIIRTR GHRLEGVWHS
     GSPMAGILNL SKGILVLVPR NLTKAAGFYN TMLQSDDPAV IVECLNGYRL KEKQPDNLGE
     FTVPVGKIEV TKEGKDVTLV TYGSTWRIVM EAAEELEKLG ISSEVIDVQS LIPFDLTNEI
     AESVKKTNRL VVIDEDVEGG TSAFILQQIL EKQKAFRYLD SDPLTIAAND HRPAYASDGD
     YFSKPSSDDM VEKIYAMFNE TNPQKYPAIF
//