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Database: UniProt
Entry: A0A0C1F732_9FLAO
LinkDB: A0A0C1F732_9FLAO
Original site: A0A0C1F732_9FLAO 
ID   A0A0C1F732_9FLAO        Unreviewed;       317 AA.
AC   A0A0C1F732;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:KIA87693.1};
GN   ORFNames=OA85_09075 {ECO:0000313|EMBL:KIA87693.1};
OS   Flavobacterium sp. AED.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA87693.1, ECO:0000313|Proteomes:UP000031403};
RN   [1] {ECO:0000313|EMBL:KIA87693.1, ECO:0000313|Proteomes:UP000031403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AED {ECO:0000313|EMBL:KIA87693.1,
RC   ECO:0000313|Proteomes:UP000031403};
RA   Gale A.N., Newman J.D.;
RT   "Flavobacterium sp. AED Genome.";
RL   Submitted (OCT-2014) 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:KIA87693.1}.
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DR   EMBL; JSYM01000001; KIA87693.1; -; Genomic_DNA.
DR   RefSeq; WP_035667569.1; NZ_JSYM01000001.1.
DR   AlphaFoldDB; A0A0C1F732; -.
DR   STRING; 1423323.OA85_09075; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000031403; 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;
FT   DOMAIN          10..175
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   317 AA;  34114 MW;  6A143873F8E416CC CRC64;
     MKKYTNTGSK DTRSGFGAGM TELGQTNENV VALCADLIGS LKFDDFKKNH PERFFQIGIA
     EANMIGIAAG LTIGGKIPFT GTFANFSTGR VYDQIRQSVA YSEKNVKICA SHAGLTLGED
     GATHQILEDI GLMKMLPGMT VINTCDYNQT KAATLAIADH HGPVYLRFGR PVVPNFMPSD
     EPFVIGKAIV LNEGADVTIV ATGHLVWEAL IAAEALEAKG ISAEVINIHT IKPLDEEAIL
     KSLAKTKCIV TAEEHNILGG LGESVSRVLA LNNPAPQEFV AVNDSFGESG TPEQLMEKYK
     LNNQAIVEAV ERVIKRK
//
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