ID A0A066WRJ5_9FLAO Unreviewed; 793 AA.
AC A0A066WRJ5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:KDN56396.1};
GN ORFNames=FEM21_04150 {ECO:0000313|EMBL:KDN56396.1};
OS Flavobacterium seoulense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1492738 {ECO:0000313|EMBL:KDN56396.1, ECO:0000313|Proteomes:UP000027064};
RN [1] {ECO:0000313|EMBL:KDN56396.1, ECO:0000313|Proteomes:UP000027064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1321 {ECO:0000313|EMBL:KDN56396.1,
RC ECO:0000313|Proteomes:UP000027064};
RA Shin S.-K., Yi H.;
RT "Genome Sequence of Flavobacterium sp. EM1321.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KDN56396.1}.
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DR EMBL; JNCA01000003; KDN56396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066WRJ5; -.
DR STRING; 1492738.FEM21_04150; -.
DR PATRIC; fig|1492738.3.peg.411; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR Proteomes; UP000027064; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
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 459..633
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 793 AA; 88796 MW; 0B67E18FF029A257 CRC64;
MTFEDFKTEV LNDYKIAVTS RECSLLGRRE VLSGKAKFGI FGDGKEVPQI AMAKFFRNGD
FRSGYYRDQT FMMAIGELTV ANFFAGLYGN TDIKQEPMSA GRQMGGHFVT HSLNDDGSWK
DLTKQKNSSS DISPTAAQMP RLLGLAQASK VYREINNIPN QKKFSNQGNE IAWGTIGNAS
TSEGLFFETI NAAGVLQVPM LISIWDDEYG ISVHARHQTT KENISEILSG FQRDKNNDGI
EIMTVKGWDY SDLITTYEKA AAITREEHVP VLVHVTELTQ PQGHSSSGSH ERYKSTERLN
WEREFDCLRQ MRLWMIAINI ASAEELNELE ANIKKEVLEA KKTAWNSFIA PIVTEKNDLI
SILEKIGPSS KNKDHILKLS NALKAIKDPL KKEILVTARK SLRLVVNENG AEELSLWIQK
YTQINQARFS DNLYSESKNN VFSVKEVLPT YAEDVKNDTD GRMIIRDNFD ALFTKHPDVL
IFGEDSGNIG DVNQGLEGMQ EKYGETRVAD VGIREATIIG QGIGLALRGL RPIAEIQYLD
YLLYAIQIMS DDLASLQYRT VGKQKAPLII RTRGHRLEGI WHSGSPMGMI INAIRGIHVL
VPRNMTKAAG FYNTLLDCDE PALVIECLNG YRLKEKAPLN LGEFKTPIGV VETIRTGTDI
TLVSYGSTLR LVEQAAKELA ETGIDCEIID IQSLLPLDVN HDIVKSVQKT NRLLVIDEDV
PGGASAYILQ QIIEKQDAFK YLDSKPQTLS AKEHRPSYGT DGDYFSKPSI EDVYEKVYAI
LSEASPTKYP KLY
//