ID   K1LJG7_9FLAO            Unreviewed;       808 AA.
AC   K1LJG7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   ORFNames=HMPREF9699_01173 {ECO:0000313|EMBL:EKB56890.1};
OS   Bergeyella zoohelcum ATCC 43767.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Bergeyella.
OX   NCBI_TaxID=883096 {ECO:0000313|EMBL:EKB56890.1, ECO:0000313|Proteomes:UP000006085};
RN   [1] {ECO:0000313|EMBL:EKB56890.1, ECO:0000313|Proteomes:UP000006085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43767 {ECO:0000313|EMBL:EKB56890.1,
RC   ECO:0000313|Proteomes:UP000006085};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bergeyella zoohelcum ATCC 43767.";
RL   Submitted (JUL-2012) 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:EKB56890.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGYA01000023; EKB56890.1; -; Genomic_DNA.
DR   RefSeq; WP_002663218.1; NZ_JH932293.1.
DR   AlphaFoldDB; K1LJG7; -.
DR   STRING; 883096.HMPREF9699_01173; -.
DR   PATRIC; fig|883096.3.peg.1208; -.
DR   eggNOG; COG0022; Bacteria.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_350462_0_0_10; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000006085; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006085}.
FT   DOMAIN          475..649
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   808 AA;  90437 MW;  55DC7CB02BFD7D68 CRC64;
     MQDKIATEKV SFEDIKRDVL HDYKLGRISR EMSLLGRREV LTGKAKFGIF GDGKELPQLA
     MAKVFREGDW RSGYYRDQTF ALAVDALTVE SFYAQLYADT SVEREPASAG RQMNGHYATR
     TLNEDGSWKD LTQIKNISSD ISPTAGQMPR LLGLAQASKV FKEIQFEGAE KFSKGGREVA
     FGTIGDASTA EGHFWETLNA ACALQVPMIV SIWDDGYGIS VPTHNQRAKV DIAEMLSGFQ
     RNEGETQGCE IIQVKAWDYP ALLDAYSRAE YFAREESCPV VVHVIEVTQP QGHSTSGSHE
     RYKSEERLSW EAEHDGLLKF REWILNYSAE LDGKEISIAT ADELDEIDRE AKKIVKDGQK
     KAWDSYQKTI TDLKNELLPL VEALANESTE VSGEITKFKN LVTVAKKEVF HLVRKALIHT
     RGKNSSAREA LQKAYERLFD IEKDNYSSHL YSQSQWKATE VPVVEPIYSD SSEEMDGRMV
     IRNNFDKIFE KYPQTLVFGE DSGNIGDVNQ GLEGMQEKYG ATRVADTGIR EATILGQGIG
     MAMRGLRPIA EIQYLDYILY CLQGMSDDLA TVHYRTKGGQ KAPVIIRTRG HRLEGIWHSG
     SPMAGILNLS KGINILVPRS LTKAAGFYNT MLQSDEPCVI VECLNGYRLK ETQPDNIGEF
     TVPVGKIEIT KEGTDVTLVT YGSTWRIVTE AAKELETLGI SAEVIDVQSL IPFDLTNEIA
     ESVKKTNRLV VIDEDVEGGT SAFIMQQIIE KQKAFRYLDS DPITISAENH RPPYASDGDY
     FSKPSADDIV EKVYALFHES NPVKFPKL
//