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Database: UniProt
Entry: A0A1M5YRB0_9VIBR
LinkDB: A0A1M5YRB0_9VIBR
Original site: A0A1M5YRB0_9VIBR 
ID   A0A1M5YRB0_9VIBR        Unreviewed;       314 AA.
AC   A0A1M5YRB0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000313|EMBL:SHI14113.1};
DE            EC=2.2.1.7 {ECO:0000313|EMBL:SHI14113.1};
GN   Name=dxs_1 {ECO:0000313|EMBL:SHI14113.1};
GN   ORFNames=VA7868_01897 {ECO:0000313|EMBL:SHI14113.1};
OS   Vibrio aerogenes CECT 7868.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI14113.1, ECO:0000313|Proteomes:UP000184608};
RN   [1] {ECO:0000313|EMBL:SHI14113.1, ECO:0000313|Proteomes:UP000184608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI14113.1,
RC   ECO:0000313|Proteomes:UP000184608};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQXZ01000016; SHI14113.1; -; Genomic_DNA.
DR   RefSeq; WP_073603605.1; NZ_FQXZ01000016.1.
DR   AlphaFoldDB; A0A1M5YRB0; -.
DR   STRING; 1216006.VA7868_01897; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000184608; Unassembled WGS sequence.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
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:UP000184608};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000313|EMBL:SHI14113.1}.
FT   DOMAIN          1..170
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   314 AA;  33349 MW;  F44F7F5686FCEEEA CRC64;
     MANAEHFANI MVERFIEAVN RGVDLVPVVA DSTSTAKIAP FIEAFPDRLV NVGIAEQALV
     GTAAGLALGG KVAVTCNAAP FLISRANEQV KVDVCYNNTN VKLFGLNSGA SYGPLASTHH
     SIDDISVMRG FGNIEIYAPA SPKQCRQIID YAIEKQGPVY IRMDGKPLPE IFSDSYQFEP
     GRVDVIAEGE EIALIGMGSV MHEVAEAAAT LNASGVSAKA ICLSSIRPCD TDELARQLTG
     IRFAVTVEEH NVNGGVGAMV AEVIAEFDTG TRLKRLGIHD GAYALAGDRQ SMRAYHGIDA
     GSVVDTALNL LREK
//
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