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Database: UniProt
Entry: A0A135I4K2_9GAMM
LinkDB: A0A135I4K2_9GAMM
Original site: A0A135I4K2_9GAMM 
ID   A0A135I4K2_9GAMM        Unreviewed;       335 AA.
AC   A0A135I4K2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KXF80381.1};
GN   ORFNames=ATN88_22405 {ECO:0000313|EMBL:KXF80381.1};
OS   Enterovibrio coralii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Enterovibrio.
OX   NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF80381.1, ECO:0000313|Proteomes:UP000070529};
RN   [1] {ECO:0000313|EMBL:KXF80381.1, ECO:0000313|Proteomes:UP000070529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF80381.1,
RC   ECO:0000313|Proteomes:UP000070529};
RA   Gomez-Gil B., Enciso-Ibarra J.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (NOV-2015) 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:KXF80381.1}.
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DR   EMBL; LNTY01000054; KXF80381.1; -; Genomic_DNA.
DR   RefSeq; WP_067419396.1; NZ_LNTY01000054.1.
DR   AlphaFoldDB; A0A135I4K2; -.
DR   STRING; 294935.ATN88_22405; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000070529; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_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; PTHR43257:SF3; ACETOIN:2,6-DICHLOROPHENOLINDOPHENOL OXIDOREDUCTASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 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   Pyruvate {ECO:0000313|EMBL:KXF80381.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070529};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          5..189
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   335 AA;  35658 MW;  790474A733D1DA47 CRC64;
     MARTLSIKDA INEAVDQEMS RDPTVIMMGE DIVGGAGAPG EDDAWGGVLG VTKGLYAKHP
     NQMMDTPLSE SAYVGAAIGA STCGLRPIAE LMFIDFMGVC FDQIFNQAAK FRYMFGGKAE
     TPVVIRAMCG AGFRAAAQHS QMLTPLFTHI PGLKVVCPSN AYDAKGLLIQ SIRDNDPVIF
     LEHKNLYAME TGVPEAPYAI PFGEANVLRE GKDVTLVSYG LTVTRAMDAA DKLAKQGVQC
     DVIDLRTLSP LDIDTVVESV EETGRLVCID EASPRCSIAS DVSAQVAELA FSSLKAPIAM
     VTPPHTPVPF SPSLEDVYVP TVDDIVAAVN RTVGA
//
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