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Database: UniProt
Entry: A0A0W0TNH8_9GAMM
LinkDB: A0A0W0TNH8_9GAMM
Original site: A0A0W0TNH8_9GAMM 
ID   A0A0W0TNH8_9GAMM        Unreviewed;       324 AA.
AC   A0A0W0TNH8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Alpha-ketoacid dehydrogenase subunit beta {ECO:0000313|EMBL:QBS11485.1};
DE   SubName: Full=Pyruvate dehydrogenase E1 subunit beta {ECO:0000313|EMBL:KTC97131.1};
GN   Name=odpB {ECO:0000313|EMBL:KTC97131.1};
GN   ORFNames=E4T54_01300 {ECO:0000313|EMBL:QBS11485.1}, Lgee_2102
GN   {ECO:0000313|EMBL:KTC97131.1};
OS   Legionella geestiana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45065 {ECO:0000313|EMBL:KTC97131.1, ECO:0000313|Proteomes:UP000054785};
RN   [1] {ECO:0000313|EMBL:KTC97131.1, ECO:0000313|Proteomes:UP000054785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTC97131.1,
RC   ECO:0000313|Proteomes:UP000054785};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QBS11485.1, ECO:0000313|Proteomes:UP000294523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1308 {ECO:0000313|EMBL:QBS11485.1,
RC   ECO:0000313|Proteomes:UP000294523};
RA   Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA   Charpentier X.;
RT   "Diverse conjugative elements silence natural transformation in Legionella
RT   species.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; LNYC01000073; KTC97131.1; -; Genomic_DNA.
DR   EMBL; CP038271; QBS11485.1; -; Genomic_DNA.
DR   RefSeq; WP_028386156.1; NZ_LNYC01000073.1.
DR   AlphaFoldDB; A0A0W0TNH8; -.
DR   STRING; 45065.Lgee_2102; -.
DR   KEGG; lgt:E4T54_01300; -.
DR   PATRIC; fig|45065.4.peg.2282; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000054785; Unassembled WGS sequence.
DR   Proteomes; UP000294523; Chromosome.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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:KTC97131.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054785};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   324 AA;  35172 MW;  3AF5ECF0731737D3 CRC64;
     MPDITLLEAV SQALGYALQH DENVVVFGED VGKNGGVFRA TAGLQERFGE SRVFDSPLAE
     SMIAGLAIGM STQGMKPVAE FQFMGFIYPA MNQIISHAAR LRNRTRGRLH CPLVFRAPFG
     GGIRAPEHHS ESTEALFAHI PGLQVVIPSS PKRAYGLLLS AIQNPDPVIF LEPKRIYCLV
     KQPVPDDGAT LPLGKCFTLQ EGDDVTLISW GASMHETLQA AKQLAEEGIH CEVIDVATIK
     PLDMDTLIAS VEKTGRCVIV HEGAKTCGVG AEIAAQLSEH LLPDLLAPIV RVTGFDVVMP
     YFQLEKFYIP SVSRIKDAVI SLME
//
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