ID   A0A0Q9YS95_9COXI        Unreviewed;       742 AA.
AC   A0A0Q9YS95;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000313|EMBL:KRG19495.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:KRG19495.1};
GN   Name=pdhB_1 {ECO:0000313|EMBL:KRG19495.1};
GN   ORFNames=CC99x_00507 {ECO:0000313|EMBL:KRG19495.1};
OS   Candidatus Berkiella cookevillensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Berkiella.
OX   NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG19495.1, ECO:0000313|Proteomes:UP000051494};
RN   [1] {ECO:0000313|EMBL:KRG19495.1, ECO:0000313|Proteomes:UP000051494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC99 {ECO:0000313|EMBL:KRG19495.1,
RC   ECO:0000313|Proteomes:UP000051494};
RA   Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT   "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT   Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT   aquae.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
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:KRG19495.1}.
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DR   EMBL; LKHV01000002; KRG19495.1; -; Genomic_DNA.
DR   RefSeq; WP_057623341.1; NZ_LKHV02000001.1.
DR   AlphaFoldDB; A0A0Q9YS95; -.
DR   STRING; 437022.CC99x_00507; -.
DR   PATRIC; fig|1590042.3.peg.525; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000051494; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:KRG19495.1}; Pyruvate {ECO:0000313|EMBL:KRG19495.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051494};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          401..582
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   742 AA;  83408 MW;  977E51DB21539652 CRC64;
     MDLNRAKIID EQWIHCLKNA VYPALTSHVL PDSVGLTKDV FLDLFHSQCV SRHLDLIART
     LKEGGKTFYT IGSSGHEGNA ALGYIFRLDD TAFLHYRSGA FMAQRAKKLP EINYIYDQLL
     SLMASREDPI SGGRHKVFGS FSLNVPPQTS TIASHLPKAL GAALSLVLSK KLKISNSFTK
     LKEDGVVLCS FGDASSNHST AQGAFNAIAW MLHQGLKLPL ILICEDNGWG ISVPTPSDWI
     EKVFSSKQSL HYIACDGRNL SDVYQAGLKA QAIARRKQEP VFLHMKTVRL MGHAGSDIEA
     HYRLQKEVEN TEKEDPLLHS AHIIRLHDWL TEPELIDIYE SVRESVRVQS QAALLRPKLS
     SLADIQSSIV PPKRSSRKIS LTEEARKRAL GKNYQWLNED RNMAQHINLA LTDLMIEYPH
     LMLFGEDVAK KGGVYRVTQD LQARFGQQRV FDTLLDEQTI LGIALGFAQN GLIPMPEIQF
     LAYTHNAVDQ IRGEAATLSF FSKGQYSNPM VIRIPALAYQ KGFGGHFHND NAFAFLREIP
     GIIVVTPSQA KDAALLLKES VRLAEEEQRV VVFLEPIALY MTKDRYQEND HLALQHYPMM
     DECLAYPEIG VEGNVHSDIV IMSYANGMHL SRQAAFILKA HYNLEVLLLD LRWLHPISFD
     KIQPWVNCKR IVLVVDESRQ TGSLSEEIFT WFVENVQPLP TLSRLCAADC FIPLGDAFEK
     VLPSKEMIVN RILSLLQGKN YA
//