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Database: UniProt
Entry: A0A0Q9YGF9_9COXI
LinkDB: A0A0Q9YGF9_9COXI
Original site: A0A0Q9YGF9_9COXI 
ID   A0A0Q9YGF9_9COXI        Unreviewed;       326 AA.
AC   A0A0Q9YGF9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000313|EMBL:KRG19631.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:KRG19631.1};
GN   Name=pdhB_2 {ECO:0000313|EMBL:KRG19631.1};
GN   ORFNames=CC99x_00644 {ECO:0000313|EMBL:KRG19631.1};
OS   Candidatus Berkiella cookevillensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Candidatus Berkiella.
OX   NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG19631.1, ECO:0000313|Proteomes:UP000051494};
RN   [1] {ECO:0000313|EMBL:KRG19631.1, ECO:0000313|Proteomes:UP000051494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC99 {ECO:0000313|EMBL:KRG19631.1,
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   -!- 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:KRG19631.1}.
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DR   EMBL; LKHV01000002; KRG19631.1; -; Genomic_DNA.
DR   RefSeq; WP_057623591.1; NZ_LKHV02000001.1.
DR   AlphaFoldDB; A0A0Q9YGF9; -.
DR   STRING; 437022.CC99x_00644; -.
DR   PATRIC; fig|1590042.3.peg.662; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000051494; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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   Oxidoreductase {ECO:0000313|EMBL:KRG19631.1};
KW   Pyruvate {ECO:0000313|EMBL:KRG19631.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051494};
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   326 AA;  35311 MW;  2C3CF7F425D2CB5B CRC64;
     MTAITLIEAV NKALAYELEH DPNVVVYGED VGVNGGVFRA TDGLAKSFGE HRVKDSPLAE
     NLIAGLAVGM SAMGLKPVAE IQFLGFIYAA LDQIISHASR LRNRTRGRLS CPMVIRTPYG
     AGIHAPEHHS ESIEAMFAHV PGLRVVIPSS PSRAYGLLLA AIRDPDPVIF LEPTRVYRLM
     KEEVEDNGEA LPLDVCFQLR EGNDVTLVSW GAMMHETLQA ADELAKNGIT ADVIDVATIK
     PLDINTILNS VHKTGRCVIV QESVSTCSVG SEISALIAEN ALTSLMAPVV RVSGYDTIVP
     LYKLEKTYLP SKQRILTAVQ QVLEFA
//
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