ID   A0A0P8A9P7_9RHOB        Unreviewed;       324 AA.
AC   A0A0P8A9P7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   Name=pdhB-2 {ECO:0000313|EMBL:KPQ14550.1};
GN   ORFNames=HLUCCA09_02905 {ECO:0000313|EMBL:KPQ14550.1};
OS   Rhodobacteraceae bacterium HLUCCA09.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666915 {ECO:0000313|EMBL:KPQ14550.1, ECO:0000313|Proteomes:UP000053417};
RN   [1] {ECO:0000313|EMBL:KPQ14550.1, ECO:0000313|Proteomes:UP000053417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCA09 {ECO:0000313|EMBL:KPQ14550.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
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:KPQ14550.1}.
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DR   EMBL; LJNT01000061; KPQ14550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8A9P7; -.
DR   PATRIC; fig|1666915.4.peg.1552; -.
DR   Proteomes; UP000053417; 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; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR   PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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:KPQ14550.1}.
FT   DOMAIN          4..178
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   324 AA;  34992 MW;  99B04F28E298360B CRC64;
     MATIRYAEAL NLALREEMAR DDTVFVFGED VATYGGVFKV TQGLRDAYGD RVRDTPISEQ
     TLTAMAVTAA MTGTRPVLEI MYADFLPLSL DALVNQASIY HYIWNEQVTM PFVLRTQGGG
     GVGTGAQHAK SLDAMVAHIP GLKVVAPVTP ADARALLKAA IRDPHPVIFL EHKLLYNLRG
     EVDEADEAPA EIGRARVARA GRDVTILATS RMVLEAQKAA EELAGEGVSA EVIDLRSLRP
     LDLDAITASV ARTNHAVVVN EGWRFCGYTA ELAATIMDHA FDDLDAPVER VAARDMPIPY
     AETLEREVIP DSADIAAAAR RALA
//