ID   A0A1H3CXH3_9RHOB        Unreviewed;       331 AA.
AC   A0A1H3CXH3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=SAMN04488238_11114 {ECO:0000313|EMBL:SDX58922.1};
OS   Roseicitreum antarcticum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Roseicitreum.
OX   NCBI_TaxID=564137 {ECO:0000313|EMBL:SDX58922.1, ECO:0000313|Proteomes:UP000198539};
RN   [1] {ECO:0000313|EMBL:SDX58922.1, ECO:0000313|Proteomes:UP000198539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8894 {ECO:0000313|EMBL:SDX58922.1,
RC   ECO:0000313|Proteomes:UP000198539};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNOM01000011; SDX58922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3CXH3; -.
DR   STRING; 564137.SAMN04488238_11114; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000198539; 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:SDX58922.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198539}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   331 AA;  35668 MW;  07CE54AF3D75B402 CRC64;
     MREITLSQAV NEAIAEEMRR DPTVFLMGED VAEAGTPFKV LSGLVEEFGT GRVIDTPISE
     PGFVGLAVGA AMTGARPIVD LMFGDFIYLV MDQLCNQAAK QHYMSGGKLT VPMVLRTNMG
     ATRRSAAQHS QSLQALVAHI PGLKVAMPSS AYEAKGLMKT AIRDNNPVVI FEDKLMYQDK
     APVPEEEYLI PFGVAHVKRE GRDITLIGTS SMVQVAEKAA EILALEGISA EVIDPRTIVP
     LDEATLLDSV KKTSRAIVID EGHQSYGVTA EIASRLNEKA FYHLDAPVLR MGAMDVPVPF
     SPALEDLTVP TPEQVAANAR KLCAGELIHA A
//