ID A9D7L6_HOEPD Unreviewed; 331 AA.
AC A9D7L6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=HPDFL43_16541 {ECO:0000313|EMBL:EDQ33102.1};
OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Hoeflea.
OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ33102.1, ECO:0000313|Proteomes:UP000004291};
RN [1] {ECO:0000313|EMBL:EDQ33102.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ33102.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDQ33102.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ33102.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Fiebig A.;
RL Submitted (JUN-2012) 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:EDQ33102.1}.
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DR EMBL; ABIA03000004; EDQ33102.1; -; Genomic_DNA.
DR RefSeq; WP_007199059.1; NZ_CM002917.1.
DR AlphaFoldDB; A9D7L6; -.
DR STRING; 411684.HPDFL43_16541; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_5; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000004291; Chromosome.
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; 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 Oxidoreductase {ECO:0000313|EMBL:EDQ33102.1};
KW Pyruvate {ECO:0000313|EMBL:EDQ33102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004291}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 331 AA; 35530 MW; AE959B6089788BED CRC64;
MREITLSQAV NEALAEEMRR DETVFIIGED VAEAGTPFKV LSGLVEEFGT SRVVDTPIAE
PGFMGIAVGA AMTGSRPVVD LMFGDFLFLI MDQLCNQAAK THYMSGGKLN VPLVLRTNLG
ATRRSAAQHS QSLHALVAHI PGLKVALPSS AYEAKGLMKT AIRDNNPVVI FEDKLMYQEK
AGVPEEEYMI PFGVANVKRE GTDITLIATS SMVQVAEKAA EILATEGISA EVIDPRTIVP
LDEATLIKSV KKTSRAIVID EGHQSYGVTS EIASRLNEKA FYHLDAPVLR MGAMDVPVPF
SPALEDLTVP TPEGVAANAR RLVAGELINA A
//
