ID A0A077EBY4_9FLAO Unreviewed; 327 AA.
AC A0A077EBY4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=BD94_0438 {ECO:0000313|EMBL:AIL44213.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL44213.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL44213.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44213.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL44213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44213.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
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; CP007547; AIL44213.1; -; Genomic_DNA.
DR RefSeq; WP_024564699.1; NZ_CP007547.1.
DR AlphaFoldDB; A0A077EBY4; -.
DR STRING; 1338011.BD94_0438; -.
DR KEGG; eao:BD94_0438; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_10; -.
DR Proteomes; UP000028933; 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 Pyruvate {ECO:0000313|EMBL:AIL44213.1}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 36239 MW; 3597341B7630E0A4 CRC64;
MAEYTFREVI AQAMSEEMRK DQSIYLMGEE VAEYNGAYKA SKGMLAEFGP DRIIDTPIAE
LGFAGISVGA AMNGCRPIVE FMTFNFSLVG IDQIINNAAK IFQMSGGQWN CPIVFRGPTA
SAGQLGATHS QALESWYANC PGLKVVVPSN PYDAKGLLKT AIQDNDPVIF MESEQMYSDK
MEIPEEEYYI PIGKADIKKE GTDVTLVSFG KIMKLAIQAA EDLEKEGISV EVIDLRTVRP
LDYDTVLASV KKTNRLVILE EAWPFASVAS EITYMVQQKA FDYLDAPIKR ITTPDAPAPY
SAALFAEWFP KLEKVKAEIK NAMYVKQ
//
