ID   A0A157S7C8_9BORD        Unreviewed;       738 AA.
AC   A0A157S7C8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   Name=acoA {ECO:0000313|EMBL:SAI65806.1};
GN   ORFNames=SAMEA3906486_00558 {ECO:0000313|EMBL:SAI65806.1};
OS   Bordetella ansorpii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI65806.1, ECO:0000313|Proteomes:UP000076848};
RN   [1] {ECO:0000313|EMBL:SAI65806.1, ECO:0000313|Proteomes:UP000076848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050680373 {ECO:0000313|EMBL:SAI65806.1,
RC   ECO:0000313|Proteomes:UP000076848};
RG   Pathogen Informatics;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
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DR   EMBL; FKIF01000001; SAI65806.1; -; Genomic_DNA.
DR   RefSeq; WP_066123203.1; NZ_FKIF01000001.1.
DR   AlphaFoldDB; A0A157S7C8; -.
DR   STRING; 288768.SAMEA3906486_00558; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000076848; Unassembled WGS sequence.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
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; PF00676; E1_dh; 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); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:SAI65806.1}; Pyruvate {ECO:0000313|EMBL:SAI65806.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076848}.
FT   DOMAIN          399..575
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   738 AA;  79006 MW;  940C5A5CB5149AE2 CRC64;
     MSRYEALAPA APWRTLIAEP RDWQAADPAL LGAMLTQLHW IRAFEETVLD LAAVGLVHGP
     AHSSIGQEGG AVGSVLALGA GDQVNGSHRG HHQFLAKALQ HVAPAGLDPA APLTPEVDTV
     LQRTLAEIMG LSQGYCKGRG GSMHLRWLEA GALGTNAIVG GGVPLAAGAA WAHRHAGTGR
     VAVTYFGDGA INIGSVLESM NLAAAWKLPL CFFVENNRYA VSTTVEEATA EPRLSARGLA
     FNIPAWHVDG MDPLAVHLAM SEAVAHMRAG NGPTLIEVDV YRYFHQNGPF PGSAFGYRPK
     DEETAWRARD PLDMLAARMI ERGLIDAPRV DALRRQCKRV MEEIAQRLTE PLADGKRRIR
     PELWPSPDFR DVGLRSDMSE FDGMRVLEAA DHTGQTVPRK LVDAVADVLG RRMETDPGVV
     VLGEDVHRLK GGTNGATRGL KDRFPDRVLG TPISENAFAG LGGGLAMDGR YKPVVEFMYP
     DFMWVAADQI FNQIGKARHM FGGDIDVPLV LRTKVAMGTG YGSQHSMDPA GIVATSPGWR
     IVAPSTAHDY IGLMNTALLS KDPVLVIEHV DLYASVDEIP AGDLDFHIPF GRAAVRRSGG
     KVTILTYLAM VARTLAAVGA SGVDAEVIDL RTLDRASLDW DTIGASVKKT NNVLIVEQGA
     RGTSYGAMLA DEIQRRLFDW LDQPVKRVTG GEASPSISKV LERAAFAGEE EVMAGLRDVL
     ADLGEADAGT GAQGASRG
//