ID A0A417Y7E8_9ACTN Unreviewed; 657 AA.
AC A0A417Y7E8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=D0Z08_05610 {ECO:0000313|EMBL:RHW28431.1};
OS Nocardioides immobilis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2049295 {ECO:0000313|EMBL:RHW28431.1, ECO:0000313|Proteomes:UP000283644};
RN [1] {ECO:0000313|EMBL:RHW28431.1, ECO:0000313|Proteomes:UP000283644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2017083 {ECO:0000313|EMBL:RHW28431.1,
RC ECO:0000313|Proteomes:UP000283644};
RA Li C., Wang G.;
RT "Genome sequencing of Nocardioides immobilis CCTCC AB 2017083 for
RT comparison to Nocardioides silvaticus.";
RL Submitted (SEP-2018) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693};
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}.
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:RHW28431.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QXGH01000010; RHW28431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417Y7E8; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000283644; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000283644}.
FT DOMAIN 335..510
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 657 AA; 69489 MW; 0AB3D6B22973F3F3 CRC64;
MLMSYELTPN DTYRRMAYIR AFEEQVLELG REGEVVGSVH LALGQEAIPV GAMAALEAQD
RVLATYRGHG WALACGSDPR GLMAEIAQRE AGVNGGRAGS PMLSDPDVGF LGENSIIGAH
LPIGTGVALA SQIAGETRVV IVSLGDGAMN QGSTTEAMIF AAAKNLPVIF LCENNGWSEM
TPIGTTTRGE HLARRGQGLC IESVIVDGGD PVAVCEAVSG AAEQCRRGEG PVLLECKTVR
LSGHYNKDIQ HYRGQDDIDA AAEEDPLLRM REMGAISAEE AATIEAEVKA EVAHLAEEVR
GLSAPSADTA LSHLYGPDPA GGLAGAEGDV NVKEIPYFRA VNEALRWAMT NCPEVIVYGE
DVGVAGGIFG VTRGLQKEFG SERVFDTPIA EAAILGSAVG AAMHGLRPVV EIMWADFVFV
ALDQIVNQAA NVRYVNRSKL SAPLVVRMQQ GFTPGSCAQH SQSIEAILSH IPGIKVGMPS
TPQDAYAMTL AAINDPDPVV QIEHRAMYQN TGEVRLGSPS ELARGARVQR DGSDVAIISW
GSMVGASLEA AEILAGEGIE ALVLDLRWLR PLDDEAIASA VRRAGGHVLV VHEAVLTGGF
GAEIAARIAE RHFETLAGPV HRLATPDVRM PSAPNLQQVL IPNASDVADL VRKLLGR
//
