ID A0A0A1DRM0_NOCSI Unreviewed; 727 AA.
AC A0A0A1DRM0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=KR76_25410 {ECO:0000313|EMBL:AIY19282.1}, NSI01_48170
GN {ECO:0000313|EMBL:GEB16502.1};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY19282.1, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY19282.1, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY19282.1,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0000313|EMBL:GEB16502.1, ECO:0000313|Proteomes:UP000318936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB16502.1,
RC ECO:0000313|Proteomes:UP000318936};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL Submitted (JUN-2019) 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}.
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DR EMBL; CP009896; AIY19282.1; -; Genomic_DNA.
DR EMBL; BJMC01000023; GEB16502.1; -; Genomic_DNA.
DR RefSeq; WP_038682332.1; NZ_JAAARG010000054.1.
DR AlphaFoldDB; A0A0A1DRM0; -.
DR STRING; 2045.KR76_25410; -.
DR KEGG; psim:KR76_25410; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000030300; Chromosome.
DR Proteomes; UP000318936; Unassembled WGS sequence.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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 ECO:0000313|EMBL:AIY19282.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT DOMAIN 402..578
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 727 AA; 78361 MW; 8FB0CC36D8F9FC46 CRC64;
MPKHVSLQPA APWVEVTLDQ RDRDAAEPQL LLDLLGRMQW VRTFEEYVLE LAGQGLVHGP
AHSSIGQEGG ALGSILPLRS DDMINGSHRG HHQFLAKAFG HVLPAGGTGL PRVTGEVREV
LRRTLAEICG LADGFCRGRG GSMHLQWREA GAMGTNAIVG GGVPQAAGFG WAMRNAGTDA
VSVTYFGDGA VNIGSVLETF NLAAAWKLPV CFFIENNLYA VSTHVDAATA EPRLSGRGLG
FNIPSWRVDG MDPLAVHVAM TEALEHMRAG NGPTIIEAEV YRYFHQNGPF PGSAFGYRDK
AEEAAWRERD PIAQLRAEVL RRELVTQDEL DAQADEVGSV MRELGEQFLE ADPEGKPGQR
RIIASAWPDP GFVDVGIRGD LSELAGSRYE EEESFSGELA ERRFIDVVSE VMARRMETDP
SVVVLGEDVD GLKGGTNGAT RAALSAYPDR VLGTPISENA FAGLAGGMAL DGRVRPVVEF
MYADFMWVAA DQLFNQVAKA RHMFGGEAAV PFVLRSKLAA GTGYGSQHSM DPAGVLATAP
GLRIVAPSNP FDYVGLMNTA LACDDPVVVL EHVDLYASSG TGPVDDLDYR LPVGKAALRR
TGDDLTIISY LSMVGHCLEA LDEVGDRISA DLIDLRWLDR ASLDWDTIEA SVRKTNQVLI
VEQGAAGTSY GGWLADEIQR RLFDWLDAPV RRVHGSEASP SISKVLERAA IARTEEVTAA
LNDIAAE
//
