ID A0A0A1CSN0_9MICC Unreviewed; 341 AA.
AC A0A0A1CSN0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=ART_0339 {ECO:0000313|EMBL:AIX99937.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIX99937.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIX99937.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIX99937.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
RL Submitted (APR-2014) 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}.
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DR EMBL; CP007595; AIX99937.1; -; Genomic_DNA.
DR RefSeq; WP_038462124.1; NZ_CP007595.1.
DR AlphaFoldDB; A0A0A1CSN0; -.
DR STRING; 1494608.ART_0339; -.
DR KEGG; arm:ART_0339; -.
DR HOGENOM; CLU_012907_1_1_11; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000030301; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:AIX99937.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030301}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 341 AA; 36518 MW; 8EE302BCBF088284 CRC64;
MPVITYRQAL NDALRAELTR DDNVILLGEE IGIFEGSYKI TAGLLAEFGP ERVRDTPIAE
EGFVGAAIGA AMLGMRPVVE IMTLNFSLIA MDQIINHAAK IYGMFGGQTP VPLVIRMPGG
GGQQLAATHS QNLEVWFAHV PGLKVVAPST PADAKALLLA AIRDNDPVIF LENLSLYNTK
GEVPDGEHVA ELGKAAVARK GTDLTVITYS RATTVALEVA RQLAEEGISI EVVDLRSLRP
LDRETVCASV RKTSRAVVLE DDWLSYGVGA EISATLMEGA FDYLDAPVRR VAAAEVPLPY
AKPLELAALP DANDLIKVIR ELLDASRFSP AATDPIAPAT R
//
