ID A0A1H0VZ72_9MICC Unreviewed; 326 AA.
AC A0A1H0VZ72;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=SAMN04487914_15211 {ECO:0000313|EMBL:SDP83548.1};
OS Arthrobacter sp. ok909.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1761746 {ECO:0000313|EMBL:SDP83548.1, ECO:0000313|Proteomes:UP000199538};
RN [1] {ECO:0000313|EMBL:SDP83548.1, ECO:0000313|Proteomes:UP000199538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK909 {ECO:0000313|EMBL:SDP83548.1,
RC ECO:0000313|Proteomes:UP000199538};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNJS01000052; SDP83548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0VZ72; -.
DR STRING; 1761746.SAMN04487914_15211; -.
DR Proteomes; UP000199538; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:SDP83548.1}.
FT DOMAIN 3..178
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 34469 MW; 74C71F4B811ADB60 CRC64;
MKSSYREALR AGIRDAMIRD ERVFLMGEDV GAYGGSFAVS LGLLEEFGPD RIRDTPLSES
GFVGAGIGAA LGGMRPIVEI MTVNFSLLAL DQIVNNAATL LHMSGGQFHV PLVIRMTTGA
GRQLGAQHSH SLEGWYAHIP GLRILAPATL EDARGMLWTA LQDPDPVLIF EHGSLYNVPG
ELADDAGPVD IDTAAIRRPG NDISLITYGG TLPAVLDAAE QLAADGIDAE VLDLRTLRPL
DDAAIMASVT RTHRAVVVDE GWRSGSLSAE VSARITEQAF FDLDAPVGRV CSAEVPIPYA
KHLELAALPS AARIITAAKE AVDAGG
//
