ID A0A0F5N6D4_9MYCO Unreviewed; 325 AA.
AC A0A0F5N6D4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=AWC17_26400 {ECO:0000313|EMBL:ORW30274.1};
OS Mycobacterium nebraskense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=244292 {ECO:0000313|EMBL:ORW30274.1, ECO:0000313|Proteomes:UP000193781};
RN [1] {ECO:0000313|EMBL:ORW30274.1, ECO:0000313|Proteomes:UP000193781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44803 {ECO:0000313|EMBL:ORW30274.1,
RC ECO:0000313|Proteomes:UP000193781};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-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}.
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:ORW30274.1}.
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DR EMBL; LQPH01000047; ORW30274.1; -; Genomic_DNA.
DR RefSeq; WP_046186008.1; NZ_LQPH01000047.1.
DR AlphaFoldDB; A0A0F5N6D4; -.
DR STRING; 244292.ABW17_19215; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000193781; Unassembled WGS sequence.
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:ORW30274.1}.
FT DOMAIN 3..178
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 34724 MW; 51E22FFC93AE57D1 CRC64;
MKTSYRTAVH DALRDALRDD PRVVLMGEDV GRYGGTYAAS KGLLDDFGPD RVRDTPLSEL
GFVGIGIGAA LNGLRPIVEV MTVNFSLLAL DQIVNTAAAL RHMSGGQFSV PIVVRMATGA
GRQLAAQHSH SLEPWYAHIP GIKVVAPATV EDAYGMLAPA LADPDPVVIF EHVQLYNTST
DVDVLAPTDI SRAAVRRSGS DVTLITYGGS LPKTLDAANE LSLAGIDCEV VDLRVLRPLD
DETILDSVRK THRAVVVDEA WRTGSLAAEI TARVMEGAFY DLDAPVARVC STEVPMPYAK
HLEEAALPQT AKIVTAVQSL FGNPS
//
