ID A0A1A2WA37_MYCSC Unreviewed; 672 AA.
AC A0A1A2WA37;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=A5679_06890 {ECO:0000313|EMBL:OBI10429.1};
OS Mycobacterium scrofulaceum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1783 {ECO:0000313|EMBL:OBI10429.1, ECO:0000313|Proteomes:UP000092207};
RN [1] {ECO:0000313|EMBL:OBI10429.1, ECO:0000313|Proteomes:UP000092207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2838 {ECO:0000313|EMBL:OBI10429.1,
RC ECO:0000313|Proteomes:UP000092207};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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 -!- 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OBI10429.1}.
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DR EMBL; LZJY01000015; OBI10429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A2WA37; -.
DR Proteomes; UP000092207; 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}.
FT DOMAIN 352..526
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 672 AA; 70311 MW; 6E1737B3789727E5 CRC64;
MATQVDTETR ALSSGRAVEL YRLMSKVHHS DQRVRKGLSS GEIAMSYWPV DGQEAMSAGA
ALALSSTDQL VTTYRGLGDV VAKGIDLPGY FAEILGRGTG LSKGKAGAMG IYDPEHGIAW
TTGIVGAGPL IANGIALAEA VKGGDRVVLV SFGDGATSIG YVHEAMNMAA LWALPVVFFC
QNNAWAECTP VAGYTRTAKL SDRAAGYAMP GVTVDGTDPH AVYQAVAEAA ERARSGAGPS
FVEAVAYRLQ GHYFGDQMPY ADPDELAAKR ADPPLARYRR RLVEEGLADE ADLDRIDVEL
VAEIDAAFAA ARDADPPDAD ELTRDVFAAG GIEIAAPVTE RAAIPKGETE TLGLVQAIHR
TLDRAMAADD SIVLLGEDIA DPSGGMFKIT AGLSTKYGSH RVRDTPIAES SIIGAAVGAA
LGGLRPVAEL MFVDFLGVAM DQIANHAAKI RYMSGGRQGA PVVIRAMVGT AAGPQHSQAF
EAWAMHTPGI KVVWPSTAAD AVGLLNACLA EDDPCLFIES MKLYYGGGKG PVPTADYVIP
LGQADVKRVG TDVTVCTYGS LVHAALDAAE QLAAQSVSVE VVDLRTLVPL DLATVFESVR
KTRRLVVAHE SVGFCGPGAE IAAAVGTELF GVLASPIQRV AGTYTPVPRA TTLEAACRPD
AARLVEAVRR IV
//
