ID   A0A1B9CSS0_MYCMA        Unreviewed;       334 AA.
AC   A0A1B9CSS0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=A5677_05160 {ECO:0000313|EMBL:OCB45528.1};
OS   Mycobacterium malmoense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1780 {ECO:0000313|EMBL:OCB45528.1, ECO:0000313|Proteomes:UP000092683};
RN   [1] {ECO:0000313|EMBL:OCB45528.1, ECO:0000313|Proteomes:UP000092683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3012 {ECO:0000313|EMBL:OCB45528.1,
RC   ECO:0000313|Proteomes:UP000092683};
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   -!- 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:OCB45528.1}.
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DR   EMBL; MBEE01000232; OCB45528.1; -; Genomic_DNA.
DR   RefSeq; WP_065483520.1; NZ_MBEE01000232.1.
DR   AlphaFoldDB; A0A1B9CSS0; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000092683; 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:OCB45528.1}.
FT   DOMAIN          6..180
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   334 AA;  35032 MW;  0A8B8EE9C1396F1B CRC64;
     MREAEMTMRE ALNLALDQAL AADDRVFLLG EDIADPGASG PTAGLSTKYG HDRVLDTPIS
     EAAIVGAAVG AAIDGLLPVA EIMIMDFIGI AADQLINNAA KLRFMTAGRT TAPITVRTQV
     YAGLATGATH SQSLEAWFMH IPGMKVIVPS TPRDGKGLLT SAIFDPDPCL FVETIRLQGK
     KGPVPVDPGF SIPLGRADIK RPGDDVSLIG YGRCVHDALT AAATLAEQGV SAEVVDLRTL
     VPLDIETVVD SVRRTRRAVV VHDAVQFAGP GAEIAAILHS ELFSELAAPV ERVAARFVPN
     PAAAALEAQV YPSPARIVAA ARRTMEKAGA RAHG
//