ID A0A2N4YIK1_9RHOB Unreviewed; 457 AA.
AC A0A2N4YIK1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138, ECO:0000256|RuleBase:RU364074};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU364074};
GN ORFNames=C0V75_07020 {ECO:0000313|EMBL:PLL13158.1};
OS Tabrizicola sp. TH137.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL13158.1, ECO:0000313|Proteomes:UP000234539};
RN [1] {ECO:0000313|EMBL:PLL13158.1, ECO:0000313|Proteomes:UP000234539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH137 {ECO:0000313|EMBL:PLL13158.1,
RC ECO:0000313|Proteomes:UP000234539};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO2.
CC {ECO:0000256|RuleBase:RU364074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|RuleBase:RU364074};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU364074};
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:PLL13158.1}.
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DR EMBL; PKRQ01000002; PLL13158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4YIK1; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000234539; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR011053; Single_hybrid_motif.
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; PTHR11624; DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 4: Predicted;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Reference proteome {ECO:0000313|Proteomes:UP000234539};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 457 AA; 47908 MW; 29055203A1AFEC9A CRC64;
MATQVLMPAL SPTMEEGTLA KWLVKEGDTV KSGQIIAEIE TDKATMEFEA VDEGIIGKLL
VAEGTASVKV NTPIAVLVEE GESADAAPAP AATAAAAPAA PVAAQAAAPA PVAAPQAAQG
WPHSDLPEGV PTKTMTVREA LREAMAEEMR ADPSVFLMGE EVGEYQGAYK ISQGLLDEFG
AKRVVDTPIT EHGFAGIAVG ASWGGLRPIV EFMTFNFAMQ AIDHIINSAA KTLYMSGGQM
GSPIVFRGPN GAAARVAAQH SQDYAAWYAA IPGIKVAMPY SAADAKGLLK SAIRDPNPVI
FLENEILYGR SFEVPAEGDF TIPFGKASIL RAGSDVTIVS FGIGLTYALQ AADDLAKDGI
SAEVINLRTL RPIDYDTVLA SVMKTNRCVT VEEGFPVGSI GNHIAATIMQ KAFDHLDAPV
VNCTGKDVPM PYAANLEKLA LTTTAEVVAA VKSVCYR
//
