ID S6CZH5_ACEPA Unreviewed; 451 AA.
AC S6CZH5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 Name=pdhB {ECO:0000313|EMBL:CCT60769.1};
GN ORFNames=APA386B_2737 {ECO:0000313|EMBL:CCT60769.1};
OS Acetobacter pasteurianus 386B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1266844 {ECO:0000313|EMBL:CCT60769.1, ECO:0000313|Proteomes:UP000015386};
RN [1] {ECO:0000313|EMBL:CCT60769.1, ECO:0000313|Proteomes:UP000015386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=386B {ECO:0000313|EMBL:CCT60769.1};
RX PubMed=23902333;
RA Illeghems K., De Vuyst L., Weckx S.;
RT "Complete genome sequence and comparative analysis of Acetobacter
RT pasteurianus 386B, a strain well-adapted to the cocoa bean fermentation
RT ecosystem.";
RL BMC Genomics 14:526-526(2013).
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}.
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DR EMBL; HF677570; CCT60769.1; -; Genomic_DNA.
DR RefSeq; WP_020944720.1; NC_021991.1.
DR AlphaFoldDB; S6CZH5; -.
DR GeneID; 60375778; -.
DR KEGG; apk:APA386B_2737; -.
DR PATRIC; fig|1266844.4.peg.2737; -.
DR HOGENOM; CLU_012907_0_0_5; -.
DR Proteomes; UP000015386; Chromosome.
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|RuleBase:RU364074,
KW ECO:0000313|EMBL:CCT60769.1};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 451 AA; 48100 MW; E38E4CBE4AC45165 CRC64;
MATEILMPAL SPTMTEGKLA RWLKKEGDAV NSGDVLAEIE TDKATMEVEA IEEGILGRIL
TAEGTEGVAV NTPIAILVEE GEAVPDNIDT PKSAAFAEAL PVAQPVASAP VSAPVSAPVE
EEKDWGETQE ITVREALRDA LAAELRRDPD VFLMGEEVAQ YQGAYKISQG LLQEFGEKRV
IDMPIAEHGF TGMAVGAALT GLKPVVEFMT MNFSMQAIDH IINSAAKTLY MSGGQMGCPI
VFRGPNGPAS RVGAQHSQCY GSWYAHVPGL KVVVPWSSAD AKGLLRAAIR DPNPVVVLEN
EILYGRKFPC PIDEDFIVPI GKAKIERAGS DVTIVAFSIA VTTALDAAAE LAKQGIEAEV
INLRSLRPLD TDTIVESVKK TSRLVTVEEG WPFAGIGAEV AMQVIEHAFD WLDAPPARVT
GVDVPMPFAA NLEKLALPQP EDVVKAALGL M
//