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Database: UniProt
Entry: S6CZH5_ACEPA
LinkDB: S6CZH5_ACEPA
Original site: S6CZH5_ACEPA 
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
//
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