ID   F9Y470_KETVW            Unreviewed;       428 AA.
AC   F9Y470;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   Name=pdhB {ECO:0000313|EMBL:AEM40506.1};
GN   OrderedLocusNames=KVU_0667 {ECO:0000313|EMBL:AEM40506.1};
OS   Ketogulonicigenium vulgare (strain WSH-001).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ketogulonicigenium.
OX   NCBI_TaxID=759362 {ECO:0000313|EMBL:AEM40506.1, ECO:0000313|Proteomes:UP000000692};
RN   [1] {ECO:0000313|EMBL:AEM40506.1, ECO:0000313|Proteomes:UP000000692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSH-001 {ECO:0000313|EMBL:AEM40506.1,
RC   ECO:0000313|Proteomes:UP000000692};
RX   PubMed=21994934; DOI=10.1128/JB.06007-11;
RA   Liu L., Li Y., Zhang J., Zhou Z., Liu J., Li X., Zhou J., Du G., Wang L.,
RA   Chen J.;
RT   "Complete genome sequence of the industrial strain Ketogulonicigenium
RT   vulgare WSH-001.";
RL   J. Bacteriol. 193:6108-6109(2011).
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=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00043782,
CC         ECO:0000256|RuleBase:RU361137};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP002018; AEM40506.1; -; Genomic_DNA.
DR   RefSeq; WP_014537612.1; NC_017384.1.
DR   RefSeq; YP_005794502.1; NC_017384.1.
DR   AlphaFoldDB; F9Y470; -.
DR   KEGG; kvl:KVU_0667; -.
DR   PATRIC; fig|759362.5.peg.698; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_5; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000000692; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01349; PDHac_trf_mito; 1.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:AEM40506.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:AEM40506.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000692};
KW   Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:AEM40506.1}.
FT   DOMAIN          2..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          122..159
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          166..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  44430 MW;  DF28E1294E6FD9D5 CRC64;
     MSIEILMPAL SPTMEEGTIA KWLVAEGDTV KSGDILAEIE TDKATMEFEA VDDGVIGKIL
     LPAGSEGVKV NTPMAILLED GETEAAAPKA AAPKVEAAPV EAPKAAPVAA AAAPVEKGDR
     VFASPLARRI AADKGLDLNA IAGSGPKGRI VRADVEGATA AKPAEAAKAP AAAAPTPAAP
     APVPTSSSAD QILKMYQGRD YTEVKLDGMR KTIAARLTEA KQTVPHFYLR RSVNLDALMA
     FRADLNAKLG PRGIKISVND FVIKACAIAL QQVPKANAIW AGDRVLQMKA SDVSIAVAVE
     GGLFTPVIRD ADAKSISALS AEMKDLAKRA RDKKLQPQDY QGGSFSISNL GMFGVENFDA
     VINPPQGAIL AVGAGIKKPI VGDDGEITTA TLMSLTLSVD HRVIDGALGA HLLTAIVENL
     ENPLSMLA
//