ID K7YS80_BDEBC Unreviewed; 548 AA.
AC K7YS80;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=pdhC {ECO:0000313|EMBL:AFY00448.1};
GN ORFNames=Bdt_0741 {ECO:0000313|EMBL:AFY00448.1};
OS Bdellovibrio bacteriovorus str. Tiberius.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFY00448.1, ECO:0000313|Proteomes:UP000010074};
RN [1] {ECO:0000313|EMBL:AFY00448.1, ECO:0000313|Proteomes:UP000010074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tiberius {ECO:0000313|EMBL:AFY00448.1,
RC ECO:0000313|Proteomes:UP000010074};
RX PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R., Milner D.S.,
RA Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J., Harris M.A.,
RA Sockett R.E.;
RT "Genome analysis of a simultaneously predatory and prey-independent, novel
RT Bdellovibrio bacteriovorus from the River Tiber, supports in silico
RT predictions of both ancient and recent lateral gene transfer from diverse
RT bacteria.";
RL BMC Genomics 13:670-670(2012).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; CP002930; AFY00448.1; -; Genomic_DNA.
DR RefSeq; WP_015089924.1; NC_019567.1.
DR AlphaFoldDB; K7YS80; -.
DR STRING; 1069642.Bdt_0741; -.
DR KEGG; bbat:Bdt_0741; -.
DR PATRIC; fig|1069642.3.peg.733; -.
DR HOGENOM; CLU_016733_10_0_7; -.
DR Proteomes; UP000010074; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:AFY00448.1};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 11..86
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 120..195
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 246..283
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 101..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 56704 MW; 8E839E381FD600C2 CRC64;
MNNERNSRNM ATDVKLPELG EGVTEGELVK WLVKPGDAVK ADQAIAEVLT DKATVEVPSP
VAGVVKDLKF KSGDVVKVGA TMITLDGAGA AKPAAAQPAA AAPAPAASTP APAAGGGGKA
QDVKLPELGE GVTEGELVKW LVKPGDSVKA DQAIAEVLTD KATVEVPTPV AGVVKELKFK
SGDVVKVGST MIILEGAGGA AAPKAAPSAG PVQSAPAHSA APAAKAAPVA TASSDIFPPV
ADSKVLATPA TRRLAREMGV DINSLSGTGL AGRVTREDVM SSNGGAGSAA AKPQQSAASA
TMSIPKPSYQ GPAGAAEERV PLIGIRKKIA ENMQRSKHVI PHFTIMDEAK VDAMVALRES
LKEHAEKNGT KITYLPIVMK ALIATIREFP MFNASIDDAA GEIVYKKYFN LGFAADTPNG
LVVPVIKNAD QKSILEISKE ILDLSKRARD GKLKPDEMKG ATITVTNIGS IGGTYATPVI
NHPEVAILGM YKIDEKVVLK NGQVSAIKVM NYTMTADHRL IDGAVAARFL AAFIGRIENP
GKLLVELI
//
