ID W2V186_9RICK Unreviewed; 396 AA.
AC W2V186;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:ETO91422.1};
GN ORFNames=P857_337 {ECO:0000313|EMBL:ETO91422.1};
OS Candidatus Xenolissoclinum pacificiensis L6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Xenolissoclinum.
OX NCBI_TaxID=1401685 {ECO:0000313|EMBL:ETO91422.1, ECO:0000313|Proteomes:UP000018951};
RN [1] {ECO:0000313|EMBL:ETO91422.1, ECO:0000313|Proteomes:UP000018951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L6 {ECO:0000313|Proteomes:UP000018951};
RX PubMed=24324632;
RA Kwan J.C., Schmidt E.W.;
RT "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT conservation of secondary metabolism.";
RL PLoS ONE 8:E80822-E80822(2013).
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 -!- 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}.
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:ETO91422.1}.
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DR EMBL; AXCJ01000005; ETO91422.1; -; Genomic_DNA.
DR AlphaFoldDB; W2V186; -.
DR STRING; 1401685.P857_337; -.
DR PATRIC; fig|1401685.3.peg.627; -.
DR Proteomes; UP000018951; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
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; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:ETO91422.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018951};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..65
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 120..157
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 396 AA; 43165 MW; 85380AA2CB05BAC2 CRC64;
MEKGNLQRWF KKEGDSVSSG DVIAEIETDK AVVELESLDD GVLHTIVVPD NSKDVPVGSI
IALLKEEGDD DQDVLKLLNN ASDTKNSPSA EVSKESQNIS LEKDTALDHQ VSINNSERIK
ISPLAKKLSE INKVSLNGMV GSGPGGRIVK SDVLSQIDKV PNNTIAHSHQ DISSSTVSPM
RMAIASRLTE SKTTIPHFYL SVDCSVDDLV KYKKQIKEQS QKNITINDFV VKAVAMSVAQ
YPDVNSYWQK DQIIKNSQVD VAVAVAIEDG LITPIVKNCD SKTITAVSAE IKSLAEKAKN
KSLKPEEFQG GSVTVSNLGM YGIKEFFAII NPPQSAIISV GAAYKIPCFN ENDHIVPKQI
MNISLSCDHR VVDGVLASMF LQSIKNYLEN PMLIVI
//
