ID A0A0G3ES56_9BURK Unreviewed; 433 AA.
AC A0A0G3ES56;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=ABW99_03935 {ECO:0000313|EMBL:AKJ67506.1};
OS Pandoraea thiooxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ67506.1, ECO:0000313|Proteomes:UP000036700};
RN [1] {ECO:0000313|Proteomes:UP000036700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700};
RA Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
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:RU003423}.
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DR EMBL; CP011568; AKJ67506.1; -; Genomic_DNA.
DR RefSeq; WP_047213111.1; NZ_CP014839.1.
DR AlphaFoldDB; A0A0G3ES56; -.
DR STRING; 445709.ABW99_03935; -.
DR KEGG; ptx:ABW99_03935; -.
DR PATRIC; fig|445709.3.peg.840; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000036700; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 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; 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:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000036700};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 146..183
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 85..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 45764 MW; 89462ABFD4115F4D CRC64;
MGTHIIKMPD IGEGIAEVEL AAWHVGVGET VKEDQPLADV MTDKATVEIP SPVSGTVLAL
GGQVGDVMAV GSELIRLEVE GAGNQKPGAA PAAPAVPAAA QAEPAPRAAP EPVPAAAPAP
VAPAASKPAP PKPAPVIARQ PGERPLASPA VRKRAWDLGI ELRFVHGTGP AGRIGHEDLD
AYLQGRGGTL GARAGLVERN DEQAVPVVGL RRKIAQKMQE AKRRIPHFSY VEEIDVTELE
ELRVQLNRKW GESRGRLTVL PLLARAMVLA LRDFPQINAR FDDELGVVTR HGAVHLGIAA
QSPAGLMVPV VRHAEARDPW SIAAEIARLG EAVRGGKAER DELLGSTITI SSLGPLGGIV
STPVINHPEV AIVGVNRIVE RPMIRHGAVV PRKLMNLSSS FDHRVVDGMD AAEFIQAVRA
LLEQPAMLFV EAP
//