ID A0A1H2MAV9_9PSED Unreviewed; 422 AA.
AC A0A1H2MAV9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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 ORFNames=SAMN05216202_1363 {ECO:0000313|EMBL:SDU90390.1};
OS Pseudomonas mucidolens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46679 {ECO:0000313|EMBL:SDU90390.1, ECO:0000313|Proteomes:UP000198600};
RN [1] {ECO:0000313|Proteomes:UP000198600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 2223 {ECO:0000313|Proteomes:UP000198600};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; LT629802; SDU90390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2MAV9; -.
DR STRING; 46679.SAMN05216202_1363; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000198600; Chromosome i.
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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 136..173
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 422 AA; 45064 MW; A3BD70AB87DC7622 CRC64;
MGTHVIKMPD IGEGIAEVEL SVWHVKVGDM VVEDQVLADV MTDKAMVDIP SPVHGKVIAL
GGEPGEVMAV GSILISIEVE GAGNTQESAL SAMVEETAPE PAQKPEAPAP VAESKPMAKP
LAAQAPVARE AAERPLASPA VRKHALDAGI PLRLVHGSGP AGRILHEDLD AYLQQGAANP
TATANPYAER SDEQQIPVIG MRRKIAQRMQ DATRRAAHFS YVEEIDVTAL DELRVHLNAK
HAATRGKLTL LPFIVRAMAV ALRDFPQINA RYDDEAQVIT RLGAVHVGVA TQSAVGLMVP
VVRHAEARNL WGTAEEIHRL AHAARNGKAS REELSGSSIT LTSLGALGGI VSTPVLNLPE
VAIVGVNRIV ERPMVIKGQI VIRKMMNLSS SFDHRVVDGM DAAQFIQAIR GLLEQPASLF
LE
//
