ID A0A127JPM6_9BURK Unreviewed; 447 AA.
AC A0A127JPM6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=UC35_02095 {ECO:0000313|EMBL:AMO21889.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO21889.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO21889.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO21889.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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; CP010951; AMO21889.1; -; Genomic_DNA.
DR RefSeq; WP_061495724.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127JPM6; -.
DR PATRIC; fig|94132.3.peg.417; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000070433; 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:UP000070433};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 159..196
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 95..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 47702 MW; 1DD6C3CFE1102E24 CRC64;
MGTYVIRTPD IGEGIAEVEL VAWHVKPGDM VKEDQVLADV MTDKATVEIP SPVTGKVMEL
VGEVGQQVAV GSDLIRLEVE GAGNVKAGAV AAAAAAPAAQ RPHPNPPPEG EGTGTAPPRE
MEAAKTDSLP HRGRAGVGAL ERPPTSAPVA QRAPGEKPIA SPAVRRRAWE LGIELQFVHG
SGPAGKITHE DLDVYLASRG QPMAGRAAAT AYAQRSGETE VPVIGLRRKI AQKMQEAKRR
IPHFSYVEEI DVTELEALRA RLNAKYAAER GKLTVLPLLA RAVVLAVRDF PQMNARFDDD
AGVVTRYNPV HLGLAAQTPS GLMVPVMRHA ETLDLWDSAR EIARLAEAAR TGKAARDELS
GSTITITSLG ALGGIVTTPV INHPEVAIIG VNRIVERPMF RNGLVVARQM MNLSSSFDHR
VVDGMDAAEF IQAIRALLEA PAMLFVE
//
