ID I6ZU05_MELRP Unreviewed; 520 AA.
AC I6ZU05;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=MROS_2259 {ECO:0000313|EMBL:AFN75489.1};
OS Melioribacter roseus (strain JCM 17771 / P3M-2).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Melioribacteraceae; Melioribacter.
OX NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN75489.1, ECO:0000313|Proteomes:UP000009011};
RN [1] {ECO:0000313|EMBL:AFN75489.1, ECO:0000313|Proteomes:UP000009011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT organotrophic bacterium representing a novel deep lineage within
RT Bacteriodetes/Chlorobi group.";
RL PLoS ONE 8:E53047-E53047(2013).
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; CP003557; AFN75489.1; -; Genomic_DNA.
DR RefSeq; WP_014856921.1; NC_018178.1.
DR AlphaFoldDB; I6ZU05; -.
DR STRING; 1191523.MROS_2259; -.
DR GeneID; 78567181; -.
DR KEGG; mro:MROS_2259; -.
DR PATRIC; fig|1191523.3.peg.2385; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_10; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000009011; 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; 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; 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; PS00189; LIPOYL; 2.
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:UP000009011};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 100..175
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 218..258
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 520 AA; 57445 MW; F7FD923BB13F3DDC CRC64;
MKVEIIMPQM GESITEGTVI KWHKKVGEEI KKDEILFEIS TDKVDTEVPS PENGILKEIL
VKENETAEVG KVVAVLETDN SEYVDKAQDT PTTTQVGGEI VDIIMPKMGE SITEGVIIKW
HKKAGDKVAK DEILFEISTD KVDTEVPSPE EGILTEILYE ENQTVEVGQT VAKLKTTTGL
RPVTTAAETV EIAEEKEKSA AEEPLRKEET ASRNANRFYS PSVINLARAE GIPLSELDTL
EGTGLKGRLT KKDLERYIES RKSVAINQDV KKTEPASVSE YKRVSSDGVE IIPMDHTRRR
IMEHMVKSRD TSVHVTAVAE VDMSVIYNFI KENKNKFAKE NLKLTYMPFI AFAAVKALQQ
YPLMNSSIEG ANIVMKKYIN LGIAVAVEPN GLIVPNIKHA EEKSVIGLAK AIADLSERTR
TKKLLPEDVQ NGTFSITNYG VFGTLIGTPI INQPEVGILG VGAVVKKPVV VENEGVESIA
IKPMMYLSLS HDHRLIDGMI GSKFLMSIKH ILENFDTSSV
//
