ID A0A176QAV8_9MICO Unreviewed; 641 AA.
AC A0A176QAV8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AWH69_10635 {ECO:0000313|EMBL:OAB86863.1};
OS Janibacter melonis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB86863.1, ECO:0000313|Proteomes:UP000076976};
RN [1] {ECO:0000313|EMBL:OAB86863.1, ECO:0000313|Proteomes:UP000076976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD11-4 {ECO:0000313|EMBL:OAB86863.1,
RC ECO:0000313|Proteomes:UP000076976};
RA Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL Submitted (JAN-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 -!- 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:OAB86863.1}.
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DR EMBL; LQZG01000003; OAB86863.1; -; Genomic_DNA.
DR RefSeq; WP_068275186.1; NZ_LQZG01000003.1.
DR AlphaFoldDB; A0A176QAV8; -.
DR STRING; 262209.AWH69_10635; -.
DR Proteomes; UP000076976; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; 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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
DR PANTHER; PTHR43416:SF8; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000076976};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OAB86863.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 147..222
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 330..367
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 70..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 66430 MW; A30F557095D57D3C CRC64;
MSERVTMPAL GESVTEGTVT RWLKSVGDSV EVDEPLLEVS TDKVDTEIPS PVAGTLQEIL
VEEDETVEVG ADLAVIGDGD APASSDSDEG GADDSADEQA ESPAASEDAA GTQEQQAEAE
EEATAPSTAE DEPAKKPQAE TASTDEGQKV QMPALGESVT EGTVTRWLKA EGDEVEVDEP
LLEVSTDKVD TEIPSPVAGT LTSILVQEDE TVEVGADLAV IGGSGGGSAS AEEPQQEAPK
EEAPKQEAPK EQPAQETQES ASSEDTDDSA QKDESLPEDG EGGDVADQPA GQSAPSTGGE
SAATQQAPAS GSSTSAPASG DSAPQDASKY VTPLVRKLAA DNGIDLADVQ GSGVGGRIRK
EDVLEAARAK NAPAEQPSAP AAQAPAAQAP ASSSTPPRGM ESSVSPSKRG TREKMTRLRK
VIAQRMVESL QVSAQLTTVV EVDMTKIARV RARTKADFER REGTKLSFLP FIALATAEAL
KQHPVVNSSV EGEEIVYHGS ENLSIAVDTE RGLLTPVVKN AGDLNVAGLA RAIADVAERT
RANKITPDDL SGGTFTITNT GSRGALFDTP ILNQPQVAML GTGAIVKRPV VVTDADGGET
IAVRSMMYLA LSYDHRVVDG ADAARFLGTV KARLEEGSFE A
//
