ID A0A0M2CR10_9MICC Unreviewed; 697 AA.
AC A0A0M2CR10;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=H488_0115400 {ECO:0000313|EMBL:EYT48784.1};
OS Kocuria sp. UCD-OTCP.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT48784.1, ECO:0000313|Proteomes:UP000033173};
RN [1] {ECO:0000313|EMBL:EYT48784.1, ECO:0000313|Proteomes:UP000033173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT48784.1,
RC ECO:0000313|Proteomes:UP000033173};
RX PubMed=23661474;
RA Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00172-13(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}.
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:EYT48784.1}.
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DR EMBL; AOSQ01000037; EYT48784.1; -; Genomic_DNA.
DR RefSeq; WP_031283342.1; NZ_AOSQ01000037.1.
DR HOGENOM; CLU_016733_10_1_11; -.
DR Proteomes; UP000033173; Unassembled WGS sequence.
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; 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; 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 Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EYT48784.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 175..250
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 385..422
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 70..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 72208 MW; 1DF0BD727367B03C CRC64;
MSETVNLPAL GESVTEGTVT RWLKQVGDEV AVDEPLVEVS TDKVDTEIPS PVAGVIEEIL
VEEDEDVEVG APLVVIGDGS GSGSGGGSGQ DEAAADTSAQ EAEDAATEAE TPEATDEAAE
QKSSGQESSX EAEDAATEAE TPEATDEAAE QKSSGQESSG QEQAPQAEAQ QTGEGSEITL
PALGESVTEG TVTRWLKQVG DEVAVDEPLL EVSTDKVDTE VPSPVAGTLL EIRVQEDEDA
EVGQVLAVIG SGSAPSGDKP AEKPAADTSA LLEIRVQEDE DAEVGQVLAV IGSGSAPSGD
KPAEKPAADT SAEEKPAKQS SAGGEGYEGS SSGKQEKAPS RDEALVETDE PVLADTSGDE
QQDAAQRDGA RTENAEAPTG DNSSYVTPLV RKLAKKEGVD LSALTGTGVG GRIRKQDVLA
AAEQQKSAAA PAAEAPAETA AAAPAKEAAP AAPKADAKRG TTEKAPRIRM TIAQRMRESL
QEAAQLTQVT EVDMTRVAVL RGRAKAKFQE REGAKLTYLP FFAKAVAEAL QAHPKLNATF
KEAEKEIVYN GSENIAIAVD TPKGLLVPVI KNAGDLNLGG LAKQIADLGS RAKDGNITPD
DLTGGTFTIT NLGSFGALFD TPIINQPQVA ILGTGSIVKR PMVVSDADGN DTIAIRQMCY
LSLTYDHRLV DGADAGRFLQ ALKARLEEGR FESEVGL
//
