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Database: UniProt
Entry: A0A177YAN2_9NOCA
LinkDB: A0A177YAN2_9NOCA
Original site: A0A177YAN2_9NOCA 
ID   A0A177YAN2_9NOCA        Unreviewed;       474 AA.
AC   A0A177YAN2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=A3K89_07155 {ECO:0000313|EMBL:OAK52585.1};
OS   Rhodococcus kyotonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK52585.1, ECO:0000313|Proteomes:UP000077519};
RN   [1] {ECO:0000313|EMBL:OAK52585.1, ECO:0000313|Proteomes:UP000077519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KB10 {ECO:0000313|EMBL:OAK52585.1,
RC   ECO:0000313|Proteomes:UP000077519};
RA   Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT   "Genome sequence of Rhodococcus kyotonensis KB10.";
RL   Submitted (MAR-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:OAK52585.1}.
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DR   EMBL; LVHI01000023; OAK52585.1; -; Genomic_DNA.
DR   RefSeq; WP_068428180.1; NZ_LVHI01000023.1.
DR   AlphaFoldDB; A0A177YAN2; -.
DR   Proteomes; UP000077519; 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; 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; 2.
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; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077519};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OAK52585.1}.
FT   DOMAIN          2..79
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          121..158
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   DOMAIN          190..227
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          84..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  48359 MW;  FE8D9C9AAB4F88D1 CRC64;
     MAQEIVLPKL GLTMQEGVIG EWLAQAGQHI GTGDVLLRLE TDKVEVDVEA EASGILATTA
     KVGEVLPVGA VIGWLLADGE VAPTGADGSS ASPADPKDSS TTAASPAAST DGPLEQGERI
     KSSPNARRVA AESDVDLAEV RGTGPGGRIV SEDVEDYVAA VSVAEPKPEP APGVPQREKS
     SSAQASSAHF VGPLVRRRAH ELGVDLSTVA GSGVGGRVTT ADVERAAGHL STDTTESTAP
     AGPRAGEVVP LKGMRGAIAR NMIDSLQTMA QLTHGYEVDV TALVAVRDSL KAELAEAGSR
     PPSLNDFVVK AAALALVQHP ILNAGIVGDE IRLFDTIDIG VAVAVPGGLV VPVVRGANSL
     SVGEISGRTS ALAAAARGNT LGLSDIEGAT FSVSTLGAYG VDFFTPVVNP GNVAILGVGR
     VKDGFRWEGE TPVRTQVLTL SLTFDHRAVD GAPAAEFLRT IASILSRPYA LLAG
//
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