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Database: UniProt
Entry: A0A1T3P282_9ACTN
LinkDB: A0A1T3P282_9ACTN
Original site: A0A1T3P282_9ACTN 
ID   A0A1T3P282_9ACTN        Unreviewed;       606 AA.
AC   A0A1T3P282;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   05-JUN-2019, entry version 9.
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=B4N89_21785 {ECO:0000313|EMBL:OPC83216.1};
OS   Streptomyces scabrisporus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC83216.1, ECO:0000313|Proteomes:UP000190037};
RN   [1] {ECO:0000313|EMBL:OPC83216.1, ECO:0000313|Proteomes:UP000190037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NF3 {ECO:0000313|EMBL:OPC83216.1,
RC   ECO:0000313|Proteomes:UP000190037};
RA   Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT   "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte
RT   isolated from Amphipterygium adstringens.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OPC83216.1}.
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DR   EMBL; MWQN01000001; OPC83216.1; -; Genomic_DNA.
DR   Proteomes; UP000190037; Unassembled WGS sequence.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 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   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR02927; SucB_Actino; 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000190037};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190037};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:OPC83216.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      138    213       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      295    332       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       81    141       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1T3P282}.
FT   REGION      244    290       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1T3P282}.
FT   COMPBIAS    255    283       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A1T3P282}.
SQ   SEQUENCE   606 AA;  61489 MW;  D0839F20ABAF5D7D CRC64;
     MPVSVTLPAL GESVQEGTIT RWLKQEGERV ELDEPLLEVS TDKVDTEIPS PAAGILVSIK
     AQEDDTVDVG AELAVIDDGT GASAPAAAPA PQAAEAPAEA PAPAEAPAAP AAPAAQEPAQ
     AAQEPAQAPA APAGDAQGTP VLLPALGESV QEGTITRWLK QEGDTVEADE PLLEVSTDKV
     DTEIPSPVGG VLLKIKVAED ETVEVGAELA VIGAPGAAPA AAPAPAAAAP AAAPAPAAAP
     ATAPAQAAAP APAPAAAPAQ APAPKPAPTP APAPAPQAAA PAPQLAPPAE ADGAYVTPLV
     RKLAAEHNVD LGAIEGTGIG GRIRKQDVLE TARKQQAAQA AAAASAPAPA AAAPAAKAAA
     PIEPSPLRGR TEKLSRMRTV IAKRMVESLQ TSAQLTTVVE VDVTNIARLR DRAKNDFVAR
     EGVKLSFMPF FAKAAVEALK VHPVLNASMD LDAGTVTYHD AEHLVIAVDT DRGLMVPVIH
     NAGDLNIAGL SRKISDLAER TRTNKVSPDE LAGGTFTLTN TGSRGALFDT PIFPQPQVAM
     LGTGAVVKRP VVVNDPTLGE VIAVRSMVYL ALSYDHRLVD GADAARFLQT VKTRLEEGAF
     EGDLGL
//
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