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Database: UniProt
Entry: L7EVV7_9ACTN
LinkDB: L7EVV7_9ACTN
Original site: L7EVV7_9ACTN 
ID   L7EVV7_9ACTN            Unreviewed;       487 AA.
AC   L7EVV7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   16-JAN-2019, entry version 31.
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=STRTUCAR8_05476 {ECO:0000313|EMBL:ELP62841.1};
OS   Streptomyces turgidiscabies Car8.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP62841.1, ECO:0000313|Proteomes:UP000010931};
RN   [1] {ECO:0000313|EMBL:ELP62841.1, ECO:0000313|Proteomes:UP000010931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Car8 {ECO:0000313|EMBL:ELP62841.1,
RC   ECO:0000313|Proteomes:UP000010931};
RX   PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA   Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT   "Streptomyces turgidiscabies Car8 contains a modular pathogenicity
RT   island that shares virulence genes with other actinobacterial plant
RT   pathogens.";
RL   Plasmid 65:118-124(2011).
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:ELP62841.1}.
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DR   EMBL; AEJB01000572; ELP62841.1; -; Genomic_DNA.
DR   RefSeq; WP_006382227.1; NZ_AEJB01000572.1.
DR   EnsemblBacteria; ELP62841; ELP62841; STRTUCAR8_05476.
DR   PATRIC; fig|698760.3.peg.8233; -.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; STUR698760:G1HE8-8300-MONOMER; -.
DR   Proteomes; UP000010931; 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; 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; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010931};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        9     85       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      188    225       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   487 AA;  50377 MW;  FEA256BE1BA03790 CRC64;
     MTTMTDASVR EFKMPDVGEG LTEAEILKWY VQPGDTVTDG QVVCEVETAK AAVELPIPYD
     GVVRSLHFPE GTTVDVGTSI IAVDVTGGAG AAVEAEAPVQ AEAPRAAPEE AKPPARQPVL
     VGYGVAVSST KRRPRKGADI PAQEVAAAVQ HELNGHSGRV ESTNGHGALT GPGLAGQALL
     AAVTARPLAK PPVRKLAKDL GVDLATVTPS GPDGVITRED VHAAVAPTAP EPVSTAPAVP
     AAPAPAATYD GARETRVPVR GVRKATAAAM VGSAFTAPHV TEFVTVDVTR TLKLVEELKA
     APDSYGLAGL RVNPLLLIAK ALLVAIKRHP DINASWDEAN QEIVLKHYVN LGIAAATPRG
     LIVPNIKDAH DKTLPQLAEA LGELVSTARD GKTSPGAMQG GTVTITNVGV FGVDTGTPIL
     PPGEAAILAV GSIKLQPWVH KGKVKPRQVT TLALSFDHRL VDGELGSKVL ADVAAILEQP
     KKLITWA
//
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