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Database: UniProt
Entry: A0A024GLY3_9STRA
LinkDB: A0A024GLY3_9STRA
Original site: A0A024GLY3_9STRA 
ID   A0A024GLY3_9STRA        Unreviewed;       420 AA.
AC   A0A024GLY3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   18-SEP-2019, entry version 22.
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=BN9_087620 {ECO:0000313|EMBL:CCI47746.1};
OS   Albugo candida.
OC   Eukaryota; Stramenopiles; Oomycetes; Albuginales; Albuginaceae;
OC   Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI47746.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI47746.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI47746.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D.,
RA   Van Oosterhout C., Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) 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:CCI47746.1}.
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DR   EMBL; CAIX01000184; CCI47746.1; -; Genomic_DNA.
DR   OrthoDB; 747232at2759; -.
DR   Proteomes; UP000053237; 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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053237};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        1     65       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      120    157       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       82    116       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      159    186       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     82    110       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    159    173       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   420 AA;  45696 MW;  64B871A91BCBA31A CRC64;
     METGTITKWC KQEGESIAAG DIICEVETDK AVVEFESQDD YYLAKILKPE GSSDIRVGEP
     IFVSTLDQTS LEAFKNYQVE EQQSQSVSSQ QIEVDTTPSS SASSSPTRSE KEVNTSDRVF
     ASPLAKKLAR EWNVSLGGIT GSGPRSRIVK ADVEEAINNV SSSSKSDTVQ EPSRAPSRVG
     GEEAQSSDYP LNPLAVEFAD SLTRQKTTVP HFHLAIDLTL DKLLDARDRL NAGRPQDRQL
     SVYDFIVRAA SLAMKTVPEV NSAWKDSFIR QFHSVNINLI LSSTTKHGGG TIAPMVANVQ
     QKGLDEINQD VSQLLESASG TSLSSQQLGR GTFTICNVGM YEVRSMAGII CPEQACLLGL
     GTIEKKVVPN EDPDAKEIYQ FATKMTATLA CDHRVVDGAV GAQWLAVFKE LVEDPLKMIL
//
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