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Database: UniProt
Entry: A0A1G7CPC4_9ACTN
LinkDB: A0A1G7CPC4_9ACTN
Original site: A0A1G7CPC4_9ACTN 
ID   A0A1G7CPC4_9ACTN        Unreviewed;       469 AA.
AC   A0A1G7CPC4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 6.
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=SAMN05660485_00872 {ECO:0000313|EMBL:SDE41274.1};
OS   Blastococcus sp. DSM 44205.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Blastococcus.
OX   NCBI_TaxID=1550233 {ECO:0000313|EMBL:SDE41274.1, ECO:0000313|Proteomes:UP000198966};
RN   [1] {ECO:0000313|EMBL:SDE41274.1, ECO:0000313|Proteomes:UP000198966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44205 {ECO:0000313|EMBL:SDE41274.1,
RC   ECO:0000313|Proteomes:UP000198966};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNAW01000001; SDE41274.1; -; Genomic_DNA.
DR   Proteomes; UP000198966; 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:UP000198966};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:SDE41274.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198966};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SDE41274.1}.
FT   DOMAIN        8     83       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      187    224       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       84    153       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G7CPC4}.
FT   REGION      166    193       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G7CPC4}.
FT   COMPBIAS    120    134       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1G7CPC4}.
SQ   SEQUENCE   469 AA;  48721 MW;  A4446B02A4DBC019 CRC64;
     MANATPVLRR FALPDVGEGL TEAELLQWLV AVGDTVTVNQ PLCEVETAKA AVELPSPYAG
     RVVELLVEAG ATVDVGSPII TVATGDGGAG TPEPTGTGLT GETNANGRTA VLVGYGPRNT
     EARRRPRRTP DDAPDRAPLL ATAPDARSKP VRHGGLEVGR QAEAAAIRED AASSAPVAPG
     RRGPRPLAKP PVRKYAKDCG VDLATVRGTG PNGVITRADI DAARTPPARA EMAISALAGE
     QRIPIKGVRK HTAAAMVASA FTAPHVTEFL TVDVTRMMKL RRRLAERPEL AGVKVSPLLF
     VAKAVLLAAG RHPMINSSWD EAAQEIVVHG QVNLGIAAAT PRGLVVPNVK DAGRLSLAEL
     AGALADLTET ARAGRTAPAD LTGGTFTITN VGVFGVDTGT PILNPGEAAI LAFGAIRERP
     WVHKGKVRPR QVTQLALSFD HRIVDGELGS RFLADVGALL ADPGAAMAF
//
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