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Database: UniProt
Entry: A0A1I4QIQ3_9ACTN
LinkDB: A0A1I4QIQ3_9ACTN
Original site: A0A1I4QIQ3_9ACTN 
ID   A0A1I4QIQ3_9ACTN        Unreviewed;       599 AA.
AC   A0A1I4QIQ3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 7.
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=SAMN04487980_100141 {ECO:0000313|EMBL:SFM39941.1};
OS   Streptomyces sp. cf124.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFM39941.1, ECO:0000313|Proteomes:UP000198530};
RN   [1] {ECO:0000313|EMBL:SFM39941.1, ECO:0000313|Proteomes:UP000198530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF124 {ECO:0000313|EMBL:SFM39941.1,
RC   ECO:0000313|Proteomes:UP000198530};
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; FOUV01000001; SFM39941.1; -; Genomic_DNA.
DR   Proteomes; UP000198530; 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:UP000198530};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      130    205       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      293    330       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       80    132       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I4QIQ3}.
FT   REGION      210    275       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I4QIQ3}.
FT   COMPBIAS    213    275       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A1I4QIQ3}.
SQ   SEQUENCE   599 AA;  59448 MW;  6644F9B11A047F61 CRC64;
     MAVSVTLPAL GESVTEGTVT RWLKAEGERV EADEPLLEVS TDKVDTEIPS PAAGILASIK
     VAEDETVEVG AELALIDDGT GAPAAAPAPA AEEAPAPAPE PAAAAPSTEQ EAPAPAPTAE
     AATGGGSAEG TDVVLPALGE SVTEGTVTRW LKEVGDSVEA DEPLLEVSTD KVDTEIPAPT
     SGVLLEITVA EDETAEVGAK LAVIGAPGAA PAAAPAAPAP APAAAAPAAP APAPAAPAAP
     APAPAPAAPA APAPAPAAAA PVAPAPAPAP VAPAPAAAPA SSAAAKATDE GAYVTPLVRK
     LAAENGVDLG SVKGTGVGGR IRKQDVIAAA EAAKAAAAAP APAAAPAAAA KKAPSLEASP
     LRGQTVKMPR IRKVIGDNMV KALHEQAQLS SVVEVDVTRL MKLRGRAKDS FAAREGVKLS
     PMPFFVKAAA QALKAHAPIN AKINEGEGTI TYFDTENVGI AVDSEKGLMT PVIKHAGDLN
     IAGIAKATAE LAGKVRANKI TPDELSGATF TISNTGSRGA LFDTIIVPPG QVAILGIGAT
     VKRPAVIETE EGTVIGVRDM TYLTLSYDHR LVDGADAARY LTAVKAILEA GEFEVELGL
//
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