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Database: UniProt
Entry: A0A1H0H800_9ACTN
LinkDB: A0A1H0H800_9ACTN
Original site: A0A1H0H800_9ACTN 
ID   A0A1H0H800_9ACTN        Unreviewed;       594 AA.
AC   A0A1H0H800;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JUL-2019, entry version 8.
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=SAMN05192576_3487 {ECO:0000313|EMBL:SDO15041.1};
OS   Nocardioides szechwanensis.
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=1005944 {ECO:0000313|EMBL:SDO15041.1, ECO:0000313|Proteomes:UP000199004};
RN   [1] {ECO:0000313|EMBL:SDO15041.1, ECO:0000313|Proteomes:UP000199004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.11147 {ECO:0000313|EMBL:SDO15041.1,
RC   ECO:0000313|Proteomes:UP000199004};
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; FNIC01000006; SDO15041.1; -; Genomic_DNA.
DR   BioCyc; GCF_900103935:BLR90_RS15235-MONOMER; -.
DR   Proteomes; UP000199004; 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:UP000199004};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199004};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      141    216       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      292    329       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       71    151       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      209    290       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      328    364       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     91    117       Acidic. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    245    268       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    348    362       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   594 AA;  62152 MW;  56CDE6F9C4235169 CRC64;
     MATEVNLPAL GESVTEGTVT RWLKQVGDSV AVDEPLLEVS TDKVDTEIPS PVAGTLLEIK
     AQEDDTIEVG AILAIIGDEG ESAGDSGGES QESEPEPEPE PEPEEKAEPE PEEQAQPEPE
     PEQPAASSEG DSGSGGGGGG GTSVVLPALG ESVTEGTVTR WLKSVGDDVA VDEPLLEVST
     DKVDTEIPSP VAGKLLEIKV EEDETVEVGA ELAVIGSGDA TPAKAEPQAE PKDEEPEPEP
     EPEPEPEEKA APEPEPEKKP EPAQETKPAA EKAPEPSPET SSESSSSEGA GYVTPLVRKL
     AAQHDVDLSA VTGTGVGGRI RKQDVLDAAK ARQAPAPAAA AAAPSAPAAS APSTTPSPLR
     GTTEKISRLR KIIAERMLDS LHSGAQLTQV VEVDVTRIAR LREASKADFL AREGVKLSYL
     PFFAKASIDA LKVHPKLNAT IDTDAGTITY YDRENLAFAV DTEKGLITPV VKDAGDLSIA
     GLAKKIADVA ERTRTNKIGP DELGGGTFTI TNLGSVGALW DTPIINKPQV AILGPGAVVK
     RPVVIDDPDL GETIAVRHMV YLALTYDHRL VDGADAGRFL QDVKKRLEAG QFEI
//
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