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Database: UniProt
Entry: A0A1Z5ICQ3_9LACO
LinkDB: A0A1Z5ICQ3_9LACO
Original site: A0A1Z5ICQ3_9LACO 
ID   A0A1Z5ICQ3_9LACO        Unreviewed;       434 AA.
AC   A0A1Z5ICQ3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   05-JUN-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   Name=pdhC {ECO:0000313|EMBL:GAW99401.1};
GN   ORFNames=IWT30_01370 {ECO:0000313|EMBL:GAW99401.1};
OS   Lactobacillus mixtipabuli.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1435342 {ECO:0000313|EMBL:GAW99401.1, ECO:0000313|Proteomes:UP000198374};
RN   [1] {ECO:0000313|EMBL:GAW99401.1, ECO:0000313|Proteomes:UP000198374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IWT30 {ECO:0000313|EMBL:GAW99401.1,
RC   ECO:0000313|Proteomes:UP000198374};
RA   Tohno M., Tanizawa Y., Arita M.;
RT   "Draft genome sequences of new species of the genus Lactobacillus
RT   isolated from orchardgrass silage.";
RL   Submitted (NOV-2015) 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:GAW99401.1}.
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DR   EMBL; BCMF01000006; GAW99401.1; -; Genomic_DNA.
DR   BioCyc; GCF_002217925:IWT5_RS06785-MONOMER; -.
DR   Proteomes; UP000198374; 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:UP000198374};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:GAW99401.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198374};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:GAW99401.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      135    172       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       70    130       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1Z5ICQ3}.
SQ   SEQUENCE   434 AA;  45922 MW;  2C7FEE517642553E CRC64;
     MAYAFKLPEL GEGMAEGEVA TWDVKEGDTV KEDDVLVEIQ NDKSVSELPS PVAGTIKKIV
     KQEGETAEIG DTLVVIDDGS PDTPDDDASS DASADEAPKE EAAPEPAPAA APAAAAAPAA
     PTGVPAQSDP NKMVLAMPSV RQYARDKGVD ITAVTPTGNH GQILKADIDN FNGAAAPAGA
     PAAAAAPAAA PIKPYKEAQP DLETREPMSM TRKVIAKAMR TSKDISPHVT SFQDVEVSAL
     MANRKKYKAM AADEDIHLTF LPYIVKALVA VLKKFPEFDA SIDSTTDEIV YKHYYNIGIA
     TDTDHGLYVP NIKNADSKGM FEIAKEIADN TQAAKDNKLS ADQMSGGSIT ISNVGSIGGG
     FFTPVINQPE VAILGVGKIA KEPYVNEDGE IEVGNMLKLS LSYDHRLIDG ALAQRALNML
     NDLLHEPELL LMEG
//
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