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Database: UniProt
Entry: A0A0W1LEQ3_9GAMM
LinkDB: A0A0W1LEQ3_9GAMM
Original site: A0A0W1LEQ3_9GAMM 
ID   A0A0W1LEQ3_9GAMM        Unreviewed;       521 AA.
AC   A0A0W1LEQ3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   31-JUL-2019, entry version 18.
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=ATS75_01810 {ECO:0000313|EMBL:KTF18171.1};
OS   Pseudoalteromonas sp. H105.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1348393 {ECO:0000313|EMBL:KTF18171.1, ECO:0000313|Proteomes:UP000054685};
RN   [1] {ECO:0000313|EMBL:KTF18171.1, ECO:0000313|Proteomes:UP000054685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H105 {ECO:0000313|EMBL:KTF18171.1,
RC   ECO:0000313|Proteomes:UP000054685};
RA   Duhaime M.B., Sullivan M.B., Wichels A.;
RT   "Six Pseudoalteromonas strains isolated from surface waters of
RT   Kabeltonne offshore Helgoland, North Sea.";
RL   Submitted (DEC-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:KTF18171.1}.
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DR   EMBL; LOFH01000001; KTF18171.1; -; Genomic_DNA.
DR   RefSeq; WP_058558711.1; NZ_LOFH01000001.1.
DR   EnsemblBacteria; KTF18171; KTF18171; ATS75_01810.
DR   Proteomes; UP000054685; 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; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054685};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:KTF18171.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      104    179       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      222    259       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       80    100       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      269    289       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   521 AA;  56638 MW;  F6D5D0866109710D CRC64;
     MAKDFILPDI GEGIVECEVV EWLVSEGDTV AEDQPICDVM TDKALVQIPA VHDGVISKLY
     YQKGDIAAVH APLFAMEVAG EETQTQEIEK PSENTENNSS VEQLEDFILP DIGEGIVECE
     IVEWLVAEGE QIEEDQAVCD VMTDKALVQI PAKHTGTVHK LYYAKGEVAQ VHSPLFKMSI
     AGTQQVNVDV NEAVVKAQTN AVEPKAMIAK DQSAKVVNKK AVASPAVRRK AREMDVDLTC
     VPGSGKNGRI YKEDIEQFVN GQVPNTIDTS PLKAEASEQN SNTPSLGGTR VESIKGIKAA
     MAKQMVASVS TIPHFTFCDE IDLTELIALR SSLKEQYKQQ GVKLTMMPFF IKALSLALKE
     FPVLNTKVND ECTELTYFDD HNIGMAVDSK IGLLVPNIKQ CQSKSIVDVA NAVTRLTEAA
     REGRVSPDDL KGGTISISNI GAIGGTIATP IINKPEVAIV ALGKLQHLPR FDSKGNVVSK
     AIMQVSWSGD HRVIDGGTIA RFNNLWKSYL EEPAKMMMAM S
//
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