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Database: UniProt
Entry: V9W549_9BACL
LinkDB: V9W549_9BACL
Original site: V9W549_9BACL 
ID   V9W549_9BACL            Unreviewed;       453 AA.
AC   V9W549;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   05-JUN-2019, entry version 31.
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=bfmBB {ECO:0000313|EMBL:AHD05089.1};
GN   ORFNames=ERIC2_c12580 {ECO:0000313|EMBL:AHD05089.1};
OS   Paenibacillus larvae subsp. larvae DSM 25430.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD05089.1, ECO:0000313|Proteomes:UP000029431};
RN   [1] {ECO:0000313|EMBL:AHD05089.1, ECO:0000313|Proteomes:UP000029431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD05089.1,
RC   ECO:0000313|Proteomes:UP000029431};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K.,
RA   Poppinga L., Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
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; CP003355; AHD05089.1; -; Genomic_DNA.
DR   RefSeq; WP_023485483.1; NZ_CP019652.1.
DR   STRING; 697284.ERIC2_c12580; -.
DR   EnsemblBacteria; AHD05089; AHD05089; ERIC2_c12580.
DR   GeneID; 36119620; -.
DR   KEGG; plv:ERIC2_c12580; -.
DR   PATRIC; fig|697284.3.peg.1192; -.
DR   KO; K09699; -.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; PLAR697284:G1HMN-1254-MONOMER; -.
DR   Proteomes; UP000029431; Chromosome.
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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AHD05089.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029431};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029431};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AHD05089.1}.
FT   REGION       92    115       Disordered. {ECO:0000256|MobiDB-lite:
FT                                V9W549}.
SQ   SEQUENCE   453 AA;  49479 MW;  8F4DC85643940E3E CRC64;
     MSEVKGTITE VTVPHLAETL VSATVGKWLK QPGDQVEQYD VLCELFTDKV NIEMPCPIEG
     KLLKILIGEG EEAAVGQAIC LVEVPVSAEE AAQIPAPSDG QPTATEGVPA DGSMRNRYSP
     AVQRLAAEHG IDLNRVPGTG LGGRITRKDV ETYIQNGHAA SAKVAGQTVP GSQVNLEQKV
     SSNTGWAINE PLKQKETPVR TSGIHLSETP PLPHIEIEEA NRGETLIDVT PMRNTIATRM
     RQSVSEIPHA WTMIEVDVTN LVQLRNKVKD EFKRREGINL TYLAFLLKAV VGAIKDYPIM
     NSVWAVDKII VKRDINLSLA VGTEDSVMTP VIQKADQKNI AGLAQEIDDL TKRARAGKLS
     LNDMQGGTFT INNTGSFGSI LSYPIINYPQ AAILTFESIV KKPVVIQDMI AVRSMVNLCL
     SLDHRILDGV ICGRFLQRVK ENLESYNLET SLY
//
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