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Database: UniProt/TrEMBL
Entry: A0A0K2LUY3_9NOST
LinkDB: A0A0K2LUY3_9NOST
Original site: A0A0K2LUY3_9NOST 
ID   A0A0K2LUY3_9NOST        Unreviewed;       429 AA.
AC   A0A0K2LUY3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-MAR-2018, entry version 16.
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=AA650_02345 {ECO:0000313|EMBL:ALB39456.1};
OS   Anabaena sp. WA102.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB39456.1, ECO:0000313|Proteomes:UP000056652};
RN   [1] {ECO:0000313|EMBL:ALB39456.1, ECO:0000313|Proteomes:UP000056652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA102 {ECO:0000313|EMBL:ALB39456.1,
RC   ECO:0000313|Proteomes:UP000056652};
RA   Brown N.M.;
RT   "The finished genome of an anatoxin-a-producing Anabaena isolate
RT   reveals extensive genome rearrangement.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP011456; ALB39456.1; -; Genomic_DNA.
DR   RefSeq; WP_053537808.1; NZ_CP011456.1.
DR   EnsemblBacteria; ALB39456; ALB39456; AA650_02345.
DR   KEGG; awa:AA650_02345; -.
DR   PATRIC; fig|1647413.5.peg.563; -.
DR   KO; K00627; -.
DR   Proteomes; UP000056652; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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:UP000056652};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      131    168       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   429 AA;  44780 MW;  89F2C9813C354BD4 CRC64;
     MSINEVFMPA LSSTMTEGKI VSWVKSPGDK VEKGETVVVV ESDKADMDVE TFYEGYLAHI
     IVPAGETAPV GAAIAYIAET EAEIATAKSL ANADNAAAPS TPAPTPVAVA AVAAPVTASQ
     NGSNHQPGRV VVSPRARKLA KELKIDLNTL TGSGPYGRIV AEDVEVAVGK VQPIATPVVT
     AAPVPVPVPV PVAAPAPVPV VSSAVPGQIV PFTTLQNAVV RGMVASLSVP VFRVSYTIST
     DGLDKLYKQI KSKGVTMTAL LAKAVAVTLQ KHPILNASYS DEGIVNHPNI NVSVAVAMDD
     GGLITPVLQN ADTVDIYSLS RNWKSLVERA RAKQLQPAEY NSGTFTLSNL GMFGVDTFDA
     ILPPGQGSIL AIGASRPQVV ATVDGLFGVR QQMQVTVTCD HRIIYGADAA GFLQDLAKLI
     ETNPQFLTM
//
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