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Database: UniProt/TrEMBL
Entry: K9V7X1_9CYAN
LinkDB: K9V7X1_9CYAN
Original site: K9V7X1_9CYAN 
ID   K9V7X1_9CYAN            Unreviewed;       431 AA.
AC   K9V7X1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 26.
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=Cal6303_4622 {ECO:0000313|EMBL:AFZ03522.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ03522.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFZ03522.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ03522.1,
RC   ECO:0000313|Proteomes:UP000010477};
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A.,
RA   Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X.,
RA   Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-2012) 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; CP003610; AFZ03522.1; -; Genomic_DNA.
DR   RefSeq; WP_015200138.1; NC_019751.1.
DR   EnsemblBacteria; AFZ03522; AFZ03522; Cal6303_4622.
DR   KEGG; calt:Cal6303_4622; -.
DR   PATRIC; fig|1170562.3.peg.5053; -.
DR   KO; K00627; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000010477; 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; 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; IPR004167; E3-bd.
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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AFZ03522.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010477};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AFZ03522.1}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   431 AA;  44847 MW;  4AC94516C07FF7AD CRC64;
     MSIYEVFMPA LSSTMTEGKI VSWVKSPGDK VEKGETVVVV ESDKADMDVE SFYEGYLAHI
     IVPAGESAPV GNAIAYVVET EAEIAGAVSK ATSAAAPATP SIAAKAATNG ATTTAAPVAT
     TTNASNHREG RIVASPRAKK LAKELKVDLN AIASGSGPFG RIVAEDIEAA AGRVSTPPTV
     TAAPAPVAAP PAIPRTAPAP APVATVVPGQ TTPFNALQNA VTRNMVASLT VPVFRANYTI
     TTDALDSLYK QIKSKGVTMT ALLAKAIALT LKKHPIINAS YSEQGIVYHS DINVSVAVAM
     DDGGLITPVL RNADAIDIYS LSRTWKSLVE RARAKQLQPE EYSTGTFTIS NLGMFGVDTF
     DAILPPGQGS ILAVGASRPQ VVATGDGMFG VKQQMQVNIT CDHRIIYGAD GAAFLRDLAK
     LIETNAQSLT L
//
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