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Database: UniProt/TrEMBL
Entry: K9RE62_9CYAN
LinkDB: K9RE62_9CYAN
Original site: K9RE62_9CYAN 
ID   K9RE62_9CYAN            Unreviewed;       439 AA.
AC   K9RE62;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-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=Riv7116_2850 {ECO:0000313|EMBL:AFY55347.1};
OS   Rivularia sp. PCC 7116.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Rivularia.
OX   NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY55347.1, ECO:0000313|Proteomes:UP000010380};
RN   [1] {ECO:0000313|EMBL:AFY55347.1, ECO:0000313|Proteomes:UP000010380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY55347.1,
RC   ECO:0000313|Proteomes:UP000010380};
RG   US DOE Joint Genome Institute;
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 Rivularia sp. PCC 7116.";
RL   Submitted (AUG-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; CP003549; AFY55347.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFY55347; AFY55347; Riv7116_2850.
DR   KEGG; riv:Riv7116_2850; -.
DR   PATRIC; fig|373994.3.peg.3018; -.
DR   KO; K00627; -.
DR   OrthoDB; POG091H04EL; -.
DR   BioCyc; RSP373994:GLJQ-2756-MONOMER; -.
DR   Proteomes; UP000010380; 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; IPR036625; E3-bd_dom_sf.
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:AFY55347.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010380};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:AFY55347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010380};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AFY55347.1}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   439 AA;  45912 MW;  1098AFA8EEEB5590 CRC64;
     MSIHEIFMPA LSSTMTEGKI VSWEKSPGDK VEKGETVVVV ESDKADMDVE SFYEGYMAHI
     LVEAGSSAPV GSAIAFLAET EAEIETAIAQ AKSSGAAPEP AKVAAATAPG QTAQSAPTTS
     TNGTSQNGAA RGSGRKIASP RARKLAKEFK VDLSGISGSG PHGRIIAQDV ETAAGKSTTV
     KSSAPATAQP TAAPAHSSPK VTPAATPAPM PVAATPGQTV PLTTLQNAVV RTMNHSLSVP
     TFHVGYSIAT DELNKLYKQI KSKGVTMTAL LAKAVAMTLQ KHPLLNTNYS EQGIVYPANI
     NIAVAVAMDD GGLITPVLQN ADRLDIYSLS RNWKSLVERA RAKQLQPEEY SSGTFTISNL
     GMFGVDTFDA ILPPNQGSIL AIAASRPEVV ATPDGMMGVR TLMKVNITCD HRVIYGAHAA
     AFLKDLAQLI ETNSQSLTM
//
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