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Database: UniProt/TrEMBL
Entry: A2CBK4_PROM3
LinkDB: A2CBK4_PROM3
Original site: A2CBK4_PROM3 
ID   A2CBK4_PROM3            Unreviewed;       439 AA.
AC   A2CBK4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   25-OCT-2017, entry version 71.
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=pdhC {ECO:0000313|EMBL:ABM78864.1};
GN   OrderedLocusNames=P9303_21291 {ECO:0000313|EMBL:ABM78864.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM78864.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM78864.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM78864.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM78864.1; -; Genomic_DNA.
DR   ProteinModelPortal; A2CBK4; -.
DR   EnsemblBacteria; ABM78864; ABM78864; P9303_21291.
DR   KEGG; pmf:P9303_21291; -.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000002274; 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:ABM78864.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002274};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABM78864.1}.
FT   DOMAIN        1     71       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   439 AA;  45709 MW;  03A5DF6E4F7A66BF CRC64;
     MPALSSTMTE GKIVEWLKQP GDKVGRGESV LVVESDKADM DVESFQDGYL AAVLMPAGRS
     APVGETIGLI VESEAEIAAV QANAPAAPAS DPAPLKAAAK VVDDHAPAST PAPVVESPPV
     AAPPPVTSQA VESDKRIVAS PRAKKLAAQM GVDLAKLRGS GPHGRIQAED VQLAAGQPIS
     VPQVAEGNAS FATTHATSAG VAHAVSSPVG QSFGAPGETA AFNNLQQAVN RNMEASLAFP
     CFRVGYTITT DQLDAFYKQV KPKGVTMTAL LAKAVALTLV RHPQVNAAYS TAGMVYPEQV
     NVAIAVAMDD GGLITPVLQN ADRTDLYEMS RQWADLVKRS RSKQLQPEEY STGTFTLSNL
     GMFGVDRFDA ILPPGTGAIL AVAASRPAVV AGKDGSIGVK RQMQVNLTAD HRVIYGADGA
     AFLKDLAELI ETRVESLAL
//
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