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Database: UniProt/TrEMBL
Entry: B0C2A9_ACAM1
LinkDB: B0C2A9_ACAM1
Original site: B0C2A9_ACAM1 
ID   B0C2A9_ACAM1            Unreviewed;       446 AA.
AC   B0C2A9;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   25-OCT-2017, entry version 70.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=AM1_3571 {ECO:0000313|EMBL:ABW28561.1};
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW28561.1, ECO:0000313|Proteomes:UP000000268};
RN   [1] {ECO:0000313|EMBL:ABW28561.1, ECO:0000313|Proteomes:UP000000268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA   Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA   Mimuro M., Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW28561.1; -; Genomic_DNA.
DR   RefSeq; WP_012163956.1; NC_009925.1.
DR   ProteinModelPortal; B0C2A9; -.
DR   STRING; 329726.AM1_3571; -.
DR   PRIDE; B0C2A9; -.
DR   EnsemblBacteria; ABW28561; ABW28561; AM1_3571.
DR   KEGG; amr:AM1_3571; -.
DR   eggNOG; ENOG4107UKP; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000000268; 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   Complete proteome {ECO:0000313|Proteomes:UP000000268};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:ABW28561.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABW28561.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   446 AA;  45427 MW;  A58434E753DA54A6 CRC64;
     MIHEVFMPAL SSTMEEGKIV SWSKEPGDKV EKGETVLVVE SDKADMDVES FHEGYLAAIA
     VPAGGVAKVG AAIGYVAETE AEIAEAQKKA SAAESAAPAP AAPAPAPAAP APAAVAPAPP
     AAAPAPVATI PVAPAATLNG GSAPAAPSNG RVVVSPRARK LAKQFKVDLN TLTGSGPHGR
     IVAADIEAAS GQTSTTATAP AASSAAPQPS LPASAPLPAG AAAGEVVPFN TLQQAVVNNM
     VASLAVPTFH VEYSIVTDAL DQLYKQVKTK GVTMTALLAK AVAVTLRQHP LVNASCAPQG
     IQYSSAINIA VAVAMPGGGL ITPVLQQADQ MDLYSLSRTW RDLVARARSK QLQPDEYSTG
     TFTLSNLGMF GVNSFDAILP PGQGSILAIG GSKPQVVADD QGMMGVKRLM NVNITCDHRV
     IYGADAAAFL KDLAELIETN PQSLTL
//
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