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Database: UniProt/TrEMBL
Entry: A4CJP9_ROBBH
LinkDB: A4CJP9_ROBBH
Original site: A4CJP9_ROBBH 
ID   A4CJP9_ROBBH            Unreviewed;       572 AA.
AC   A4CJP9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   OrderedLocusNames=RB2501_09645 {ECO:0000313|EMBL:EAR17157.1};
OS   Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR17157.1, ECO:0000313|Proteomes:UP000009049};
RN   [1] {ECO:0000313|EMBL:EAR17157.1, ECO:0000313|Proteomes:UP000009049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC   {ECO:0000313|Proteomes:UP000009049};
RX   PubMed=19767438; DOI=10.1128/JB.01191-09;
RA   Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL   J. Bacteriol. 191:7144-7145(2009).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP001712; EAR17157.1; -; Genomic_DNA.
DR   RefSeq; WP_015753912.1; NC_013222.1.
DR   ProteinModelPortal; A4CJP9; -.
DR   STRING; 313596.RB2501_09645; -.
DR   EnsemblBacteria; EAR17157; EAR17157; RB2501_09645.
DR   KEGG; rbi:RB2501_09645; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H0NG1; -.
DR   BioCyc; RBIF313596:GH7G-1286-MONOMER; -.
DR   Proteomes; UP000009049; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate 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; IPR006257; LAT1.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009049};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:EAR17157.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009049};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:EAR17157.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      136    211       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   572 AA;  59980 MW;  579FA8F9617FE292 CRC64;
     MAEIIKMPRL SDTMEEGTVA KWLKQVGDKI EEGDILAEIE TDKATMEFES FYEGTLLHIG
     IEEGDGAPVD ALLAIVGEEG EDISGLIDGA GSGDAGAGED TKETVAEEAA TGDGSEDAET
     ASGDDAGGQA EVPEGVEIIR MPRLSDTMEE GTVASWIKKK GDAVEEGDIL AEIETDKATM
     EFESFYSGTL LHIGIEEGES APVDAVLAVI GPEGTDVEAV LSAGSGSGKP AATEEKGAEA
     KKESSEEKAA STDGAAAGRE EARSGGSSSG DGRIFISPLA RKMAEEKGID LSDVEGTGDN
     GRIVKRDIEN YTPSAKPAAS VGEGAAKAPA EQAVPASAAS MAPAGEESVE EVKNSQMRKV
     IAKRLSESKF TAPHYYLTIE VDMSQAMASR ARINELPDTK VSFNDMVVKA CAMALRKHPQ
     VNTTWNGDTT KYNGHVHIGV AVAVEEGLVV PVLKFTDQMS LTAIGASVKD LAGRARNKKL
     TPAEMEGSTF TVSNLGMFGI REFTSIINQP NSAILSVGAI VEKPVVRDGQ IVVGHTMTIT
     LACDHRTVDG ATGAQFLQTL RAYLEHPVTM LA
//
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