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Database: UniProt/TrEMBL
Entry: S8GMY7_TOXGM
LinkDB: S8GMY7_TOXGM
Original site: S8GMY7_TOXGM 
ID   S8GMY7_TOXGM            Unreviewed;       929 AA.
AC   S8GMY7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 19.
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=PDHE2 {ECO:0000313|EMBL:EPT29904.1};
GN   ORFNames=TGME49_206610 {ECO:0000313|EMBL:EPT29904.1};
OS   Toxoplasma gondii (strain ATCC 50611 / Me49).
OC   Eukaryota; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=508771 {ECO:0000313|EMBL:EPT29904.1, ECO:0000313|Proteomes:UP000001529};
RN   [1] {ECO:0000313|EMBL:EPT29904.1, ECO:0000313|Proteomes:UP000001529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50611 / Me49 {ECO:0000313|Proteomes:UP000001529};
RA   Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A.,
RA   Brunk B., Roos D., Caler E., Lorenzi H.;
RL   Submitted (APR-2013) 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; KE138829; EPT29904.1; -; Genomic_DNA.
DR   RefSeq; XP_018637240.1; XM_018779368.1.
DR   GeneID; 7894015; -.
DR   KEGG; tgo:TGME49_206610; -.
DR   Proteomes; UP000001529; Chromosome VIIa.
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; 3.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 3.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR   PROSITE; PS00189; LIPOYL; 3.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:EPT29904.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001529};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:EPT29904.1};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:EPT29904.1}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    929       Dihydrolipoamide acetyltransferase
FT                                component of pyruvate dehydrogenase
FT                                complex. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004552225.
FT   DOMAIN      134    209       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      240    315       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      346    421       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   929 AA;  96880 MW;  9491DDE51B3CA4A3 CRC64;
     MALPSPGILV HVSLFLAAVS SAFGLQLVPS SSPAPSASST SFSGSSAPAF VAPAVSSGSG
     VHSTRPRFFA SPSASSASSV SSTNAGQRPL SAGSSLQTRE RRCGSRLTSS LLCAAEGTVR
     RQETAVGSSL RGAVQEISMP ALSSTMKEGK VVTWSKQVGD RVEPGDVLMV VESDKADMDV
     EAFDSGFMAM HLVREGDAAP VGTTVALLAE KEEDISLIQA KGLSLISASS SPAADSTPAV
     TDLLMPSLSP SLKTARMTVW RKKEGEKVNK GDVLFVVESD KADMDVEAPH DGVLAHIAVR
     EGVTVDVGST VGYLAPSAEV ASAFKNALSD SAAPAAANPS TMPEGAQEIF MPALSSTMTS
     GKVSKWNKAV GDAVHVGDTL MVVESDKADM DVESFDEGYL AAITVAEGES APVGQTVAII
     VPSKDDIAKV QDALTAASTA SSSSPAHAPL SSASSPSTPS SRLSSSDSVS VSSSQSGRPT
     TGGDSRTAAF MKHGQALARW TSPSVDQDVK DQLPEGLTGN DLQQEWLQRI EATMPTTFAA
     LQANPQMQKA LLERLNLRVP PPHTLRVSPA PPPYLKRAVS TYGAATAGVP DTRASGIDRT
     SRGPARDPSG QPLATFNAIE LAKKNKLNLE EVKGTGTNRR ITAADVRQHL HLPSDEATVV
     TSKRENEGKI ESLGVPPPGS VPLDAMQKAV ARNMEATMDV PVFRVSRGIY VDKLEAMVQE
     LKQIVAEQNA AAIAAEGPDA PQQSTVTMSV LLAKAVALTL EKHPIMNAAY NPKDGGQIQH
     PGAVNVAMAV SVDGGLLTPV LRNVNTKSVF ELSADWAVLV DKARKRRLTA EENSAGTFYI
     SNLGMFGVSQ FDAVLPKGVG TIMAVGGTES VPFFPKTGTL DAPAGNPSVR RRMTVTITAD
     HRHIYGSHAA AFLKDFASLL ETRPSALLI
//
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