(data stored in ACNUC7421 zone)

EMBL: CP002343.PE245

CP002343.PE245       Location/Qualifiers
FT   CDS             270237..271715
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Intca_0250"
FT                   /product="catalytic domain-containing protein of components
FT                   of various dehydrogenase complexes"
FT                   /note="COGs: COG0508 Pyruvate/2-oxoglutarate dehydrogenase
FT                   complex dihydrolipoamide acyltransferase (E2) protein;
FT                   InterPro IPR000089: IPR004167: IPR001078; KEGG:
FT                   kse:Ksed_02370 pyruvate/2-oxoglutarate dehydrogenase
FT                   complex, dihydrolipoamide acyltransferase component; PFAM:
FT                   catalytic domain-containing protein of components of
FT                   various dehydrogenase complexes; biotin/lipoyl attachment
FT                   domain-containing protein; E3 binding domain protein; SPTR:
FT                   Putative dihydrolipoamide acyltransferase component; PFAM:
FT                   2-oxoacid dehydrogenases acyltransferase (catalytic
FT                   domain); e3 binding domain; Biotin-requiring enzyme"
FT                   /db_xref="EnsemblGenomes-Gn:Intca_0250"
FT                   /db_xref="EnsemblGenomes-Tr:ADU46807"
FT                   /db_xref="GOA:E6S6S1"
FT                   /db_xref="InterPro:IPR000089"
FT                   /db_xref="InterPro:IPR001078"
FT                   /db_xref="InterPro:IPR004167"
FT                   /db_xref="InterPro:IPR011053"
FT                   /db_xref="InterPro:IPR023213"
FT                   /db_xref="InterPro:IPR036625"
FT                   /db_xref="UniProtKB/TrEMBL:E6S6S1"
FT                   /protein_id="ADU46807.1"
FT                   /translation="MAIRTFNLPDPGEGLVEAEIVEWKVAPGDTVKVNDMVLEIETAKS
FT                   LVELPIPWSGTVRELLVNVGDTVDVGTPIISIDDGQGGDAPAAPAGETAQAPKGEQQEA
FT                   NLVGYGAKAGATARRARKQGDGRMPLGSVPESAPARAAAPTETEQVAEAEPVAEQTAPA
FT                   PRTESPAPAVEPVAREGRPKAKPPVRKLAKDLGVDLWSVPGSGPDGIITRDDVESFARG
FT                   VNLPERQGVSDQGEAAASVSAAPSPAAYPFGSGEREVRTPIKGVRKMTAQAMVGSAFTA
FT                   PHVTEWVTVDVTRTMELVDRLKRSREFKDVKVTPLLVLARAMILAIRRNPGVNATWDEA
FT                   AQEIVQKNYVNLGIAAATPRGLIVPNIKDAHGMSMLQLAQAIGELTATAREGRTQPAEM
FT                   SGGTITITNVGVFGVDSGTPIINPGESAIVAFGAIRKMPWVVEGPAGDEIVVRHVTQLA
FT                   MSFDHRLVDGELGSRFLADLAAIMADPGQALVWG"
     MAIRTFNLPD PGEGLVEAEI VEWKVAPGDT VKVNDMVLEI ETAKSLVELP IPWSGTVREL        60
     LVNVGDTVDV GTPIISIDDG QGGDAPAAPA GETAQAPKGE QQEANLVGYG AKAGATARRA       120
     RKQGDGRMPL GSVPESAPAR AAAPTETEQV AEAEPVAEQT APAPRTESPA PAVEPVAREG       180
     RPKAKPPVRK LAKDLGVDLW SVPGSGPDGI ITRDDVESFA RGVNLPERQG VSDQGEAAAS       240
     VSAAPSPAAY PFGSGEREVR TPIKGVRKMT AQAMVGSAFT APHVTEWVTV DVTRTMELVD       300
     RLKRSREFKD VKVTPLLVLA RAMILAIRRN PGVNATWDEA AQEIVQKNYV NLGIAAATPR       360
     GLIVPNIKDA HGMSMLQLAQ AIGELTATAR EGRTQPAEMS GGTITITNVG VFGVDSGTPI       420
     INPGESAIVA FGAIRKMPWV VEGPAGDEIV VRHVTQLAMS FDHRLVDGEL GSRFLADLAA       480
     IMADPGQALV WG                                                           492
//

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