(data stored in SCRATCH9089 zone)

EMBL: CP002209.PE55

CP002209.PE55        Location/Qualifiers
FT   CDS             complement(71773..73128)
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Fbal_0055"
FT                   /product="NADPH-glutathione reductase"
FT                   /EC_number="1.8.1.7"
FT                   /note="COGs: COG1249 Pyruvate/2-oxoglutarate dehydrogenase
FT                   complex dihydrolipoamide dehydrogenase (E3); InterPro
FT                   IPR013027: IPR000103: IPR000815: IPR001327: IPR 004099:
FT                   IPR012999: IPR006322; KEGG: slo:Shew_3660 glutathione
FT                   reductase; PFAM: pyridine nucleotide-disulphide
FT                   oxidoreductase dimerisation region; FAD-dependent pyridine
FT                   nucleotide-disulphide oxidoreductase; SPTR: A3UP40
FT                   Glutathione reductase; TIGRFAM: glutathione-disulfide
FT                   reductase; PFAM: Pyridine nucleotide-disulphide
FT                   oxidoreductase; Pyridine nucleotide-disulphide
FT                   oxidoreductase, dimerisation domain; TIGRFAM:
FT                   glutathione-disulfide reductase, animal/bacterial"
FT                   /db_xref="EnsemblGenomes-Gn:Fbal_0055"
FT                   /db_xref="EnsemblGenomes-Tr:ADN74269"
FT                   /db_xref="GOA:E1SVB5"
FT                   /db_xref="InterPro:IPR001100"
FT                   /db_xref="InterPro:IPR004099"
FT                   /db_xref="InterPro:IPR006322"
FT                   /db_xref="InterPro:IPR012999"
FT                   /db_xref="InterPro:IPR016156"
FT                   /db_xref="InterPro:IPR023753"
FT                   /db_xref="InterPro:IPR036188"
FT                   /db_xref="UniProtKB/TrEMBL:E1SVB5"
FT                   /protein_id="ADN74269.1"
FT                   /translation="MAQQFDYIVLGAGSGGIASANRAAMRGAKVLLIEAQHLGGTCVNV
FT                   GCVPKKVMWFGAQVAEAIKLYGPDYGFDTTLNQFSWSKLVESREAYIERIHGGYNRGLD
FT                   ANGVTLVKGFGKFVDAKTVEVNGEHYTAPNILIATGGRPTIPAIPGAEHGIDSNGFFAL
FT                   TEQPKRVAVVGAGYIAVELAGVLHSLGSETHLLVRKHAPLRNFDPMIVDTLVKLMAAEG
FT                   PTLHTHSIPKAVEKEADGSLTLHLENGNSLNVDCLIWAIGREPATDKINIEASGVKVNE
FT                   RGFIPVDEYQNTNVPGIYTVGDIMEGGIELTPVAVKAGRALSERLFGGQPEAKMDYSLV
FT                   PTVVFSHPAIGTIGLTEPQAREQYGDDNVKVYTSSFAAMYTAVTAHRQATEMKLVCVGP
FT                   EEKIVGLHGIGFGMDEILQGFAVAIKMGATKADFDATVALHPTSAEEFVTMR"
     MAQQFDYIVL GAGSGGIASA NRAAMRGAKV LLIEAQHLGG TCVNVGCVPK KVMWFGAQVA        60
     EAIKLYGPDY GFDTTLNQFS WSKLVESREA YIERIHGGYN RGLDANGVTL VKGFGKFVDA       120
     KTVEVNGEHY TAPNILIATG GRPTIPAIPG AEHGIDSNGF FALTEQPKRV AVVGAGYIAV       180
     ELAGVLHSLG SETHLLVRKH APLRNFDPMI VDTLVKLMAA EGPTLHTHSI PKAVEKEADG       240
     SLTLHLENGN SLNVDCLIWA IGREPATDKI NIEASGVKVN ERGFIPVDEY QNTNVPGIYT       300
     VGDIMEGGIE LTPVAVKAGR ALSERLFGGQ PEAKMDYSLV PTVVFSHPAI GTIGLTEPQA       360
     REQYGDDNVK VYTSSFAAMY TAVTAHRQAT EMKLVCVGPE EKIVGLHGIG FGMDEILQGF       420
     AVAIKMGATK ADFDATVALH PTSAEEFVTM R                                      451
//

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