(data stored in SCRATCH3701 zone)

EMBL: CP001994.PE393

CP001994.PE393       Location/Qualifiers
FT   CDS             complement(417043..418386)
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Mmah_0399"
FT                   /product="FAD-dependent pyridine nucleotide-disulfide
FT                   oxidoreductase"
FT                   /note="COGs: COG1249 Pyruvate/2-oxoglutarate dehydrogenase
FT                   complex dihydrolipoamide dehydrogenase (E3);
FT                   InterProIPR013027:IPR000103:IPR000815:IPR001327:IPR
FT                   004099:IPR012999; KEGG: gbm:Gbem_3786 pyridine
FT                   nucleotide-disulphide oxidoreductase dimerisation region;
FT                   PFAM: FAD-dependent pyridine nucleotide-disulphide
FT                   oxidoreductase; pyridine nucleotide-disulphide
FT                   oxidoreductase dimerisation region; SPTR: Q46EZ2
FT                   Glutathione reductase (NADPH); PFAM: Pyridine
FT                   nucleotide-disulphide oxidoreductase; Pyridine
FT                   nucleotide-disulphide oxidoreductase, dimerisation domain"
FT                   /db_xref="EnsemblGenomes-Gn:Mmah_0399"
FT                   /db_xref="EnsemblGenomes-Tr:ADE35931"
FT                   /db_xref="GOA:D5E9T0"
FT                   /db_xref="InterPro:IPR001100"
FT                   /db_xref="InterPro:IPR004099"
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:D5E9T0"
FT                   /protein_id="ADE35931.1"
FT                   /translation="MAREYDIVIIGTGVAGTVCANKASAAGMKIAITDIREYGGTCALR
FT                   GCVPKKVLVGVAETVEQVNRFNKLGIMPQSSVNWNKLMDFKQTFVDNFPQNKEEKFTNM
FT                   DIDTYHGGAKFVSKNEVKIADTILKGKHILIAPGSVPRKTGIKGEENLITSEQFLNLDE
FT                   LPRKIVFVGGGYISFELAHIAARAGSQVTILQRSEVLKQFDRDMVKLLVKASEEAGINV
FT                   NTGISVSSVESTSSGFTVNTRNREGKESRIECDLVVNGSGRIAALEGMELEKGNVETKD
FT                   GFVETNDYMQSVSNPYVYAAGDCVKPGAPLTPVASLQGTTAADNMIKGNVKTVDYTGIP
FT                   STVFTLPPLSSVGISLSESTDRYEVLIHDRSHWYNSRRLSENYAASKVIIEKESQKIAG
FT                   AHILGSHSEEVINIFAMAIRLGLTLSQFKKVVYVFPTVSSEIQSMIRG"
     MAREYDIVII GTGVAGTVCA NKASAAGMKI AITDIREYGG TCALRGCVPK KVLVGVAETV        60
     EQVNRFNKLG IMPQSSVNWN KLMDFKQTFV DNFPQNKEEK FTNMDIDTYH GGAKFVSKNE       120
     VKIADTILKG KHILIAPGSV PRKTGIKGEE NLITSEQFLN LDELPRKIVF VGGGYISFEL       180
     AHIAARAGSQ VTILQRSEVL KQFDRDMVKL LVKASEEAGI NVNTGISVSS VESTSSGFTV       240
     NTRNREGKES RIECDLVVNG SGRIAALEGM ELEKGNVETK DGFVETNDYM QSVSNPYVYA       300
     AGDCVKPGAP LTPVASLQGT TAADNMIKGN VKTVDYTGIP STVFTLPPLS SVGISLSEST       360
     DRYEVLIHDR SHWYNSRRLS ENYAASKVII EKESQKIAGA HILGSHSEEV INIFAMAIRL       420
     GLTLSQFKKV VYVFPTVSSE IQSMIRG                                           447
//

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