(data stored in ACNUC7421 zone)

EMBL: CP001743.PE354

CP001743.PE354       Location/Qualifiers
FT   CDS             complement(334925..336244)
FT                   /codon_start=1
FT                   /transl_table=11
FT                   /locus_tag="Mrub_0359"
FT                   /product="nucleotide sugar dehydrogenase"
FT                   /EC_number="1.1.1.22"
FT                   /note="TIGRFAM: nucleotide sugar dehydrogenase; PRIAM:
FT                   UDP-glucose 6-dehydrogenase; PFAM: UDP-glucose/GDP-mannose
FT                   dehydrogenase; UDP-glucose/GDP-mannose dehydrogenase
FT                   dimerisation; UDP-glucose/GDP-mannose dehydrogenase ;
FT                   6-phosphogluconate dehydrogenase NAD-binding;
FT                   InterProIPR014027:IPR014026:IPR001732:IPR006115:IPR 017476;
FT                   KEGG: ank:AnaeK_1384 nucleotide sugar dehydrogenase; COGs:
FT                   COG0677 UDP-N-acetyl-D-mannosaminuronate dehydrogenase;
FT                   SPTR: A6CP32 UDP-N-acetyl-D-mannosaminuronate
FT                   dehydrogenase; PFAM: UDP-glucose/GDP-mannose dehydrogenase
FT                   family, central domain; UDP-glucose/GDP-mannose
FT                   dehydrogenase family, NAD binding domain;
FT                   UDP-glucose/GDP-mannose dehydrogenase family, UDP binding
FT                   domain; TIGRFAM: nucleotide sugar dehydrogenase"
FT                   /db_xref="EnsemblGenomes-Gn:Mrub_0359"
FT                   /db_xref="EnsemblGenomes-Tr:ADD27136"
FT                   /protein_id="ADD27136.1"
FT                   /translation="MQTVVDPKTLLLQRIEDKTALVGVVGMGYVGLPFAVEKAKVGYRV
FT                   VGIDRSAKRVAMINQGQNYIGDVKDEELRDLVAQGLIRATTGFEEVPELDVIVIAVPTP
FT                   LTKNLVPDLQYVEGVTREIAKYLRPGQLVSLESTTYPGTTEEVMLPILEQSGLKLNQDF
FT                   FLAHSPERVDPGNARYTTKNTNKVVGGVGPQSLEVAVAFYSKTINHVVPVSSAKAAEMV
FT                   KVFENTFRAVNIALVNELTLLCDRMDLNVWEVLDAAFTKPFGIMPFYPGPGVGGHCIPL
FT                   DPHYLEWKAKEYNFNTHFINLAGEINRKMPEFTVDKAARVLSQHGKPLRGAKVVLLGMA
FT                   YKANLDDYRESPAIEVFKLLQKRGAEVVFHDSWTPHVEEHGFVADSVELTDELLQNADL
FT                   VIITTNHSNVDYARVVALSKVVLDTRYATRGIKADNVVLL"
     MQTVVDPKTL LLQRIEDKTA LVGVVGMGYV GLPFAVEKAK VGYRVVGIDR SAKRVAMINQ        60
     GQNYIGDVKD EELRDLVAQG LIRATTGFEE VPELDVIVIA VPTPLTKNLV PDLQYVEGVT       120
     REIAKYLRPG QLVSLESTTY PGTTEEVMLP ILEQSGLKLN QDFFLAHSPE RVDPGNARYT       180
     TKNTNKVVGG VGPQSLEVAV AFYSKTINHV VPVSSAKAAE MVKVFENTFR AVNIALVNEL       240
     TLLCDRMDLN VWEVLDAAFT KPFGIMPFYP GPGVGGHCIP LDPHYLEWKA KEYNFNTHFI       300
     NLAGEINRKM PEFTVDKAAR VLSQHGKPLR GAKVVLLGMA YKANLDDYRE SPAIEVFKLL       360
     QKRGAEVVFH DSWTPHVEEH GFVADSVELT DELLQNADLV IITTNHSNVD YARVVALSKV       420
     VLDTRYATRG IKADNVVLL                                                    439
//

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