Comparing AO356_28535 FitnessBrowser__pseudo5_N2C3_1:AO356_28535 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
4im7A Crystal structure of fructuronate reductase (ydfi) from e. Coli cft073 (efi target efi-506389) complexed with nadh and d-mannonate
45% identity, 94% coverage: 18:472/485 of query aligns to 21:472/483 of 4im7A
1m2wA Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and d-mannitol (see paper)
38% identity, 99% coverage: 2:480/485 of query aligns to 13:488/492 of 1m2wA
1lj8A Crystal structure of mannitol dehydrogenase in complex with NAD (see paper)
38% identity, 99% coverage: 2:480/485 of query aligns to 13:488/492 of 1lj8A
7rk5B Mannitol-2-dehydrogenase bound to nadh from aspergillus fumigatus
34% identity, 96% coverage: 11:477/485 of query aligns to 29:494/501 of 7rk5B
P09424 Mannitol-1-phosphate 5-dehydrogenase; EC 1.1.1.17 from Escherichia coli (strain K12) (see paper)
28% identity, 53% coverage: 154:409/485 of query aligns to 94:340/382 of P09424
Q4X1A4 Mannitol-1-phosphate 5-dehydrogenase; M1PDH; MPD; MPDH; EC 1.1.1.17 from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
24% identity, 40% coverage: 215:410/485 of query aligns to 154:340/388 of Q4X1A4
>AO356_28535 FitnessBrowser__pseudo5_N2C3_1:AO356_28535
MPVVKRVPCTGTAAQIGIVHLGLGAFHRAHQAVYLQRHLNRHGESDWGVCSANLRSNRTL
VEQLREQDGRYHVAEYRDCEQVTLREIGVLRQALYVGEGGPDLEQLLMRMAAPQTRIVTL
TVTEKGYCLSPSSGQLRSEDPAIAHDLAHPQAPRSAPGIVLEALRRRRAAGVPAFTVLCC
DNMPDNGQRTRQAVSALAALQDEALAQWVEQQVAFPSCMVDRIVPAMDGESFRRLEQLDC
HDPAAVVCESFSQWVIEDHFPLGRPDWEVEGVQMVDDVGPFETMKLRMLNGSHSLLAYVG
LLVGHDTVFEAVSDANLLHLIGRYMADEAAPTLDMPAGIDLSVYAHDLKARFANDSLQHR
LRQIAMDGSQKLPQRWLLGAQQLLDQGRGIDCTALGIAAWIHYCTQPLPGRPAHVVDDPL
SATFADLAGRFEGASRVDAVLDLHEVFPPRLSARAVFRDAVHHAYSALTRDGVDSLLHTL
AASKR
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory