Comparing BPHYT_RS28510 FitnessBrowser__BFirm:BPHYT_RS28510 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
44% identity, 97% coverage: 16:492/492 of query aligns to 4:482/483 of 4im7A
1m2wA Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and d-mannitol (see paper)
40% identity, 99% coverage: 1:487/492 of query aligns to 1:485/492 of 1m2wA
1lj8A Crystal structure of mannitol dehydrogenase in complex with NAD (see paper)
40% identity, 99% coverage: 1:487/492 of query aligns to 1:485/492 of 1lj8A
7rk5B Mannitol-2-dehydrogenase bound to nadh from aspergillus fumigatus
38% identity, 100% coverage: 1:490/492 of query aligns to 3:497/501 of 7rk5B
P09424 Mannitol-1-phosphate 5-dehydrogenase; EC 1.1.1.17 from Escherichia coli (strain K12) (see paper)
24% identity, 51% coverage: 161:410/492 of query aligns to 96:334/382 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)
22% identity, 54% coverage: 148:412/492 of query aligns to 74:327/388 of Q4X1A4
>BPHYT_RS28510 FitnessBrowser__BFirm:BPHYT_RS28510
MRLSNAALASLAARAAGKVVVPAYDRASLAPGIVHLGLGAFHRAHQALYTEHALRAGDHR
WGIVGVSLRRADTSEALTAQDHLYAVDVRDGTADSLQVIGALIASLVAPQSPAAVLDAMT
DPRCHIVSLTITEKGYCRNPASGALQFDHPDIAHDLRAAAAPRSAIGFVVRALALRRAAG
LGPFTVLSCDNLPSNGDTMRALTLAFARETDPALADWIELEAAFPNTMVDRIVPLTTDAD
RLRVAKQLGADDAWPVITEPFSQWVIEDRFAGPRPAWERAGATLVGDARPYEQAKLRMLN
GAHSALAYLGSLIGYDTVDQAIGAPAVLNFVESMLRDEVEPTLSRPALATYRAELFARFR
NTALDHRLQQIATDGSQKLPQRWLESVRANLKSGAPTERLAFALAGWIAYLGGHDETGRT
YAIADPLADRLTEAVRATLHADAADAVRTLFEIEPIFGRDLCAHPRFVAQVARHLAAIRA
QGVVKAMDAFAV
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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