Comparing WP_011952724.1 NCBI__GCF_000016765.1:WP_011952724.1 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
40% identity, 89% coverage: 25:455/485 of query aligns to 12:450/483 of 4im7A
7rk5B Mannitol-2-dehydrogenase bound to nadh from aspergillus fumigatus
40% identity, 83% coverage: 25:425/485 of query aligns to 26:444/501 of 7rk5B
1m2wA Pseudomonas fluorescens mannitol 2-dehydrogenase ternary complex with NAD and d-mannitol (see paper)
40% identity, 75% coverage: 25:389/485 of query aligns to 20:397/492 of 1m2wA
1lj8A Crystal structure of mannitol dehydrogenase in complex with NAD (see paper)
40% identity, 75% coverage: 25:389/485 of query aligns to 20:397/492 of 1lj8A
P09424 Mannitol-1-phosphate 5-dehydrogenase; EC 1.1.1.17 from Escherichia coli (strain K12) (see paper)
28% identity, 52% coverage: 175:424/485 of query aligns to 105:345/382 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, 60% coverage: 113:405/485 of query aligns to 36:335/388 of Q4X1A4
>WP_011952724.1 NCBI__GCF_000016765.1:WP_011952724.1
MSAGPGARPRLSAATVPEGVAPLRYARDRARSGIVHLGLGAFHRAHQAVYTDDAMAAGDA
GWGIVGVSLRSPAVRDALVPQDCLYIVEERGAPGGRHLVGSINDALVAPEAPERVIAALA
DPAVHVATLTVTEKGYHRDPRTNGLLVDAPDVAHDLAGGGDPRTVFGFLAAALDRRAAQG
AGPLTILSCDNLPDNGRLLGGLLDDYLAARRGARPGGWTSPSSMVDRIVPAITADDLARL
PVEDRALTVCEPFRQWVIEDRFAGPRPRWEAGGAQIVDDVRPFELAKLRLLNGAHSALAY
WGLPLGHAHVHEAVCDPDLLAFVRRQLLAEAAPSLPPSAALDPAAYVETILRRFDNPALP
HRLAQIAMDGSQKLPQRWLATIVERAATGLASPAHLRSVAAWLAFVGDASGGGRPADDPL
ASRLETIWDGQATPADIAAAIVRSSGVFPAAFGADEALVGALGAALAERLSKGPRAMLRD
FLGRS
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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