Comparing WP_094505081.1 NCBI__GCF_002252445.1:WP_094505081.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 hits to proteins with known functional sites (download)
Q8R2K1 Fucose mutarotase; EC 5.1.3.29 from Mus musculus (Mouse) (see paper)
44% identity, 98% coverage: 2:138/140 of query aligns to 4:148/153 of Q8R2K1
2wcuA Crystal structure of mammalian fucu (see paper)
44% identity, 98% coverage: 2:138/140 of query aligns to 4:148/149 of 2wcuA
2wcvB Crystal structure of bacterial fucu (see paper)
41% identity, 98% coverage: 1:137/140 of query aligns to 1:138/140 of 2wcvB
P0AEN8 L-fucose mutarotase; D-ribose pyranase; Fucose 1-epimerase; Type-2 mutarotase; EC 5.1.3.29; EC 5.4.99.62 from Escherichia coli (strain K12) (see paper)
41% identity, 98% coverage: 1:137/140 of query aligns to 1:138/140 of P0AEN8
4a34I Crystal structure of the fucose mutarotase in complex with l-fucose from streptococcus pneumoniae (see paper)
36% identity, 98% coverage: 2:138/140 of query aligns to 1:139/142 of 4a34I
P04982 D-ribose pyranase; EC 5.4.99.62 from Escherichia coli (strain K12) (see paper)
26% identity, 93% coverage: 8:137/140 of query aligns to 6:137/139 of P04982
1ogeA The structure of bacillus subtilis rbsd complexed with ribose 5- phosphate (see paper)
30% identity, 94% coverage: 8:138/140 of query aligns to 6:130/131 of 1ogeA
1ogdA The structure of bacillus subtilis rbsd complexed with d-ribose (see paper)
30% identity, 94% coverage: 8:138/140 of query aligns to 6:130/131 of 1ogdA
P36946 D-ribose pyranase; EC 5.4.99.62 from Bacillus subtilis (strain 168) (see paper)
30% identity, 94% coverage: 8:138/140 of query aligns to 6:130/131 of P36946
>WP_094505081.1 NCBI__GCF_002252445.1:WP_094505081.1
MLKNINPLLSGSLLEVLADMGHGDDLVIVDANYPAQASGVQVLDFPGISATDIAEAVLSL
LPLDDFVDKPAAVMEAPKETPAIFGEFEAVIEKAEGRKIAVDPIERFAFYDRASAAYAVI
RSGEKRLYGNIIFKKGVIRS
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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