SitesBLAST

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)
47% identity, 94% coverage: 1:139/148 of query aligns to 1:138/140 of P0AEN8

query
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P0AEN8

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H22 (= H22) active site, Proton donor; mutation to A: Affects slightly binding affinity toward L-fucose. Significantly reduced ribose pyranase activity.
D30 (= D30) binding substrate
D64 (= D64) active site; mutation to A: Affects slightly binding affinity toward L-fucose. Significantly reduced ribose pyranase activity.
M73 (≠ R73) binding substrate
Y111 (= Y112) active site; binding substrate; mutation to F: Reduces binding affinity toward L-fucose. Significantly reduced ribose pyranase activity.
Y129 (= Y130) binding substrate
N131 (= N132) binding substrate

4a34I Crystal structure of the fucose mutarotase in complex with l-fucose from streptococcus pneumoniae (see paper)
44% identity, 94% coverage: 2:140/148 of query aligns to 1:139/142 of 4a34I

query
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4a34I

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binding beta-L-fucopyranose: H21 (= H22), D29 (= D30), Y32 (≠ F33), Y65 (≠ F66), Y129 (= Y130), V138 (= V139)

2wcuA Crystal structure of mammalian fucu (see paper)
43% identity, 94% coverage: 2:140/148 of query aligns to 4:148/149 of 2wcuA

query
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2wcuA

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binding alpha-L-fucopyranose: D32 (= D30), F35 (= F33), M79 (= M74), Y120 (= Y112), Y138 (= Y130), N140 (= N132)

Q8R2K1 Fucose mutarotase; EC 5.1.3.29 from Mus musculus (Mouse) (see paper)
43% identity, 94% coverage: 2:140/148 of query aligns to 4:148/153 of Q8R2K1

query
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Q8R2K1

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H24 (= H22) active site, Proton donor
D32 (= D30) binding substrate
D69 (= D64) active site
M79 (= M74) binding substrate
Y120 (= Y112) active site; binding substrate
Y138 (= Y130) binding substrate
N140 (= N132) binding substrate

Query Sequence

>WP_011650308.1 NCBI__GCF_000009265.1:WP_011650308.1
MLKGIHPLLGPDLLHALKTMGHGDDIVISDANFPSGSMGPPVIRADGVSATAMAEAILTH
MPLDTFVPEAAWRMEVVGDPDAMPEVCTEFQQIVSKHAGDFRIVPVERFAFYAMARKATY
IVATTEFRLYGNLILKKGVVHPHEVDQA

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SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory