SitesBLAST

P0A9J8 Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 from Escherichia coli (strain K12)
32% identity, 96% coverage: 1:92/96 of query aligns to 1:90/386 of P0A9J8

query
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P0A9J8

M

M

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R11 (= R13) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
R28 (= R30) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
K39 (= K41) mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
E52 (= E54) mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
Q88 (≠ H90) mutation Q->A,E,K: Important decrease in catalytic efficiency and affinity.

1ecmB Atomic structure of the buried catalytic pocket of escherichia coli chorismate mutase
30% identity, 82% coverage: 9:87/96 of query aligns to 2:80/95 of 1ecmB

query
sites
1ecmB

L

L

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A

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binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: R23 (= R30), V30 (≠ I37), K34 (= K41), R42 (≠ S49), D43 (= D50), R46 (= R53), E47 (= E54), I76 (= I83), S79 (≠ V86)

Sites not aligning to the query:

binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: 83

Query Sequence

>WP_012755776.1 NCBI__GCF_000023185.1:WP_012755776.1
MTSTFPHELLALRASIDNIDAALMHMLAERFRCTKAIGALKARQGLPASDPEREQSQIQR
LRSLASTSGLDPDFAEKFLTFTIDEVIRHHRAAAAR

Or try a new SitesBLAST search

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