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)
29% identity, 82% coverage: 11:90/98 of query aligns to 10:89/386 of P0A9J8

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P0A9J8

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R11 (= R12) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
R28 (= R29) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
K39 (= K40) mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
E52 (= E53) mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
Q88 (= Q89) 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
29% identity, 77% coverage: 11:85/98 of query aligns to 5:79/95 of 1ecmB

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1ecmB

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binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: R23 (= R29), V30 (≠ I36), K34 (= K40), R42 (≠ N48), D43 (= D49), R46 (= R52), E47 (= E53), I76 (≠ M82), S79 (= S85)

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_011973623.1 NCBI__GCF_000017185.1:WP_011973623.1
MTNPKDRLNIIRNRINEIDEQLIKLMAERTQFAGEIANLKSELNMPINDEEREHHIKETI
KSLCNKYDFDSNLSLEILTLLMEHSKELQKKACEKKNI

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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