Comparing Echvi_0123 FitnessBrowser__Cola:Echvi_0123 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
2qmxA The crystal structure of l-phe inhibited prephenate dehydratase from chlorobium tepidum tls (see paper)
37% identity, 95% coverage: 10:275/279 of query aligns to 4:273/278 of 2qmxA
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)
31% identity, 97% coverage: 5:275/279 of query aligns to 101:375/386 of P0A9J8
Sites not aligning to the query:
6vh5D Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine
29% identity, 97% coverage: 8:278/279 of query aligns to 7:279/282 of 6vh5D
7am0B Gqqa- a novel type of quorum quenching acylases (see paper)
26% identity, 98% coverage: 7:279/279 of query aligns to 1:273/278 of 7am0B
3mwbB The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
27% identity, 84% coverage: 14:246/279 of query aligns to 7:241/303 of 3mwbB
3mwbA The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
27% identity, 84% coverage: 14:246/279 of query aligns to 7:244/306 of 3mwbA
3luyA Putative chorismate mutase from bifidobacterium adolescentis
22% identity, 97% coverage: 8:279/279 of query aligns to 4:287/326 of 3luyA
>Echvi_0123 FitnessBrowser__Cola:Echvi_0123
MTSTPHQQKVAIQGIKGSYHYQVALNQFGQDIHVIECLTFSDLVKSITSNDADIGVLALE
NSIAGAILPNYDLMDRNNLQVIGEFYLPISHQLMVLKGQSIDDITEVRSHPMALLQCKAF
FEQYPQIKLIEDLDTASVAKEISEQHLQGVGAIAGKSAAEFYGLDILASDIQTIKNNITR
FCIVKNAADAKPVIGFDKASIKVTIKNEQGSLAKVLTTMSAYRLDLTKIQSLPVIDQPWH
YAFFIDLLFENLEDYQQALKELKANGHQIKVLGEYKNTK
Or try a new SitesBLAST search
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