SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013537413.1 NCBI__GCF_000185805.1:WP_013537413.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 3 hits to proteins with known functional sites (download)

1nsjA Crystal structure of phosphoribosyl anthranilate isomerase from thermotoga maritima (see paper)
48% identity, 98% coverage: 1:206/210 of query aligns to 2:203/205 of 1nsjA

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1nsjA

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active site: C7 (= C6), D126 (= D126)
binding phosphate ion: G133 (= G134), V179 (= V182), S180 (≠ C183), S181 (= S184)

1lbmA Crystal structure of phosphoribosyl anthranilate isomerase (prai) in complex with reduced 1-(o-carboxyphenylamino)-1-deoxyribulose 5- phosphate (rcdrp) (see paper)
45% identity, 98% coverage: 1:206/210 of query aligns to 2:192/194 of 1lbmA

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1lbmA

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active site: C7 (= C6), D126 (= D126)
binding 1-(o-carboxy-phenylamino)-1-deoxy-d-ribulose-5-phosphate: C7 (= C6), S34 (= S33), R36 (= R35), H83 (= H82), D126 (= D126), G147 (= G161), G148 (= G162), D167 (= D181), S169 (≠ C183), S170 (= S184)

1piiA Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from escherichia coli refined at 2.0 angstroms resolution (see paper)
29% identity, 91% coverage: 4:194/210 of query aligns to 258:438/452 of 1piiA

query
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1piiA

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active site: C260 (= C6), D379 (= D126)
binding phosphate ion: G386 (= G137), G407 (= G162), N427 (≠ C183), S428 (= S184)

Sites not aligning to the query:

active site: 53, 55, 114, 163, 184, 214, 215
binding phosphate ion: 55, 215, 235, 236, 237

Query Sequence

>WP_013537413.1 NCBI__GCF_000185805.1:WP_013537413.1
MKVKVCGITNLTDALSAVGSGADAVGFIIYKGSKRYVSAKEVRSITAQLPPFVTKVGVFV
NEDPRSILEILSYAHLDFAQLHGDETPEDCDYVGPNRVIKVFRFRSKEEISAVEPYIGKV
RAILLDTYDTKVYGGTGKPFNWEIAVAVKERYPELPLILSGGLNPLNVVDAVETVNPYAV
DVCSGVELSPGRKDPGKVEEFIRRAKCSCK

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