SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_047216711.1 NCBI__GCF_001931675.1:WP_047216711.1 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)

O87170 2-pyrone-4,6-dicarboxylate hydrolase; PDC hydrolase; 2-pyrone-4,6-dicarboxylate lactonase; EC 3.1.1.57 from Sphingobium sp. (strain NBRC 103272 / SYK-6) (see paper)
45% identity, 97% coverage: 10:290/290 of query aligns to 13:293/293 of O87170

query
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O87170

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HCH 29:31 (= HCH 26:28) binding substrate
Y47 (= Y44) binding substrate
S75 (= S72) binding substrate
R122 (= R119) binding substrate
R128 (≠ H125) binding substrate
Y154 (≠ H152) binding substrate
H178 (= H176) binding substrate
D246 (= D243) mutation to A: Loss of catalytic activity.; mutation to N: Almost inactive.
N251 (= N248) binding substrate

4di8A Crystal structure of the d248a mutant of 2-pyrone-4,6-dicarboxylic acid hydrolase from sphingomonas paucimobilis complexed with substrate at ph 8.5 (see paper)
45% identity, 97% coverage: 10:290/290 of query aligns to 14:294/294 of 4di8A

query
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4di8A

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active site: A247 (≠ D243)
binding (1E,3Z)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylic acid: H30 (= H26), H32 (= H28), Y48 (= Y44), A75 (= A71), S76 (= S72), R123 (= R119), R129 (≠ H125), L130 (= L126), Y155 (≠ H152), H179 (= H176), R216 (= R212), N252 (= N248)
binding 2-oxo-2H-pyran-4,6-dicarboxylic acid: H30 (= H26), Y48 (= Y44), A75 (= A71), S76 (= S72), R123 (= R119), R129 (≠ H125), L130 (= L126), Y155 (≠ H152), R216 (= R212), N252 (= N248)

A9CEQ7 D-galactarolactone isomerase; GLI; Galactaro delta-lactone isomerase; EC 5.4.1.4 from Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) (see paper)
30% identity, 97% coverage: 9:290/290 of query aligns to 13:289/292 of A9CEQ7

query
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A9CEQ7

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N240 (≠ D243) mutation to D: 28-fold decrease in enzymatic activity. Does not gain the ability to hydrolyze D-galactaro-1,5-lactone or D-galactaro-1,4-lactone.

Query Sequence

>WP_047216711.1 NCBI__GCF_001931675.1:WP_047216711.1
MKSCLPPDPNPLKPAHALPAGACDAHCHVFGPGNVFPYAPDRSYTPPDAPYEGLVKLHDW
LGISRGVIVQASCHGTDNRAMLDAIERSQGRYRGVAIVDGDVTDEALAQMDAQGVRGVRF
NFVAHLGGAPDLDVFDRVLRRIEALGWHVVLHLDAQDIVTYAERIDRIRVPFVIDHMGRI
RAEAGTDQPSFQRLLGLMRNPLAWVKVCGSERVSVGRRPFDDAIPFARALIEAAPDRVLW
GTDWPHPNISKDMPNDGELVDLMFRFCDDAGLRERLLVTNPARLYGFEAI

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