SitesBLAST
Comparing WP_057506742.1 NCBI__GCF_001431535.1:WP_057506742.1 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)
P00547 Homoserine kinase; HK; HSK; EC 2.7.1.39 from Escherichia coli (strain K12) (see paper)
36% identity, 90% coverage: 2:275/304 of query aligns to 1:280/310 of P00547
- H139 (= H137) mutation to L: 35-fold decrease in kinase activity.
- H203 (≠ Q198) mutation to L: 2-fold decrease in kinase activity but nearly no change in substrates affinity.
- H206 (≠ N201) mutation to Q: 3500-fold decrease in kinase activity.
- R235 (= R230) mutation to H: 250-fold decrease in kinase activity but no change in substrates affinity.; mutation to L: 26200-fold decrease in catalytic efficiency.
Q8L7R2 Homoserine kinase; Protein DOWNY MILDEW RESISTANT 1; EC 2.7.1.39 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 93% coverage: 4:286/304 of query aligns to 55:346/370 of Q8L7R2
- G118 (= G64) mutation to R: In dmr1-6; loss of function.
- G180 (≠ A125) mutation to D: In dmr1-5; loss of function.
- G202 (= G148) mutation to R: In dmr1-4; loss of function.
- M241 (≠ A182) mutation to K: In dmr1-3; loss of function.
- A267 (≠ G208) mutation to V: In dmr1-1; loss of function.
Sites not aligning to the query:
- 46 E→K: In dmr1-2; loss of function.
1h74B Crystal structure of homoserine kinase complexed with ile (see paper)
30% identity, 88% coverage: 1:268/304 of query aligns to 1:268/296 of 1h74B
- active site: E126 (= E129), T179 (= T179)
- binding phosphothiophosphoric acid-adenylate ester: N58 (= N61), V59 (≠ T62), K83 (= K86), A87 (≠ L90), G88 (= G91), G90 (= G93), G92 (= G95), S93 (≠ G96), S94 (= S97), S97 (= S100), S129 (≠ A132)
- binding isoleucine: A12 (≠ G12), N13 (= N13), D19 (= D19), H134 (= H137), D136 (= D139), N137 (= N140), R183 (= R183), R231 (= R230), G256 (= G256)
1h74A Crystal structure of homoserine kinase complexed with ile (see paper)
30% identity, 88% coverage: 1:268/304 of query aligns to 1:268/296 of 1h74A
- active site: E126 (= E129), T179 (= T179)
- binding adenosine-5'-diphosphate: I51 (≠ L54), N58 (= N61), V59 (≠ T62), K83 (= K86), A87 (≠ L90), G88 (= G91), S93 (≠ G96), S94 (= S97), S97 (= S100), T179 (= T179)
- binding isoleucine: N13 (= N13), F18 (= F18), D19 (= D19), H134 (= H137), T179 (= T179), R183 (= R183), R231 (= R230)
1h73A Crystal structure of homoserine kinase complexed with threonine (see paper)
30% identity, 88% coverage: 1:268/304 of query aligns to 1:268/296 of 1h73A
- active site: E126 (= E129), T179 (= T179)
- binding phosphoaminophosphonic acid-adenylate ester: I51 (≠ L54), N58 (= N61), V59 (≠ T62), K83 (= K86), A87 (≠ L90), G88 (= G91), G90 (= G93), L91 (≠ M94), G92 (= G95), S93 (≠ G96), S94 (= S97), S97 (= S100)
- binding threonine: N13 (= N13), D19 (= D19), R183 (= R183), R231 (= R230)
1h72C Crystal structure of homoserine kinase complexed with hse (see paper)
30% identity, 88% coverage: 1:268/304 of query aligns to 1:268/296 of 1h72C
- active site: E126 (= E129), T179 (= T179)
- binding phosphoaminophosphonic acid-adenylate ester: I51 (≠ L54), N58 (= N61), V59 (≠ T62), K83 (= K86), A87 (≠ L90), G88 (= G91), G90 (= G93), L91 (≠ M94), G92 (= G95), S93 (≠ G96), S94 (= S97), S97 (= S100), S129 (≠ A132), T179 (= T179), S257 (≠ A257)
- binding l-homoserine: N13 (= N13), F18 (= F18), D19 (= D19), D136 (= D139), N137 (= N140), R183 (= R183), R231 (= R230)
1fwkA Crystal structure of homoserine kinase complexed with adp (see paper)
30% identity, 88% coverage: 1:268/304 of query aligns to 1:268/296 of 1fwkA
Query Sequence
>WP_057506742.1 NCBI__GCF_001431535.1:WP_057506742.1
MIARAFAPASVGNVGVGFDILGHAIAGVGDTVTVRRIAEREVRIEAIRGADVPLPREAAL
NTAGASLLALRQALDLPFGFAVEIDKGIPLGSGMGGSAASCVAALVAANALLDSALDRHA
LYRFALEGELVASGGRHGDNLGPMLLGGLVLSTADRLVPIPVPARWHSLLVHPDAVLETR
RARAALQGSYALGDFVAQSANLALVLAGCHQGDATLVRAGLRDVLVEPRRAPLIIGFDAA
RAAALAAGAMGASISGAGPSVFAWFEDQASAQAAAAPVQAAFAASGFDSQAWVSSLAAPA
AVLL
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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