SitesBLAST
Comparing 17442 FitnessBrowser__Keio:17442 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 20 (the maximum) hits to proteins with known functional sites (download)
P45548 Phosphotriesterase homology protein; EC 3.1.-.- from Escherichia coli (strain K12) (see 2 papers)
100% identity, 100% coverage: 1:292/292 of query aligns to 1:292/292 of P45548
- H12 (= H12) binding
- H14 (= H14) binding
- E125 (= E125) binding ; binding
- HN 148:149 (= HN 148:149) binding
- H158 (= H158) binding
- G176 (= G176) binding
- D178 (= D178) binding
- R181 (= R181) binding
- H186 (= H186) binding
- D243 (= D243) binding
- D280 (= D280) binding
- R284 (= R284) binding
1bf6A Phosphotriesterase homology protein from escherichia coli (see paper)
100% identity, 100% coverage: 2:292/292 of query aligns to 1:291/291 of 1bf6A
- active site: H11 (= H12), H13 (= H14), E124 (= E125), H157 (= H158), H185 (= H186), L188 (= L189), T209 (= T210), D242 (= D243)
- binding zinc ion: H11 (= H12), H13 (= H14), E124 (= E125), E124 (= E125), H157 (= H158), H185 (= H186), D242 (= D243)
4lefB Crystal structure of phosphotriesterase homology protein from escherichia coli complexed with phosphate in active site
100% identity, 99% coverage: 3:292/292 of query aligns to 1:290/290 of 4lefB
- active site: H10 (= H12), H12 (= H14), E123 (= E125), H156 (= H158), H184 (= H186), L187 (= L189), T208 (= T210), D241 (= D243)
- binding beta-D-glucopyranose: H146 (= H148), N147 (= N149), D176 (= D178), R179 (= R181)
- binding zinc ion: H10 (= H12), H12 (= H14), E123 (= E125), E123 (= E125), H156 (= H158), H184 (= H186), D241 (= D243)
4g2dA Crystal structure of the hyperthermophilic sulfolobus islandicus pll sislac (see paper)
32% identity, 98% coverage: 7:292/292 of query aligns to 17:314/314 of 4g2dA
- active site: H22 (= H12), H24 (= H14), K137 (≠ E125), H170 (= H158), H199 (= H186), D202 (≠ L189), R223 (≠ T210), D256 (= D243)
- binding cobalt (ii) ion: H22 (= H12), K137 (≠ E125), H170 (= H158), H199 (= H186)
- binding fe (ii) ion: H22 (= H12), H24 (= H14), K137 (≠ E125), D256 (= D243)
3uf9A Crystal structure of ssopox in complex with the phosphotriester fensulfothion (see paper)
31% identity, 98% coverage: 7:292/292 of query aligns to 17:314/314 of 3uf9A
- active site: H22 (= H12), H24 (= H14), K137 (≠ E125), H170 (= H158), H199 (= H186), D202 (≠ L189), R223 (≠ T210), D256 (= D243)
- binding cobalt (ii) ion: K137 (≠ E125), H170 (= H158), H199 (= H186)
- binding fe (ii) ion: H22 (= H12), H24 (= H14), K137 (≠ E125), D256 (= D243)
- binding O,O-diethyl O-{4-[(R)-methylsulfinyl]phenyl} phosphorothioate: H24 (= H14), D256 (= D243), C258 (vs. gap), I261 (vs. gap), W263 (vs. gap), T265 (= T245), A266 (≠ R246)
2vc7A Structural basis for natural lactonase and promiscuous phosphotriesterase activities (see paper)
31% identity, 98% coverage: 7:292/292 of query aligns to 17:314/314 of 2vc7A
- active site: H22 (= H12), H24 (= H14), K137 (≠ E125), H170 (= H158), H199 (= H186), D202 (≠ L189), R223 (≠ T210), D256 (= D243)
- binding cobalt (ii) ion: K137 (≠ E125), H170 (= H158), H199 (= H186)
- binding fe (ii) ion: H22 (= H12), H24 (= H14), K137 (≠ E125), D256 (= D243)
- binding (4S)-4-(decanoylamino)-5-hydroxy-3,4-dihydro-2H-thiophenium: H24 (= H14), Y97 (= Y84), H170 (= H158), R223 (≠ T210), L226 (≠ K213), F229 (≠ Y216), C258 (vs. gap), I261 (vs. gap), W263 (vs. gap)
Q97VT7 Aryldialkylphosphatase; Paraoxonase; SsoPox; Phosphotriesterase-like lactonase; EC 3.1.8.1 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
31% identity, 98% coverage: 7:292/292 of query aligns to 17:314/314 of Q97VT7
- H22 (= H12) binding
- H24 (= H14) binding
- K137 (≠ E125) binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
- H170 (= H158) binding
- H199 (= H186) binding
- D256 (= D243) binding
5w3uD Crystal structure of ssopox asb5 mutant (v27a-i76t-y97w-y99f-l130p- l226v) (see paper)
31% identity, 98% coverage: 7:292/292 of query aligns to 17:294/294 of 5w3uD
- active site: H22 (= H12), H24 (= H14), K137 (≠ E125), H170 (= H158), H199 (= H186), D202 (≠ L189), R223 (≠ T210), D256 (= D243)
- binding cobalt (ii) ion: W97 (≠ Y84), K137 (≠ E125), H170 (= H158), H199 (= H186)
- binding fe (ii) ion: H22 (= H12), H24 (= H14), K137 (≠ E125), H199 (= H186), D256 (= D243)
5w3zD Crystal structure of ssopox asc6 mutant (l72i-y99f-i122l-l228m-f229s- w263l) (see paper)
31% identity, 98% coverage: 7:292/292 of query aligns to 17:314/314 of 5w3zD
- active site: H22 (= H12), H24 (= H14), K137 (≠ E125), H170 (= H158), H199 (= H186), D202 (≠ L189), R223 (≠ T210), D256 (= D243)
- binding cobalt (ii) ion: K137 (≠ E125), H170 (= H158), H199 (= H186)
- binding fe (ii) ion: H22 (= H12), H24 (= H14), K137 (≠ E125), D256 (= D243)
3k2gB Crystal structure of a resiniferatoxin-binding protein from rhodobacter sphaeroides
31% identity, 92% coverage: 22:291/292 of query aligns to 73:351/358 of 3k2gB
Sites not aligning to the query:
4h9tA Structure of geobacillus kaustophilus lactonase, mutant e101n with bound n-butyryl-dl-homoserine lactone (see paper)
31% identity, 98% coverage: 7:291/292 of query aligns to 16:318/319 of 4h9tA
- active site: H21 (= H12), H23 (= H14), K139 (≠ E125), H172 (= H158), H200 (= H186), G203 (≠ L189), R224 (≠ T210), N260 (≠ D243)
- binding fe (iii) ion: H21 (= H12), H23 (= H14), K139 (≠ E125), N260 (≠ D243)
- binding N-[(3S)-2-oxotetrahydrofuran-3-yl]butanamide: Y28 (≠ L19), V262 (≠ T245), W265 (vs. gap), L272 (vs. gap), W283 (≠ Y256)
- binding manganese (ii) ion: K139 (≠ E125), H172 (= H158), H200 (= H186)
3ojgA Structure of an inactive lactonase from geobacillus kaustophilus with bound n-butyryl-dl-homoserine lactone (see paper)
31% identity, 98% coverage: 7:291/292 of query aligns to 16:322/323 of 3ojgA
- active site: H21 (= H12), H23 (= H14), K143 (≠ E125), H176 (= H158), H204 (= H186), G207 (≠ L189), R228 (≠ T210), N264 (≠ D243)
- binding fe (iii) ion: Y97 (= Y84), K143 (≠ E125), H176 (= H158), H204 (= H186)
- binding N-[(3S)-2-oxotetrahydrofuran-3-yl]butanamide: F26 (≠ I17), Y28 (≠ L19), R228 (≠ T210), M234 (≠ Y216), N264 (≠ D243), V266 (≠ T245), W269 (vs. gap)
- binding zinc ion: H21 (= H12), H23 (= H14), K143 (≠ E125), N264 (≠ D243)
6jstA Structure of geobacillus kaustophilus lactonase, y99p/d266n double mutant with bound 3-oxo-c8-hsl (see paper)
31% identity, 98% coverage: 7:291/292 of query aligns to 16:322/323 of 6jstA
- active site: H21 (= H12), H23 (= H14), K143 (≠ E125), H176 (= H158), H204 (= H186), G207 (≠ L189), R228 (≠ T210), N264 (≠ D243)
- binding fe (iii) ion: H21 (= H12), H23 (= H14), K143 (≠ E125), N264 (≠ D243)
- binding 3-oxo-octanoic acid (2-oxo-tetrahydro-furan-3-yl)-amide: Y28 (≠ L19), N264 (≠ D243), V266 (≠ T245), F274 (vs. gap), L276 (vs. gap), W287 (≠ Y256)
- binding zinc ion: K143 (≠ E125), H176 (= H158), H204 (= H186)
5ch9A Gkap mutant b12
31% identity, 98% coverage: 7:291/292 of query aligns to 16:326/328 of 5ch9A
- active site: H21 (= H12), H23 (= H14), K143 (≠ E125), H176 (= H158), H204 (= H186), G207 (≠ L189), R228 (≠ T210), D268 (= D243)
- binding cobalt (ii) ion: H21 (= H12), H23 (= H14), K143 (≠ E125), K143 (≠ E125), H176 (= H158), H204 (= H186), D268 (= D243)
3pnzA Crystal structure of the lactonase lmo2620 from listeria monocytogenes
28% identity, 98% coverage: 7:291/292 of query aligns to 16:325/329 of 3pnzA
4if2A Structure of the phosphotriesterase from mycobacterium tuberculosis (see paper)
31% identity, 98% coverage: 7:292/292 of query aligns to 16:319/324 of 4if2A
- active site: H21 (= H12), H23 (= H14), K144 (≠ E125), H177 (= H158), H206 (= H186), D209 (≠ L189), R230 (≠ T210), D263 (= D243)
- binding zinc ion: H21 (= H12), H23 (= H14), K144 (≠ E125), K144 (≠ E125), H177 (= H158), H206 (= H186), D263 (= D243)
P9WHN9 Phosphotriesterase homology protein from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
31% identity, 98% coverage: 7:292/292 of query aligns to 17:320/326 of P9WHN9
- H22 (= H12) binding
- H24 (= H14) binding
- K145 (≠ E125) binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
- H178 (= H158) binding
- H207 (= H186) binding
- D264 (= D243) binding
7p85A Engineered phosphotriesterase bdpte 10-2-c3(c59v/c227v) in complex with ethyl-4-methylbenzylphosphonate (see paper)
29% identity, 100% coverage: 1:292/292 of query aligns to 15:330/335 of 7p85A
- binding ethyl-4-methylbenzylphosphonate: H28 (= H14), I77 (≠ M59), W102 (≠ Y84), H172 (= H158), H201 (= H186), I231 (vs. gap), D272 (= D243), F277 (≠ R247)
- binding zinc ion: H26 (= H12), H28 (= H14), H172 (= H158), H201 (= H186), D272 (= D243)
3gtxA D71g/e101g mutant in organophosphorus hydrolase from deinococcus radiodurans (see paper)
29% identity, 98% coverage: 7:291/292 of query aligns to 26:332/333 of 3gtxA
- active site: H31 (= H12), H33 (= H14), K153 (≠ E125), H186 (= H158), H214 (= H186), G217 (≠ L189), R238 (≠ T210), D274 (= D243)
- binding cobalt (ii) ion: H31 (= H12), H33 (= H14), Y107 (= Y84), K153 (≠ E125), K153 (≠ E125), H186 (= H158), H214 (= H186), D274 (= D243)
3htwA Organophosphorus hydrolase from deinococcus radiodurans with cacodylate bound (see paper)
29% identity, 98% coverage: 7:291/292 of query aligns to 15:321/322 of 3htwA
- active site: H20 (= H12), H22 (= H14), K142 (≠ E125), H175 (= H158), H203 (= H186), G206 (≠ L189), R227 (≠ T210), D263 (= D243)
- binding cobalt (ii) ion: H20 (= H12), H22 (= H14), K142 (≠ E125), K142 (≠ E125), H175 (= H158), H203 (= H186), D263 (= D243)
- binding magnesium ion: R301 (≠ Q271), R302 (≠ S272)
Query Sequence
>17442 FitnessBrowser__Keio:17442
MSFDPTGYTLAHEHLHIDLSGFKNNVDCRLDQYAFICQEMNDLMTRGVRNVIEMTNRYMG
RNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGIDGTELKA
GIIAEIGTSEGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQLALLQAHGVDLS
RVTVGHCDLKDNLDNILKMIDLGAYVQFDTIGKNSYYPDEKRIAMLHALRDRGLLNRVML
SMDITRRSHLKANGGYGYDYLLTTFIPQLRQSGFSQADVDVMLRENPSQFFQ
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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