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Comparing BWI76_RS14505 FitnessBrowser__Koxy:BWI76_RS14505 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
89% identity, 99% coverage: 2:434/436 of query aligns to 1:424/424 of 5jy9B
- active site: K183 (= K193), E230 (= E240), A246 (= A256), E274 (= E284), H311 (= H321), T338 (= T348), Y362 (= Y372), R381 (= R391), G397 (= G407), E410 (= E420), K414 (= K424)
- binding fe (ii) ion: E274 (= E284), E410 (= E420)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
85% identity, 99% coverage: 2:434/436 of query aligns to 1:408/408 of 2fn1A
- active site: K167 (= K193), E214 (= E240), A230 (= A256), E258 (= E284), H295 (= H321), T322 (= T348), Y346 (= Y372), R365 (= R391), G381 (= G407), E394 (= E420), K398 (= K424)
- binding magnesium ion: E258 (= E284), E394 (= E420)
- binding pyruvic acid: Y346 (= Y372), L364 (= L390), R365 (= R391), A378 (= A404), G379 (= G405), K398 (= K424)
2fn0A Crystal structure of yersinia enterocolitica salicylate synthase (irp9) (see paper)
85% identity, 99% coverage: 2:434/436 of query aligns to 1:408/408 of 2fn0A
- active site: K167 (= K193), E214 (= E240), A230 (= A256), E258 (= E284), H295 (= H321), T322 (= T348), Y346 (= Y372), R365 (= R391), G381 (= G407), E394 (= E420), K398 (= K424)
- binding acetate ion: Y346 (= Y372), L364 (= L390), R365 (= R391), A378 (= A404), G379 (= G405)
- binding magnesium ion: E258 (= E284), E394 (= E420)
- binding phosphate ion: A230 (= A256), G231 (= G257), T232 (= T258), E258 (= E284), G381 (= G407), E394 (= E420), K398 (= K424)
P9WFX1 Salicylate synthase; Chorismate mutase; CM; Isochorismate synthase/isochorismate lyase; Mycobactin synthase protein; EC 5.4.99.5; EC 4.2.99.21; EC 5.4.4.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
37% identity, 95% coverage: 20:432/436 of query aligns to 33:446/450 of P9WFX1
- K205 (= K193) mutation to A: Only the chorismate mutase activity is observed.
- E252 (= E240) mutation to Q: No activity is observed.
- L268 (= L255) Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl; mutation to A: Only the chorismate mutase activity is observed.
- GT 270:271 (= GT 257:258) binding
- T271 (= T258) mutation to A: Only the chorismate mutase activity is observed.
- E297 (= E284) binding
- H334 (= H321) mutation to M: Only the chorismate mutase activity is observed.
- Y385 (= Y372) binding
- R405 (= R391) binding ; mutation to A: Only the chorismate mutase activity is observed.
- GAG 419:421 (= GAG 405:407) binding
- E431 (= E417) binding
- E434 (= E420) binding
- K438 (= K424) binding
3logB Crystal structure of mbti from mycobacterium tuberculosis (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 34:447/450 of 3logB
- active site: K206 (= K193), E253 (= E240), A270 (= A256), E298 (= E284), H335 (= H321), T362 (= T348), Y386 (= Y372), R406 (= R391), G422 (= G407), E435 (= E420), K439 (= K424)
- binding carbonate ion: G271 (= G257), T272 (= T258), E298 (= E284), E435 (= E420)
2g5fA The structure of mbti from mycobacterium tuberculosis, the first enzyme in the synthesis of mycobactin, reveals it to be a salicylate synthase (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 19:432/435 of 2g5fA
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E283 (= E284), H320 (= H321), T347 (= T348), Y371 (= Y372), R391 (= R391), G407 (= G407), E420 (= E420), K424 (= K424)
- binding pyruvic acid: Y371 (= Y372), L390 (= L390), R391 (= R391), G405 (= G405), K424 (= K424)
6za5B M. Tuberculosis salicylate synthase mbti in complex with salicylate and mg2+ (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 24:437/440 of 6za5B
- active site: K196 (= K193), E243 (= E240), A260 (= A256), E288 (= E284), H325 (= H321), T352 (= T348), Y376 (= Y372), R396 (= R391), G412 (= G407), E425 (= E420), K429 (= K424)
- binding magnesium ion: E288 (= E284), E425 (= E420)
3vehB Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor methylamt (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 35:448/451 of 3vehB
- active site: K207 (= K193), E254 (= E240), A271 (= A256), E299 (= E284), H336 (= H321), T363 (= T348), Y387 (= Y372), R407 (= R391), G423 (= G407), E436 (= E420), K440 (= K424)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: L270 (= L255), T273 (= T258), H336 (= H321), T363 (= T348), Y387 (= Y372), L406 (= L390), A420 (= A404), G421 (= G405), K440 (= K424)
8qc4A Salicylate synthase (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 21:434/438 of 8qc4A
- binding 5-(3-carboxyphenyl)furan-2-carboxylic acid: K193 (= K193), I195 (= I195), A257 (= A256), H322 (= H321), T349 (= T348), Y373 (= Y372), L392 (= L390), R393 (= R391), A406 (= A404), G407 (= G405), K426 (= K424)
3st6A Structure of a m. Tuberculosis synthase, mbti, in complex with an isochorismate analogue inhibitor (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 19:432/436 of 3st6A
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E283 (= E284), H320 (= H321), T347 (= T348), Y371 (= Y372), R391 (= R391), G407 (= G407), E420 (= E420), K424 (= K424)
- binding 3-[(1-carboxyethenyl)oxy]-2-hydroxybenzoic acid: H320 (= H321), T347 (= T348), Y371 (= Y372), L390 (= L390), R391 (= R391), A404 (= A404), G405 (= G405), G407 (= G407), K424 (= K424)
3rv8C Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor with cyclopropyl r-group (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 19:427/430 of 3rv8C
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E278 (= E284), H315 (= H321), T342 (= T348), Y366 (= Y372), R386 (= R391), G402 (= G407), E415 (= E420), K419 (= K424)
- binding 3-{[(Z)-1-carboxy-2-cyclopropylethenyl]oxy}-2-hydroxybenzoic acid: L254 (= L255), H315 (= H321), T342 (= T348), L385 (= L390), R386 (= R391), K419 (= K424)
- binding 3-{[(E)-1-carboxy-2-cyclopropylethenyl]oxy}-2-hydroxybenzoic acid: H315 (= H321), T342 (= T348), Y366 (= Y372), L385 (= L390), R386 (= R391), A399 (= A404), K419 (= K424)
6za4A M. Tuberculosis salicylate synthase mbti in complex with 5-(3- cyanophenyl)furan-2-carboxylate (see paper)
37% identity, 95% coverage: 20:432/436 of query aligns to 19:426/429 of 6za4A
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E277 (= E284), H314 (= H321), T341 (= T348), Y365 (= Y372), R385 (= R391), G401 (= G407), E414 (= E420), K418 (= K424)
- binding 5-(3-cyanophenyl)furan-2-carboxylic acid: K191 (= K193), I193 (= I195), T341 (= T348), Y365 (= Y372), L384 (= L390), A398 (= A404), G399 (= G405), K418 (= K424)
3rv8A Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor with cyclopropyl r-group (see paper)
36% identity, 95% coverage: 20:432/436 of query aligns to 19:414/418 of 3rv8A
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E269 (= E284), H302 (= H321), T329 (= T348), Y353 (= Y372), R373 (= R391), G389 (= G407), E402 (= E420), K406 (= K424)
- binding 3-{[(Z)-1-carboxy-2-cyclopropylethenyl]oxy}-2-hydroxybenzoic acid: L254 (= L255), T329 (= T348), Y353 (= Y372), L372 (= L390), R373 (= R391), G387 (= G405), K406 (= K424)
3rv7A Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor with isopropyl r-group (see paper)
36% identity, 95% coverage: 20:432/436 of query aligns to 19:413/416 of 3rv7A
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E270 (= E284), H301 (= H321), T328 (= T348), Y352 (= Y372), R372 (= R391), G388 (= G407), E401 (= E420), K405 (= K424)
- binding 3-{[(1Z)-1-carboxy-3-methylbut-1-en-1-yl]oxy}-2-hydroxybenzoic acid: P237 (= P239), L254 (= L255), T257 (= T258), H301 (= H321), T328 (= T348), Y352 (= Y372), L371 (= L390), R372 (= R391), A385 (= A404), G386 (= G405), K405 (= K424)
3rv9A Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor with ethyl r-group (see paper)
36% identity, 95% coverage: 20:432/436 of query aligns to 19:416/420 of 3rv9A
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E272 (= E284), H304 (= H321), T331 (= T348), Y355 (= Y372), R375 (= R391), G391 (= G407), E404 (= E420), K408 (= K424)
- binding 3-{[(1Z)-1-carboxybut-1-en-1-yl]oxy}-2-hydroxybenzoic acid: T331 (= T348), Y355 (= Y372), L374 (= L390), R375 (= R391), A388 (= A404), G389 (= G405), K408 (= K424)
3rv6B Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor with phenyl r-group (see paper)
35% identity, 95% coverage: 20:432/436 of query aligns to 19:409/413 of 3rv6B
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E264 (= E284), H297 (= H321), T324 (= T348), Y348 (= Y372), R368 (= R391), G384 (= G407), E397 (= E420), K401 (= K424)
- binding 3-{[(Z)-1-carboxy-2-phenylethenyl]oxy}-2-hydroxybenzoic acid: H190 (≠ V192), K191 (= K193), E238 (= E240), V263 (≠ L283), I267 (≠ L287), S268 (= S288), T324 (= T348), Y348 (= Y372), L367 (= L390), R368 (= R391), A381 (= A404), G382 (= G405), K401 (= K424)
3rv6A Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor with phenyl r-group (see paper)
36% identity, 95% coverage: 20:432/436 of query aligns to 19:413/417 of 3rv6A
- active site: K191 (= K193), E238 (= E240), A255 (= A256), E271 (= E284), T328 (= T348), Y352 (= Y372), R372 (= R391), G388 (= G407), E401 (= E420), K405 (= K424)
- binding 3-{[(Z)-1-carboxy-2-phenylethenyl]oxy}-2-hydroxybenzoic acid: I141 (vs. gap), R142 (vs. gap), H190 (≠ V192), I274 (≠ L287), R277 (≠ K290), I332 (= I352)
- binding 3-{[(E)-1-carboxy-2-phenylethenyl]oxy}-2-hydroxybenzoic acid: L254 (= L255), G256 (= G257), E271 (= E284), Y352 (= Y372), L371 (= L390), A385 (= A404), G386 (= G405), K405 (= K424)
3rv9C Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor with ethyl r-group (see paper)
35% identity, 95% coverage: 20:432/436 of query aligns to 19:410/413 of 3rv9C
- active site: K191 (= K193), E238 (= E240), E266 (= E284), H298 (= H321), T325 (= T348), Y349 (= Y372), R369 (= R391), G385 (= G407), E398 (= E420), K402 (= K424)
- binding 3-{[(1Z)-1-carboxybut-1-en-1-yl]oxy}-2-hydroxybenzoic acid: E238 (= E240), T325 (= T348), Y349 (= Y372), L368 (= L390), R369 (= R391), A382 (= A404), G383 (= G405), K402 (= K424)
6za4B M. Tuberculosis salicylate synthase mbti in complex with 5-(3- cyanophenyl)furan-2-carboxylate (see paper)
35% identity, 95% coverage: 20:432/436 of query aligns to 35:420/423 of 6za4B
- active site: K207 (= K193), E254 (= E240), A271 (= A256), E278 (= E284), T335 (= T348), Y359 (= Y372), R379 (= R391), G395 (= G407), E408 (= E420), K412 (= K424)
- binding 5-(3-cyanophenyl)furan-2-carboxylic acid: K207 (= K193), I209 (= I195), T335 (= T348), Y359 (= Y372), L378 (= L390), R379 (= R391), A392 (= A404), G393 (= G405), K412 (= K424)
A0QX93 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
33% identity, 59% coverage: 173:428/436 of query aligns to 249:511/524 of A0QX93
- K355 (≠ R273) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>BWI76_RS14505 FitnessBrowser__Koxy:BWI76_RS14505
MKISEFLHLALPEEQWLPMISGVLRQFGDEECYVYERQPCWYIGKGCQAQLQINADGTQA
IFIDDAGEQKWAVDSITDCARRFMTHPRVRGCRVYGQVGFNFAAHARGMAFDAGEWPLLT
LTAPREELIFEKGNVTVYADSADGCRRLCEWVKEVDTATPCGPMVVDTALDGEAYKQQVA
RAVSAIHRGDYVKVIVSRAIPLPARIDMPATLLYGRQANTPTRSFMFRQQGREALGFSPE
LVMSVTGNKVVTEPLAGTRDRMGDTAHNQANERELLHDGKEVLEHILSVKEAIAELEAVC
QPGSVVVEDLMSVRQRGSVQHLGSGVSGQLAEDKDAWDAFTVLFPSITASGIPKKAALNA
IMQIEKTPRELYSGAILLLEDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTE
TREKLASIAPYLKVPA
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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