SitesBLAST
Comparing 14729 FitnessBrowser__Keio:14729 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)
P0AEJ2 Isochorismate synthase EntC; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:391/391 of query aligns to 1:391/391 of P0AEJ2
- T140 (= T140) binding
- T142 (= T142) binding
- V145 (= V145) binding
- D146 (= D146) binding
- G214 (= G214) binding
- S215 (= S215) binding
- E241 (= E241) binding ; binding
- A303 (= A303) binding ; mutation to T: Loss of mutase activity.
- L304 (= L304) mutation to A: Loss of mutase activity.
- F327 (= F327) mutation to Y: Loss of mutase activity.
- I346 (= I346) mutation to L: Loss of mutase activity.
- R347 (= R347) binding
- F359 (= F359) mutation to Q: Loss of mutase activity.
- G361 (= G361) binding
- E376 (= E376) binding
- K380 (= K380) binding
3hwoA Crystal structure of escherichia coli enterobactin-specific isochorismate synthase entc in complex with isochorismate (see paper)
100% identity, 97% coverage: 13:391/391 of query aligns to 1:379/379 of 3hwoA
- active site: K135 (= K147), E185 (= E197), A201 (= A213), E229 (= E241), H264 (= H276), A291 (= A303), F315 (= F327), R335 (= R347), G351 (= G363), E364 (= E376), K368 (= K380)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: G202 (= G214), S203 (= S215), E229 (= E241), H264 (= H276), I334 (= I346), R335 (= R347), A348 (= A360), G349 (= G361), E364 (= E376), K368 (= K380)
- binding magnesium ion: T128 (= T140), T130 (= T142), V133 (= V145), D134 (= D146), E229 (= E241), E364 (= E376)
5jxzA A low magnesium structure of the isochorismate synthase, entc (see paper)
99% identity, 96% coverage: 15:390/391 of query aligns to 1:373/373 of 5jxzA
- active site: K130 (= K147), E180 (= E197), A196 (= A213), E224 (= E241), H259 (= H276), A286 (= A303), F310 (= F327), R330 (= R347), G346 (= G363), E359 (= E376), K363 (= K380)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: L195 (= L212), G197 (= G214), S198 (= S215), E224 (= E241), A286 (= A303), I329 (= I346), R330 (= R347), A343 (= A360), G344 (= G361), E359 (= E376), K363 (= K380)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E180 (= E197), L195 (= L212), A196 (= A213), G197 (= G214), E224 (= E241), A286 (= A303), I329 (= I346), R330 (= R347), G344 (= G361), A345 (= A362), E359 (= E376), K363 (= K380)
- binding magnesium ion: E224 (= E241), E359 (= E376)
5jy8A An iron-bound structure of the isochorismate synthase entc (see paper)
98% identity, 96% coverage: 16:390/391 of query aligns to 1:368/368 of 5jy8A
- active site: K125 (= K147), E175 (= E197), A191 (= A213), E219 (= E241), H254 (= H276), A281 (= A303), F305 (= F327), R325 (= R347), G341 (= G363), E354 (= E376), K358 (= K380)
- binding fe (iii) ion: E219 (= E241), E237 (= E259), H239 (= H261), E354 (= E376)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E175 (= E197), L190 (= L212), A191 (= A213), G192 (= G214), E219 (= E241), L282 (= L304), I324 (= I346), F337 (= F359), A338 (= A360), G339 (= G361), E354 (= E376), K358 (= K380)
P45744 Isochorismate synthase DhbC; Isochorismate mutase; EC 5.4.4.2 from Bacillus subtilis (strain 168) (see paper)
37% identity, 95% coverage: 18:390/391 of query aligns to 21:395/398 of P45744
- S271 (≠ Q267) modified: Phosphoserine
3bznA Crystal structure of open form of menaquinone-specific isochorismate synthase, menf (see paper)
32% identity, 70% coverage: 115:387/391 of query aligns to 158:430/430 of 3bznA
- active site: K190 (= K147), E240 (= E197), A256 (= A213), E284 (= E241), H318 (= H276), A344 (= A303), Y368 (≠ F327), R387 (= R347), G403 (= G363), E416 (= E376), K420 (= K380)
- binding magnesium ion: E284 (= E241), E416 (= E376)
P38051 Isochorismate synthase MenF; Isochorismate hydroxymutase; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see 2 papers)
32% identity, 70% coverage: 115:387/391 of query aligns to 158:430/431 of P38051
- K190 (= K147) active site, Proton acceptor; mutation to A: Lack of activity.
- E240 (= E197) active site, Proton donor; mutation to Q: Lack of activity.
- L255 (= L212) mutation to A: Decrease in activity.
- E284 (= E241) binding
- A344 (= A303) mutation to T: Lack of activity.
- R387 (= R347) mutation to A: Lack of activity.
- E416 (= E376) binding
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
32% identity, 55% coverage: 170:386/391 of query aligns to 271:488/499 of 7bvdA
Sites not aligning to the query:
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)
32% identity, 55% coverage: 170:386/391 of query aligns to 292:513/524 of A0QX93
- K355 (≠ N230) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
30% identity, 76% coverage: 90:386/391 of query aligns to 207:492/505 of 5cwaA
- active site: Q248 (≠ K147), E301 (= E197), A317 (= A213), E345 (= E241), H382 (= H276), T409 (≠ A303), Y433 (≠ F327), R453 (= R347), G469 (= G363), E482 (= E376), K486 (= K380)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (≠ F327), I452 (= I346), A466 (= A360), G467 (= G361), K486 (= K380)
P28820 Aminodeoxychorismate synthase component 1; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 1; EC 2.6.1.85 from Bacillus subtilis (strain 168) (see paper)
26% identity, 65% coverage: 129:384/391 of query aligns to 202:456/470 of P28820
- A283 (= A213) mutation to I: Complete loss of aminodeoxychorismate synthase activity.; mutation to K: Absence of covalent intermediate.; mutation to V: Complete loss of aminodeoxychorismate synthase activity.
7pi1DDD Aminodeoxychorismate synthase component 1
26% identity, 65% coverage: 129:384/391 of query aligns to 195:449/459 of 7pi1DDD
Sites not aligning to the query:
O94582 Probable anthranilate synthase component 1; Anthranilate synthase component I; EC 4.1.3.27 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 55% coverage: 167:383/391 of query aligns to 251:469/489 of O94582
- S390 (= S305) modified: Phosphoserine
- S392 (≠ F307) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
P05041 Aminodeoxychorismate synthase component 1; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 1; EC 2.6.1.85 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 51% coverage: 189:386/391 of query aligns to 250:449/453 of P05041
- E258 (= E197) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A213) mutation to A: Absence of covalent intermediate. Addition of ammonia allows the formation of the covalent intermediate and shows that ammonia can replace the function of K-274. Reduced catalytic efficiency.; mutation to R: Absence of covalent intermediate.; mutation to R: Reduced catalytic efficiency.
- G275 (= G214) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (≠ K250) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ E255) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ E259) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H276) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
Sites not aligning to the query:
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
28% identity, 65% coverage: 129:384/391 of query aligns to 149:402/408 of 2fn1A
- active site: K167 (= K147), E214 (= E197), A230 (= A213), E258 (= E241), H295 (= H276), T322 (≠ A303), Y346 (≠ F327), R365 (= R347), G381 (= G363), E394 (= E376), K398 (= K380)
- binding magnesium ion: E258 (= E241), E394 (= E376)
- binding pyruvic acid: Y346 (≠ F327), L364 (≠ I346), R365 (= R347), A378 (= A360), G379 (= G361), K398 (= K380)
2fn0A Crystal structure of yersinia enterocolitica salicylate synthase (irp9) (see paper)
28% identity, 65% coverage: 129:384/391 of query aligns to 149:402/408 of 2fn0A
- active site: K167 (= K147), E214 (= E197), A230 (= A213), E258 (= E241), H295 (= H276), T322 (≠ A303), Y346 (≠ F327), R365 (= R347), G381 (= G363), E394 (= E376), K398 (= K380)
- binding acetate ion: Y346 (≠ F327), L364 (≠ I346), R365 (= R347), A378 (= A360), G379 (= G361)
- binding magnesium ion: E258 (= E241), E394 (= E376)
- binding phosphate ion: A230 (= A213), G231 (= G214), T232 (≠ S215), E258 (= E241), G381 (= G363), E394 (= E376), K398 (= K380)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
28% identity, 65% coverage: 129:384/391 of query aligns to 165:418/424 of 5jy9B
- active site: K183 (= K147), E230 (= E197), A246 (= A213), E274 (= E241), H311 (= H276), T338 (≠ A303), Y362 (≠ F327), R381 (= R347), G397 (= G363), E410 (= E376), K414 (= K380)
- binding fe (ii) ion: E274 (= E241), E410 (= E376)
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
29% identity, 55% coverage: 171:385/391 of query aligns to 280:503/512 of 1i1qA
- active site: E305 (= E197), A323 (= A213), E357 (≠ V245), H394 (= H276), T421 (= T301), Y445 (≠ F327), R465 (= R347), G481 (= G363), E494 (= E376), K498 (= K380)
- binding tryptophan: P287 (≠ S178), Y288 (= Y179), M289 (≠ N180), G450 (= G332), C461 (≠ V343)
Sites not aligning to the query:
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
29% identity, 55% coverage: 171:385/391 of query aligns to 284:507/520 of P00898
- N288 (= N175) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P176) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ N180) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F181) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G193) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ P280) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G338) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ V343) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
Sites not aligning to the query:
- 39 E→K: Complete loss of feedback control by tryptophan.
- 40 binding ; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding
- 128 R→H: Almost no change in feedback control by tryptophan.
- 174 C→Y: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
8qc4A Salicylate synthase (see paper)
28% identity, 71% coverage: 107:384/391 of query aligns to 158:430/438 of 8qc4A
- binding 5-(3-carboxyphenyl)furan-2-carboxylic acid: K193 (= K147), I195 (≠ V149), A257 (= A213), H322 (= H276), T349 (≠ A303), Y373 (≠ F327), L392 (≠ I346), R393 (= R347), A406 (= A360), G407 (= G361), K426 (= K380)
Query Sequence
>14729 FitnessBrowser__Keio:14729
MDTSLAEEVQQTMATLAPNRFFFMSPYRSFTTSGCFARFDEPAVNGDSPDSPFQQKLAAL
FADAKAQGIKNPVMVGAIPFDPRQPSSLYIPESWQSFSRQEKQASARRFTRSQSLNVVER
QAIPEQTTFEQMVARAAALTATPQVDKVVLSRLIDITTDAAIDSGVLLERLIAQNPVSYN
FHVPLADGGVLLGASPELLLRKDGERFSSIPLAGSARRQPDEVLDREAGNRLLASEKDRH
EHELVTQAMKEVLRERSSELHVPSSPQLITTPTLWHLATPFEGKANSQENALTLACLLHP
TPALSGFPHQAATQVIAELEPFDRELFGGIVGWCDSEGNGEWVVTIRCAKLRENQVRLFA
GAGIVPASSPLGEWRETGVKLSTMLNVFGLH
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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