SitesBLAST
Comparing AO353_24000 FitnessBrowser__pseudo3_N2E3:AO353_24000 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)
5jy8A An iron-bound structure of the isochorismate synthase entc (see paper)
47% identity, 94% coverage: 23:389/391 of query aligns to 6:368/368 of 5jy8A
- active site: K125 (= K145), E175 (= E195), A191 (= A211), E219 (= E239), H254 (= H274), A281 (= A302), F305 (= F326), R325 (= R346), G341 (= G362), E354 (= E375), K358 (= K379)
- binding fe (iii) ion: E219 (= E239), E237 (≠ Q257), H239 (≠ D259), E354 (= E375)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E175 (= E195), L190 (= L210), A191 (= A211), G192 (= G212), E219 (= E239), L282 (≠ V303), I324 (= I345), F337 (= F358), A338 (= A359), G339 (= G360), E354 (= E375), K358 (= K379)
5jxzA A low magnesium structure of the isochorismate synthase, entc (see paper)
46% identity, 94% coverage: 23:389/391 of query aligns to 7:373/373 of 5jxzA
- active site: K130 (= K145), E180 (= E195), A196 (= A211), E224 (= E239), H259 (= H274), A286 (= A302), F310 (= F326), R330 (= R346), G346 (= G362), E359 (= E375), K363 (= K379)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: L195 (= L210), G197 (= G212), S198 (= S213), E224 (= E239), A286 (= A302), I329 (= I345), R330 (= R346), A343 (= A359), G344 (= G360), E359 (= E375), K363 (= K379)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E180 (= E195), L195 (= L210), A196 (= A211), G197 (= G212), E224 (= E239), A286 (= A302), I329 (= I345), R330 (= R346), G344 (= G360), A345 (= A361), E359 (= E375), K363 (= K379)
- binding magnesium ion: E224 (= E239), E359 (= E375)
P0AEJ2 Isochorismate synthase EntC; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see paper)
45% identity, 98% coverage: 8:389/391 of query aligns to 6:390/391 of P0AEJ2
- T140 (≠ F138) binding
- T142 (≠ H140) binding
- V145 (= V143) binding
- D146 (≠ R144) binding
- G214 (= G212) binding
- S215 (= S213) binding
- E241 (= E239) binding ; binding
- A303 (= A302) binding ; mutation to T: Loss of mutase activity.
- L304 (≠ V303) mutation to A: Loss of mutase activity.
- F327 (= F326) mutation to Y: Loss of mutase activity.
- I346 (= I345) mutation to L: Loss of mutase activity.
- R347 (= R346) binding
- F359 (= F358) mutation to Q: Loss of mutase activity.
- G361 (= G360) binding
- E376 (= E375) binding
- K380 (= K379) binding
3hwoA Crystal structure of escherichia coli enterobactin-specific isochorismate synthase entc in complex with isochorismate (see paper)
47% identity, 94% coverage: 23:389/391 of query aligns to 9:378/379 of 3hwoA
- active site: K135 (= K145), E185 (= E195), A201 (= A211), E229 (= E239), H264 (= H274), A291 (= A302), F315 (= F326), R335 (= R346), G351 (= G362), E364 (= E375), K368 (= K379)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: G202 (= G212), S203 (= S213), E229 (= E239), H264 (= H274), I334 (= I345), R335 (= R346), A348 (= A359), G349 (= G360), E364 (= E375), K368 (= K379)
- binding magnesium ion: T128 (≠ F138), T130 (≠ H140), V133 (= V143), D134 (≠ R144), E229 (= E239), E364 (= E375)
P45744 Isochorismate synthase DhbC; Isochorismate mutase; EC 5.4.4.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 95% coverage: 22:391/391 of query aligns to 23:397/398 of P45744
- S271 (= S265) modified: Phosphoserine
P38051 Isochorismate synthase MenF; Isochorismate hydroxymutase; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see 2 papers)
30% identity, 85% coverage: 47:379/391 of query aligns to 60:420/431 of P38051
- K190 (= K145) active site, Proton acceptor; mutation to A: Lack of activity.
- E240 (= E195) active site, Proton donor; mutation to Q: Lack of activity.
- L255 (= L210) mutation to A: Decrease in activity.
- E284 (= E239) binding
- A344 (= A302) mutation to T: Lack of activity.
- R387 (= R346) mutation to A: Lack of activity.
- E416 (= E375) binding
3bznA Crystal structure of open form of menaquinone-specific isochorismate synthase, menf (see paper)
30% identity, 85% coverage: 47:379/391 of query aligns to 60:420/430 of 3bznA
- active site: K190 (= K145), E240 (= E195), A256 (= A211), E284 (= E239), H318 (= H274), A344 (= A302), Y368 (≠ F326), R387 (= R346), G403 (= G362), E416 (= E375), K420 (= K379)
- binding magnesium ion: E284 (= E239), E416 (= E375)
7pi1DDD Aminodeoxychorismate synthase component 1
28% identity, 68% coverage: 124:390/391 of query aligns to 192:456/459 of 7pi1DDD
Sites not aligning to the query:
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)
28% identity, 68% coverage: 124:390/391 of query aligns to 199:463/470 of P28820
- A283 (= A211) 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.
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)
30% identity, 69% coverage: 117:386/391 of query aligns to 205:473/489 of O94582
- S390 (≠ C304) modified: Phosphoserine
- S392 (≠ F306) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
30% identity, 55% coverage: 169:384/391 of query aligns to 291:512/524 of A0QX93
- K355 (≠ D228) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
30% identity, 55% coverage: 169:384/391 of query aligns to 270:487/499 of 7bvdA
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
28% identity, 74% coverage: 94:384/391 of query aligns to 183:491/505 of 5cwaA
- active site: Q248 (vs. gap), E301 (= E195), A317 (= A211), E345 (= E239), H382 (= H274), T409 (≠ A302), Y433 (≠ F326), R453 (= R346), G469 (= G362), E482 (= E375), K486 (= K379)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (≠ F326), I452 (= I345), A466 (= A359), G467 (= G360), K486 (= K379)
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)
27% identity, 55% coverage: 169:385/391 of query aligns to 233:449/453 of P05041
- E258 (= E195) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A211) 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 (= G212) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (≠ A248) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ E253) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ Q257) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H274) 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)
26% identity, 66% coverage: 125:383/391 of query aligns to 147:402/408 of 2fn1A
- active site: K167 (= K145), E214 (= E195), A230 (= A211), E258 (= E239), H295 (= H274), T322 (≠ A302), Y346 (≠ F326), R365 (= R346), G381 (= G362), E394 (= E375), K398 (= K379)
- binding magnesium ion: E258 (= E239), E394 (= E375)
- binding pyruvic acid: Y346 (≠ F326), L364 (≠ I345), R365 (= R346), A378 (= A359), G379 (= G360), K398 (= K379)
2fn0A Crystal structure of yersinia enterocolitica salicylate synthase (irp9) (see paper)
26% identity, 66% coverage: 125:383/391 of query aligns to 147:402/408 of 2fn0A
- active site: K167 (= K145), E214 (= E195), A230 (= A211), E258 (= E239), H295 (= H274), T322 (≠ A302), Y346 (≠ F326), R365 (= R346), G381 (= G362), E394 (= E375), K398 (= K379)
- binding acetate ion: Y346 (≠ F326), L364 (≠ I345), R365 (= R346), A378 (= A359), G379 (= G360)
- binding magnesium ion: E258 (= E239), E394 (= E375)
- binding phosphate ion: A230 (= A211), G231 (= G212), T232 (≠ S213), E258 (= E239), G381 (= G362), E394 (= E375), K398 (= K379)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
26% identity, 66% coverage: 125:383/391 of query aligns to 163:418/424 of 5jy9B
- active site: K183 (= K145), E230 (= E195), A246 (= A211), E274 (= E239), H311 (= H274), T338 (≠ A302), Y362 (≠ F326), R381 (= R346), G397 (= G362), E410 (= E375), K414 (= K379)
- binding fe (ii) ion: E274 (= E239), E410 (= E375)
P32068 Anthranilate synthase alpha subunit 1, chloroplastic; Anthranilate synthase component 1-1; Anthranilate synthase component I-1; Protein A-METHYL TRYPTOPHAN RESISTANT 1; Protein JASMONATE-INDUCED DEFECTIVE LATERAL ROOT 1; Protein TRYPTOPHAN BIOSYNTHESIS 5; Protein WEAK ETHYLENE INSENSITIVE 2; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 70% coverage: 116:390/391 of query aligns to 299:588/595 of P32068
- D341 (≠ Q158) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
30% identity, 58% coverage: 167:391/391 of query aligns to 279:511/517 of 1i7qA
- active site: E306 (= E195), A324 (= A211), E358 (= E239), H395 (= H274), T422 (= T300), Y446 (≠ F326), R466 (= R346), G482 (= G362), E495 (= E375), K499 (= K379)
- binding magnesium ion: E358 (= E239), E495 (= E375)
- binding pyruvic acid: Y446 (≠ F326), I465 (= I345), R466 (= R346), A479 (= A359), G480 (= G360), K499 (= K379)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
30% identity, 58% coverage: 167:391/391 of query aligns to 273:505/511 of 1i7sA
- active site: E300 (= E195), A318 (= A211), E352 (= E239), H389 (= H274), T416 (= T300), Y440 (≠ F326), R460 (= R346), G476 (= G362), E489 (= E375), K493 (= K379)
- binding tryptophan: P282 (≠ G176), Y283 (= Y177), M284 (≠ H178), V444 (= V330), G445 (= G331), D454 (≠ E340), C456 (≠ V342)
Sites not aligning to the query:
Query Sequence
>AO353_24000 FitnessBrowser__pseudo3_N2E3:AO353_24000
MRSGTLRANDTDEVQAIDEKESFSFTSGDRELTVAGMLQRIETPAIGGENANSLFQKTVM
QALDRARKAGQSNPIIVGAIPFDPAEASCLYIPEHAEWRTRSATVQTDVAALPELIEQKN
IPDEQGFKRAVEHAIVNFRHSDVRKAVLSVQRELVFAQDVDVGAMQNNLRAQNQSGYHFR
VPMPDGATLIGVSPELLVHKDGLNFVSNPLAGSAKRMSDPQADRRNADWLSASEKDHYEH
RLVTEDIATQLGELCTQLDVPQRPSLISTPALWHLSTRIEGTLADPTVSALQLACRLHPT
PAVCGFPTERARRLIRFVEPFERGLFTGMVGWCDAQGNGEWVVTIRCGTVKRNRVRLFAG
AGIVEASSPDSEWTEVQTKLGTMLRACGLAH
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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