SitesBLAST
Comparing WP_022046192.1 NCBI__GCF_001406815.1:WP_022046192.1 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)
7pi1DDD Aminodeoxychorismate synthase component 1
38% identity, 98% coverage: 6:464/470 of query aligns to 3:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G439), E438 (= E449)
- binding tryptophan: L33 (= L35), E34 (= E36), S35 (= S37), G39 (≠ N41), Y41 (= Y45), P242 (= P253), Y243 (= Y254), M244 (≠ L255), Q406 (≠ D417), N408 (≠ C419)
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)
40% identity, 95% coverage: 16:460/470 of query aligns to 52:511/524 of A0QX93
- K355 (≠ D304) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
37% identity, 98% coverage: 6:464/470 of query aligns to 5:460/470 of P28820
- A283 (= A287) 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.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
40% identity, 95% coverage: 16:460/470 of query aligns to 32:486/499 of 7bvdA
- active site: Q248 (= Q224), E301 (= E271), A317 (= A287), E341 (= E315), H378 (= H352), T405 (= T379), Y429 (= Y403), R449 (= R423), G465 (= G439), E478 (= E452), K482 (= K456)
- binding pyruvic acid: S93 (≠ R75), G94 (≠ Q76), A100 (≠ R82)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
39% identity, 95% coverage: 16:460/470 of query aligns to 32:490/505 of 5cwaA
- active site: Q248 (= Q224), E301 (= E271), A317 (= A287), E345 (= E315), H382 (= H352), T409 (= T379), Y433 (= Y403), R453 (= R423), G469 (= G439), E482 (= E452), K486 (= K456)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y403), I452 (= I422), A466 (= A436), G467 (= G437), K486 (= K456)
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)
37% identity, 92% coverage: 32:464/470 of query aligns to 110:585/595 of P32068
- D341 (≠ T238) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
36% identity, 92% coverage: 33:464/470 of query aligns to 95:567/577 of Q94GF1
- D323 (≠ T238) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
36% identity, 94% coverage: 28:470/470 of query aligns to 45:480/489 of O94582
- S390 (= S381) modified: Phosphoserine
- S392 (≠ A383) 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)
33% identity, 91% coverage: 39:464/470 of query aligns to 40:451/453 of P05041
- E258 (= E271) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A287) 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 (= G288) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R324) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R329) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T335) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H352) 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:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
33% identity, 91% coverage: 39:464/470 of query aligns to 38:435/437 of 1k0eA
- active site: E256 (= E271), K272 (≠ A287), E286 (= E315), H323 (= H352), S350 (≠ T379), W374 (≠ Y403), R394 (= R423), G410 (= G439), E423 (= E452), K427 (= K456)
- binding tryptophan: Y41 (= Y42), F44 (≠ Y45), P238 (= P253), F239 (≠ Y254), S240 (≠ L255)
Sites not aligning to the query:
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
36% identity, 80% coverage: 91:464/470 of query aligns to 131:506/512 of 1i1qA
- active site: Q259 (= Q224), E305 (= E271), A323 (= A287), E357 (= E315), H394 (= H352), T421 (= T379), Y445 (= Y403), R465 (= R423), G481 (= G439), E494 (= E452), K498 (= K456)
- binding tryptophan: P287 (= P253), Y288 (= Y254), M289 (≠ L255), G450 (= G408), C461 (= C419)
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)
36% identity, 80% coverage: 91:464/470 of query aligns to 135:510/520 of P00898
- C174 (≠ I128) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N250) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P251) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L255) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y256) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G267) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ M356) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G414) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C419) 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 L-tryptophan; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding L-tryptophan
- 128 R→H: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
41% identity, 57% coverage: 197:464/470 of query aligns to 235:507/517 of 1i7qA
- active site: Q260 (= Q224), E306 (= E271), A324 (= A287), E358 (= E315), H395 (= H352), T422 (= T379), Y446 (= Y403), R466 (= R423), G482 (= G439), E495 (= E452), K499 (= K456)
- binding magnesium ion: E358 (= E315), E495 (= E452)
- binding pyruvic acid: Y446 (= Y403), I465 (= I422), R466 (= R423), A479 (= A436), G480 (= G437), K499 (= K456)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
41% identity, 57% coverage: 197:464/470 of query aligns to 229:501/511 of 1i7sA
- active site: Q254 (= Q224), E300 (= E271), A318 (= A287), E352 (= E315), H389 (= H352), T416 (= T379), Y440 (= Y403), R460 (= R423), G476 (= G439), E489 (= E452), K493 (= K456)
- binding tryptophan: P282 (= P253), Y283 (= Y254), M284 (≠ L255), V444 (≠ T407), G445 (= G408), D454 (= D417), C456 (= C419)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 91% coverage: 39:464/470 of query aligns to 40:418/420 of 1k0gA
- active site: E258 (= E271), K274 (= K311), E278 (= E315), S333 (≠ T379), W357 (≠ Y403), R377 (= R423), G393 (= G439), E406 (= E452), K410 (= K456)
- binding phosphate ion: D113 (= D112), R116 (= R115), D347 (= D393), R353 (= R399)
- binding tryptophan: Y43 (= Y42), S44 (≠ D43), F46 (≠ Y45), P240 (= P253), F241 (≠ Y254), S242 (≠ L255)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
41% identity, 57% coverage: 197:464/470 of query aligns to 237:509/519 of P00897
- PYM 290:292 (≠ PYL 253:255) binding L-tryptophan
- E360 (= E315) binding Mg(2+)
- E497 (= E452) binding Mg(2+)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 91% coverage: 39:464/470 of query aligns to 40:415/415 of 1k0gB
- active site: E258 (= E271), K274 (≠ A287), E277 (= E315), S330 (≠ T379), W354 (≠ Y403), R374 (= R423), G390 (= G439), E403 (= E452), K407 (= K456)
- binding phosphate ion: Y112 (= Y111), D113 (= D112), R116 (= R115), D344 (= D393), R350 (= R399)
- binding tryptophan: Y43 (= Y42), S44 (≠ D43), R45 (= R44), F46 (≠ Y45), P240 (= P253), F241 (≠ Y254)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
32% identity, 93% coverage: 26:464/470 of query aligns to 222:670/673 of 8hx8A
- binding magnesium ion: E521 (= E315), E655 (= E449), E658 (= E452)
- binding tryptophan: L231 (= L35), D232 (≠ E36), S233 (= S37), S241 (≠ D43), F243 (≠ Y45), P458 (= P253), Y459 (= Y254), G460 (≠ L255), G614 (= G408)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 93% coverage: 26:464/470 of query aligns to 180:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I286), K454 (≠ A287), G455 (= G288), T456 (= T289), M547 (≠ L380), Y570 (= Y403), R590 (= R423), V603 (≠ A436), G604 (= G437), G605 (≠ A438), A606 (≠ G439), E619 (= E452), K623 (= K456)
- binding tryptophan: L189 (= L35), D190 (≠ E36), S191 (= S37), S199 (≠ D43), F201 (≠ Y45), P419 (= P253), Y420 (= Y254), G421 (≠ L255), L574 (≠ T407), G575 (= G408)
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)
31% identity, 56% coverage: 204:465/470 of query aligns to 147:407/408 of 2fn1A
- active site: K167 (≠ Q224), E214 (= E271), A230 (= A287), E258 (= E315), H295 (= H352), T322 (= T379), Y346 (= Y403), R365 (= R423), G381 (= G439), E394 (= E452), K398 (= K456)
- binding magnesium ion: E258 (= E315), E394 (= E452)
- binding pyruvic acid: Y346 (= Y403), L364 (≠ I422), R365 (= R423), A378 (= A436), G379 (= G437), K398 (= K456)
Query Sequence
>WP_022046192.1 NCBI__GCF_001406815.1:WP_022046192.1
MKRRLRVYKKTVSIVNETAIGMYESLVGNKKGFLLESYDKNYDRYTFFGKEPEEIITSRG
DALVIRRNNGTEEIRQGNPLERLKEYYSEFDIVKENEELSFSGGLVGNLGYDFVRYAEVL
PDNNPDEIGIETIQMMLMTKFILVDHVAETLTAVILGEDSEDGKKKALAEAAELIEEARK
NAGQIPDRNFTHDGVIVNQSDTLEQYCEKVEKIKQYIREGHIFQTVLSQRWTIETKQTGF
ELYKELRELNPSPYLYYFNYGEFEVIGSSPEMIVKQQGSRVYTCPIAGTRRRGVDAEEDA
LLRDELLRDEKERAEHVMLVDLARNDMGRISEFGTVKVTQFMEVQNYSHVMHIVSMVEGK
KKGEFHPLDLVSSFLPAGTLSGAPKIRAMEIIDELESVRRGLYGGATGYIDFSGDMDFCI
TIRTMIKKKNRVYLQAGAGIVADSVPENEYQECCNKVMALAKTLIEEENL
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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