SitesBLAST
Comparing WP_057509108.1 NCBI__GCF_001431535.1:WP_057509108.1 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)
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)
40% identity, 98% coverage: 9:494/496 of query aligns to 11:479/489 of O94582
- S390 (= S406) modified: Phosphoserine
- S392 (≠ A408) 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)
44% identity, 97% coverage: 7:486/496 of query aligns to 32:512/524 of A0QX93
- K355 (≠ A329) 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)
45% identity, 97% coverage: 7:486/496 of query aligns to 12:491/505 of 5cwaA
- active site: Q248 (= Q244), E301 (= E291), A317 (= A312), E345 (= E340), H382 (= H377), T409 (= T404), Y433 (= Y428), R453 (= R448), G469 (= G464), E482 (= E477), K486 (= K481)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y428), I452 (= I447), A466 (= A461), G467 (= G462), K486 (= K481)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
44% identity, 97% coverage: 7:486/496 of query aligns to 12:487/499 of 7bvdA
- active site: Q248 (= Q244), E301 (= E291), A317 (= A312), E341 (= E340), H378 (= H377), T405 (= T404), Y429 (= Y428), R449 (= R448), G465 (= G464), E478 (= E477), K482 (= K481)
- binding pyruvic acid: S93 (≠ D90), G94 (≠ V91), A100 (≠ E97)
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)
41% identity, 95% coverage: 17:489/496 of query aligns to 4:460/470 of P28820
- A283 (= A312) 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
40% identity, 95% coverage: 17:489/496 of query aligns to 2:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G464), E438 (= E474)
- binding tryptophan: L33 (≠ F47), E34 (= E48), S35 (= S49), G39 (= G53), Y41 (= Y59), P242 (= P273), Y243 (= Y274), M244 (= M275), Q406 (≠ D442), N408 (≠ A444)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 98% coverage: 5:489/496 of query aligns to 51:567/577 of Q94GF1
- D323 (≠ R258) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
39% identity, 97% coverage: 11:489/496 of query aligns to 73:585/595 of P32068
- D341 (≠ R258) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
37% identity, 86% coverage: 64:492/496 of query aligns to 93:509/512 of 1i1qA
- active site: Q259 (= Q244), E305 (= E291), A323 (= A312), E357 (= E340), H394 (= H377), T421 (= T404), Y445 (= Y428), R465 (= R448), G481 (= G464), E494 (= E477), K498 (= K481)
- binding tryptophan: P287 (= P273), Y288 (= Y274), M289 (= M275), G450 (= G433), C461 (≠ A444)
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)
37% identity, 86% coverage: 64:492/496 of query aligns to 97:513/520 of P00898
- R128 (≠ E99) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ L151) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N270) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P271) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M275) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y276) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G287) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ E381) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G439) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A444) 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
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
39% identity, 75% coverage: 120:492/496 of query aligns to 137:504/511 of 1i7sA
- active site: Q254 (= Q244), E300 (= E291), A318 (= A312), E352 (= E340), H389 (= H377), T416 (= T404), Y440 (= Y428), R460 (= R448), G476 (= G464), E489 (= E477), K493 (= K481)
- binding tryptophan: P282 (= P273), Y283 (= Y274), M284 (= M275), V444 (≠ I432), G445 (= G433), D454 (= D442), C456 (≠ A444)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
39% identity, 75% coverage: 120:492/496 of query aligns to 143:510/517 of 1i7qA
- active site: Q260 (= Q244), E306 (= E291), A324 (= A312), E358 (= E340), H395 (= H377), T422 (= T404), Y446 (= Y428), R466 (= R448), G482 (= G464), E495 (= E477), K499 (= K481)
- binding magnesium ion: E358 (= E340), E495 (= E477)
- binding pyruvic acid: Y446 (= Y428), I465 (= I447), R466 (= R448), A479 (= A461), G480 (= G462), K499 (= K481)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
34% identity, 93% coverage: 31:492/496 of query aligns to 20:512/519 of P00897
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)
31% identity, 96% coverage: 16:491/496 of query aligns to 3:453/453 of P05041
- S36 (= S49) binding
- E258 (= E291) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A312) 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 (= G313) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R349) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R354) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T360) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H377) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
31% identity, 96% coverage: 16:491/496 of query aligns to 1:437/437 of 1k0eA
- active site: E256 (= E291), K272 (≠ A312), E286 (= E340), H323 (= H377), S350 (≠ T404), W374 (≠ Y428), R394 (= R448), G410 (= G464), E423 (= E477), K427 (= K481)
- binding tryptophan: L32 (≠ F47), H33 (≠ E48), S34 (= S49), Y41 (≠ F56), F44 (≠ Y59), P238 (= P273), F239 (≠ Y274), S240 (≠ M275)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
33% identity, 90% coverage: 44:489/496 of query aligns to 228:670/673 of 8hx8A
- binding magnesium ion: E521 (= E340), E655 (= E474), E658 (= E477)
- binding tryptophan: L231 (≠ F47), D232 (≠ E48), S233 (= S49), S241 (≠ G57), F243 (≠ Y59), P458 (= P273), Y459 (= Y274), G460 (≠ M275), G614 (= G433)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
33% identity, 90% coverage: 44:489/496 of query aligns to 186:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I311), K454 (≠ A312), G455 (= G313), T456 (= T314), M547 (≠ V405), Y570 (= Y428), R590 (= R448), V603 (≠ A461), G604 (= G462), G605 (≠ A463), A606 (≠ G464), E619 (= E477), K623 (= K481)
- binding tryptophan: L189 (≠ F47), D190 (≠ E48), S191 (= S49), S199 (≠ G57), F201 (≠ Y59), P419 (= P273), Y420 (= Y274), G421 (≠ M275), L574 (≠ I432), G575 (= G433)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 96% coverage: 16:491/496 of query aligns to 3:420/420 of 1k0gA
- active site: E258 (= E291), K274 (= K336), E278 (= E340), S333 (≠ T404), W357 (≠ Y428), R377 (= R448), G393 (= G464), E406 (= E477), K410 (= K481)
- binding phosphate ion: D113 (≠ E127), R116 (≠ G130), D347 (≠ R418), R353 (≠ K424)
- binding tryptophan: L34 (≠ F47), H35 (≠ E48), S36 (= S49), Y43 (≠ F56), S44 (≠ G57), F46 (≠ Y59), P240 (= P273), F241 (≠ Y274), S242 (≠ M275)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 96% coverage: 16:489/496 of query aligns to 3:415/415 of 1k0gB
- active site: E258 (= E291), K274 (≠ A312), E277 (= E340), S330 (≠ T404), W354 (≠ Y428), R374 (= R448), G390 (= G464), E403 (= E477), K407 (= K481)
- binding phosphate ion: Y112 (≠ F126), D113 (≠ E127), R116 (≠ G130), D344 (≠ R418), R350 (≠ K424)
- binding tryptophan: L34 (≠ F47), H35 (≠ E48), S36 (= S49), Y43 (≠ F56), S44 (≠ G57), R45 (= R58), F46 (≠ Y59), P240 (= P273), F241 (≠ Y274)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
30% identity, 53% coverage: 219:481/496 of query aligns to 158:414/424 of 5jy9B
- active site: K183 (≠ Q244), E230 (= E291), A246 (= A312), E274 (= E340), H311 (= H377), T338 (= T404), Y362 (= Y428), R381 (= R448), G397 (= G464), E410 (= E477), K414 (= K481)
- binding fe (ii) ion: E274 (= E340), E410 (= E477)
Query Sequence
>WP_057509108.1 NCBI__GCF_001431535.1:WP_057509108.1
MNTPAQFQQQAAEGHTRIPVVREVLSDLDTPLSVYLKLADGPHTYLFESVEGGERFGRYS
IIGLPARRVYTFRGHTLTIAEHGQVVETRDVADPFAEVEALRSAHSVPKLDGLPGFTGGL
VGWFGFECIGYIEPRLAPPAGRDELGTPDILLMHSEELAVFDNLKGRLYLIVHADPRQPG
AWDEAQARLDALAGKLRAPGAGYPAPLHSDVLDEGDFISGFTREGFIDAVERSKDYIRSG
DIFQVVLSQRLSVPFKARPVDVYRALRALNPSPYMYFLDVGDMQVVGSSPEILVRLQHDA
EGVGHVTVRPIAGTRPRGATVEEDNALEAELLADPKERAEHLMLIDLGRNDAGRVSRAGT
VEVGEQFVIERYSHVMHIVSEVTGQLQPGLSYADVLRATFPAGTVSGAPKIRALEVIREL
EPIKRNVYAGSIGYIGWHGDADTAIAIRTAVIKDGRLHVQAGAGIVYDSDPQKEWDETMN
KGRALFRAVAQAAKGL
Or try a new SitesBLAST search
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