SitesBLAST
Comparing WP_013821147.1 NCBI__GCF_000214665.1:WP_013821147.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
40% identity, 98% coverage: 10:493/494 of query aligns to 73:595/595 of P32068
- D341 (≠ S257) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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)
41% identity, 96% coverage: 15:487/494 of query aligns to 20:478/489 of O94582
- S390 (= S400) modified: Phosphoserine
- S392 (≠ A402) 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, 94% coverage: 17:480/494 of query aligns to 42:512/524 of A0QX93
- K355 (≠ Q323) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7pi1DDD Aminodeoxychorismate synthase component 1
41% identity, 96% coverage: 16:487/494 of query aligns to 2:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G458), E438 (= E468)
- binding tryptophan: L33 (≠ F46), E34 (= E47), S35 (= S48), G39 (= G52), Y41 (= Y58), P242 (= P272), Y243 (= Y273), M244 (= M274), Q406 (≠ D436), N408 (≠ A438)
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)
40% identity, 96% coverage: 16:487/494 of query aligns to 4:464/470 of P28820
- A283 (= A306) 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.
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: 4:488/494 of query aligns to 51:572/577 of Q94GF1
- D323 (≠ S257) mutation to N: Insensitive to feedback inhibition by tryptophan.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
43% identity, 94% coverage: 17:480/494 of query aligns to 22:491/505 of 5cwaA
- active site: Q248 (= Q243), E301 (= E290), A317 (= A306), E345 (= E334), H382 (= H371), T409 (= T398), Y433 (= Y422), R453 (= R442), G469 (= G458), E482 (= E471), K486 (= K475)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y422), I452 (= I441), A466 (= A455), G467 (= G456), K486 (= K475)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 94% coverage: 17:480/494 of query aligns to 22:487/499 of 7bvdA
- active site: Q248 (= Q243), E301 (= E290), A317 (= A306), E341 (= E334), H378 (= H371), T405 (= T398), Y429 (= Y422), R449 (= R442), G465 (= G458), E478 (= E471), K482 (= K475)
- binding pyruvic acid: S93 (≠ T85), G94 (≠ Q86), A100 (≠ W96)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
38% identity, 77% coverage: 105:486/494 of query aligns to 135:513/520 of P00898
- C174 (≠ L150) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N269) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P270) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M274) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y275) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G286) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N375) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G433) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A438) 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
38% identity, 77% coverage: 105:486/494 of query aligns to 131:509/512 of 1i1qA
- active site: Q259 (= Q243), E305 (= E290), A323 (= A306), E357 (= E334), H394 (= H371), T421 (= T398), Y445 (= Y422), R465 (= R442), G481 (= G458), E494 (= E471), K498 (= K475)
- binding tryptophan: P287 (= P272), Y288 (= Y273), M289 (= M274), G450 (= G427), C461 (≠ A438)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
37% identity, 74% coverage: 119:486/494 of query aligns to 143:510/517 of 1i7qA
- active site: Q260 (= Q243), E306 (= E290), A324 (= A306), E358 (= E334), H395 (= H371), T422 (= T398), Y446 (= Y422), R466 (= R442), G482 (= G458), E495 (= E471), K499 (= K475)
- binding magnesium ion: E358 (= E334), E495 (= E471)
- binding pyruvic acid: Y446 (= Y422), I465 (= I441), R466 (= R442), A479 (= A455), G480 (= G456), K499 (= K475)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
37% identity, 74% coverage: 119:486/494 of query aligns to 137:504/511 of 1i7sA
- active site: Q254 (= Q243), E300 (= E290), A318 (= A306), E352 (= E334), H389 (= H371), T416 (= T398), Y440 (= Y422), R460 (= R442), G476 (= G458), E489 (= E471), K493 (= K475)
- binding tryptophan: P282 (= P272), Y283 (= Y273), M284 (= M274), V444 (= V426), G445 (= G427), D454 (= D436), C456 (≠ A438)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
37% identity, 74% coverage: 119:486/494 of query aligns to 145:512/519 of P00897
- PYM 290:292 (= PYM 272:274) binding L-tryptophan
- E360 (= E334) binding Mg(2+)
- E497 (= E471) binding Mg(2+)
Sites not aligning to the query:
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)
32% identity, 91% coverage: 34:483/494 of query aligns to 22:451/453 of P05041
- S36 (= S48) binding L-tryptophan
- E258 (= E290) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A306) 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 (= G307) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R343) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R348) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S354) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H371) 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)
32% identity, 91% coverage: 34:481/494 of query aligns to 20:433/437 of 1k0eA
- active site: E256 (= E290), K272 (≠ A306), E286 (= E334), H323 (= H371), S350 (≠ T398), W374 (≠ Y422), R394 (= R442), G410 (= G458), E423 (= E471), K427 (= K475)
- binding tryptophan: L32 (≠ F46), H33 (≠ E47), S34 (= S48), Y41 (≠ W55), F44 (≠ Y58), P238 (= P272), F239 (≠ Y273), S240 (≠ M274)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
34% identity, 81% coverage: 82:483/494 of query aligns to 270:670/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
34% identity, 81% coverage: 82:483/494 of query aligns to 228:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I305), K454 (≠ A306), G455 (= G307), T456 (= T308), M547 (≠ V399), Y570 (= Y422), R590 (= R442), V603 (≠ A455), G604 (= G456), G605 (≠ A457), A606 (≠ G458), E619 (= E471), K623 (= K475)
- binding tryptophan: P419 (= P272), Y420 (= Y273), G421 (≠ M274), L574 (≠ V426), G575 (= G427)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 34:483/494 of query aligns to 22:418/420 of 1k0gA
- active site: E258 (= E290), K274 (= K330), E278 (= E334), S333 (≠ T398), W357 (≠ Y422), R377 (= R442), G393 (= G458), E406 (= E471), K410 (= K475)
- binding phosphate ion: D113 (≠ E126), R116 (≠ Y130), D347 (= D412), R353 (≠ K418)
- binding tryptophan: L34 (≠ F46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), F46 (≠ Y58), P240 (= P272), F241 (≠ Y273), S242 (≠ M274)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 34:483/494 of query aligns to 22:415/415 of 1k0gB
- active site: E258 (= E290), K274 (≠ A306), E277 (= E334), S330 (≠ T398), W354 (≠ Y422), R374 (= R442), G390 (= G458), E403 (= E471), K407 (= K475)
- binding phosphate ion: Y112 (= Y125), D113 (≠ E126), R116 (≠ Y130), D344 (= D412), R350 (≠ K418)
- binding tryptophan: L34 (≠ F46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), R45 (= R57), F46 (≠ Y58), P240 (= P272), F241 (≠ Y273)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
32% identity, 52% coverage: 218:475/494 of query aligns to 158:414/424 of 5jy9B
- active site: K183 (≠ Q243), E230 (= E290), A246 (= A306), E274 (= E334), H311 (= H371), T338 (= T398), Y362 (= Y422), R381 (= R442), G397 (= G458), E410 (= E471), K414 (= K475)
- binding fe (ii) ion: E274 (= E334), E410 (= E471)
Query Sequence
>WP_013821147.1 NCBI__GCF_000214665.1:WP_013821147.1
MTPAQFTDYAQQGYNRIPVCREVLADLDTPLSAYLKLADGAYSYLFESVHGGEQWGRYSI
IGLPCKTRVKISGNTISLEQDGADTQTFEHAQPLEWIEEFRQQYQVPDIEGLPRFNGGLV
GYFGYETIGYIEPRLKSAGKPDPIGTPDILLMVSQDLLVFDNLSGKMLLLTHADPAQEGA
YELAQARLAELVDKLHQLKAHPQPHPAVKQVHENDFVSGFTQQGFEDAVRKAKQYITDGD
VMQVVLSQRMSIPFSASPLDLYRSLRCLNPSPYMYYLNLDGFHIVGSSPEILVRLEDDEV
TVRPIAGTRPRGATHEQDQALEQELLADPKEIAEHLMLIDLGRNDAGRVAKIGSVKLTDK
MIIERYSHVMHIVSNVTGQLQDGKNAFDVLAATFPAGTVSGAPKIRAMEIIDELEPVKRG
IYSGAVGYISWSGNLDTAIAIRTAVIKDQTLHIQAGAGIVYDSVPRNEWDETMNKGRAVF
RAVSMAEAGLGGKA
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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