SitesBLAST
Comparing WP_012384136.1 NCBI__GCF_000019845.1:WP_012384136.1 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)
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)
36% identity, 94% coverage: 25:472/476 of query aligns to 24:450/453 of P05041
- S36 (= S37) binding L-tryptophan
- E258 (= E280) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K296) 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 (= G297) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R333) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ K338) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S344) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H361) 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)
35% identity, 94% coverage: 25:472/476 of query aligns to 22:434/437 of 1k0eA
- active site: E256 (= E280), K272 (= K296), E286 (= E324), H323 (= H361), S350 (= S388), W374 (≠ Y412), R394 (= R432), G410 (= G448), E423 (= E461), K427 (= K465)
- binding tryptophan: L32 (= L35), H33 (≠ D36), S34 (= S37), Y41 (≠ L44), F44 (≠ Y47), P238 (= P258), F239 (≠ Y259), S240 (≠ A260)
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)
33% identity, 90% coverage: 39:465/476 of query aligns to 35:452/470 of P28820
- A283 (≠ K296) 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
32% identity, 90% coverage: 39:465/476 of query aligns to 33:445/459 of 7pi1DDD
- binding magnesium ion: G428 (= G448), E438 (= E458)
- binding tryptophan: L33 (= L39), E34 (≠ P40), S35 (≠ M41), G39 (= G45), Y41 (= Y47), P242 (= P258), Y243 (= Y259), M244 (≠ A260), Q406 (≠ A426), N408 (= N428)
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)
35% identity, 96% coverage: 15:470/476 of query aligns to 51:512/524 of A0QX93
- K355 (≠ D313) 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)
35% identity, 96% coverage: 15:471/476 of query aligns to 31:492/505 of 5cwaA
- active site: Q248 (= Q227), E301 (= E280), A317 (≠ K296), E345 (= E324), H382 (= H361), T409 (≠ S388), Y433 (= Y412), R453 (= R432), G469 (= G448), E482 (= E461), K486 (= K465)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y412), I452 (= I431), A466 (= A445), G467 (= G446), K486 (= K465)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
35% identity, 95% coverage: 15:465/476 of query aligns to 31:482/499 of 7bvdA
- active site: Q248 (= Q227), E301 (= E280), A317 (≠ K296), E341 (= E324), H378 (= H361), T405 (≠ S388), Y429 (= Y412), R449 (= R432), G465 (= G448), E478 (= E461), K482 (= K465)
- binding pyruvic acid: S93 (≠ C72), G94 (≠ P73), A100 (= A79)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 97% coverage: 6:465/476 of query aligns to 158:623/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I295), K454 (= K296), G455 (= G297), T456 (= T298), M547 (≠ I389), Y570 (= Y412), R590 (= R432), V603 (≠ A445), G604 (= G446), G605 (= G447), A606 (≠ G448), E619 (= E461), K623 (= K465)
- binding tryptophan: L189 (= L35), D190 (= D36), S191 (= S37), S199 (≠ G45), F201 (≠ Y47), P419 (= P258), Y420 (= Y259), G421 (≠ A260), L574 (≠ I416), G575 (= G417)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 97% coverage: 6:465/476 of query aligns to 200:662/673 of 8hx8A
- binding magnesium ion: E521 (= E324), E655 (= E458), E658 (= E461)
- binding tryptophan: L231 (= L35), D232 (= D36), S233 (= S37), S241 (≠ G45), F243 (≠ Y47), P458 (= P258), Y459 (= Y259), G460 (≠ A260), G614 (= G417)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
33% identity, 94% coverage: 25:472/476 of query aligns to 24:417/420 of 1k0gA
- active site: E258 (= E280), K274 (= K296), E278 (= E324), S333 (= S388), W357 (≠ Y412), R377 (= R432), G393 (= G448), E406 (= E461), K410 (= K465)
- binding phosphate ion: D113 (= D109), R116 (≠ P112), D347 (≠ A402), R353 (≠ A408)
- binding tryptophan: L34 (= L35), H35 (≠ D36), S36 (= S37), Y43 (≠ L44), S44 (≠ G45), F46 (≠ Y47), P240 (= P258), F241 (≠ Y259), S242 (≠ A260)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 94% coverage: 25:472/476 of query aligns to 24:414/415 of 1k0gB
- active site: E258 (= E280), K274 (= K296), E277 (= E324), S330 (= S388), W354 (≠ Y412), R374 (= R432), G390 (= G448), E403 (= E461), K407 (= K465)
- binding phosphate ion: Y112 (= Y108), D113 (= D109), R116 (≠ P112), D344 (≠ A402), R350 (≠ A408)
- binding tryptophan: L34 (= L35), H35 (≠ D36), S36 (= S37), Y43 (≠ L44), S44 (≠ G45), R45 (= R46), F46 (≠ Y47), P240 (= P258), F241 (≠ Y259)
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, 96% coverage: 8:466/476 of query aligns to 24:467/489 of O94582
- S390 (≠ T390) modified: Phosphoserine
- S392 (≠ A392) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
34% identity, 77% coverage: 101:465/476 of query aligns to 192:577/595 of P32068
- D341 (= D243) 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)
34% identity, 77% coverage: 101:465/476 of query aligns to 174:559/577 of Q94GF1
- D323 (= D243) mutation to N: Insensitive to feedback inhibition by tryptophan.
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
32% identity, 76% coverage: 104:465/476 of query aligns to 148:502/520 of P00898
- C174 (≠ G131) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N255) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P256) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A260) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A261) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S276) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ S365) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G423) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N428) 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)
32% identity, 76% coverage: 104:465/476 of query aligns to 144:498/512 of 1i1qA
- active site: Q259 (= Q227), E305 (= E280), A323 (≠ K296), E357 (= E324), H394 (= H361), T421 (≠ S388), Y445 (= Y412), R465 (= R432), G481 (= G448), E494 (= E461), K498 (= K465)
- binding tryptophan: P287 (= P258), Y288 (= Y259), M289 (≠ A260), G450 (= G417), C461 (≠ N428)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
31% identity, 81% coverage: 79:465/476 of query aligns to 123:499/517 of 1i7qA
- active site: Q260 (= Q227), E306 (= E280), A324 (≠ K296), E358 (= E324), H395 (= H361), T422 (≠ S388), Y446 (= Y412), R466 (= R432), G482 (= G448), E495 (= E461), K499 (= K465)
- binding magnesium ion: E358 (= E324), E495 (= E461)
- binding pyruvic acid: Y446 (= Y412), I465 (= I431), R466 (= R432), A479 (= A445), G480 (= G446), K499 (= K465)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
31% identity, 81% coverage: 79:465/476 of query aligns to 117:493/511 of 1i7sA
- active site: Q254 (= Q227), E300 (= E280), A318 (≠ K296), E352 (= E324), H389 (= H361), T416 (≠ S388), Y440 (= Y412), R460 (= R432), G476 (= G448), E489 (= E461), K493 (= K465)
- binding tryptophan: P282 (= P258), Y283 (= Y259), M284 (≠ A260), V444 (≠ I416), G445 (= G417), D454 (≠ A426), C456 (≠ N428)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
31% identity, 78% coverage: 79:450/476 of query aligns to 125:486/519 of P00897
- PYM 290:292 (≠ PYA 258:260) binding L-tryptophan
- E360 (= E324) binding Mg(2+)
Sites not aligning to the query:
- 39 binding L-tryptophan
- 497 binding Mg(2+)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
32% identity, 46% coverage: 252:469/476 of query aligns to 190:402/408 of 2fn1A
- active site: E214 (= E280), A230 (≠ K296), E258 (= E324), H295 (= H361), T322 (≠ S388), Y346 (= Y412), R365 (= R432), G381 (= G448), E394 (= E461), K398 (= K465)
- binding magnesium ion: E258 (= E324), E394 (= E461)
- binding pyruvic acid: Y346 (= Y412), L364 (≠ I431), R365 (= R432), A378 (= A445), G379 (= G446), K398 (= K465)
Sites not aligning to the query:
Query Sequence
>WP_012384136.1 NCBI__GCF_000019845.1:WP_012384136.1
MSSLDPLILHVAPLDSIAPLEAAERLVGLPGLAFLDSALPMPRLGRYSYLAADPFGWLTV
ENGIAFWNGQPCPEPPLAALRARLAAHALPKDERLLPLQTGVIGYFAYDFAPCLDPAAKV
VRSQGVQASLGFYDVVLAFDHETGKGWLMASGLPETEPEARHRRAEQRLAQFKSLLERPL
ENPMQGASHRDSPVPTSLAWRQHWRKADYLSAVRRVKEHILAGDLYQANIAQCFEADVPR
GFDSWRFYKDLRSRNPAPYAAFLAQEGRHTGDAIASSSPEAFLSLIDGMVETRPIKGTQK
RLEEPELDAACRDNLARSEKDRAENIMIVDLLRNDLSKVCTAASIEVPDLCVVETYAGVH
HLVSSVTGRLRPGCDALDLFAACFPGGSITGAPKLKAMEIIAAIENRARGPYCGAIGFIA
FNGDMALNIAIRTIVFAGDKACLNAGGGITLLSDPEAEYAESLAKLERIFEREGSA
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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