SitesBLAST
Comparing N515DRAFT_2823 N515DRAFT_2823 anthranilate synthase component 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
43% identity, 79% coverage: 95:449/449 of query aligns to 96:457/459 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)
42% identity, 79% coverage: 95:449/449 of query aligns to 98:464/470 of P28820
- A283 (= A269) 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.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
38% identity, 83% coverage: 72:445/449 of query aligns to 282:670/673 of 8hx8A
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)
35% identity, 94% coverage: 25:445/449 of query aligns to 30:451/453 of P05041
- S36 (= S31) binding
- E258 (= E253) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A269) 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 (= G270) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R305) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R310) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S316) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H333) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
38% identity, 83% coverage: 72:445/449 of query aligns to 240:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I268), K454 (≠ A269), G455 (= G270), T456 (= T271), M547 (≠ I361), Y570 (= Y384), R590 (= R404), V603 (≠ A417), G604 (= G418), G605 (≠ A419), A606 (≠ G420), E619 (= E433), K623 (= K437)
- binding tryptophan: P419 (= P235), Y420 (≠ F236), G421 (≠ A237), L574 (= L388), G575 (= G389)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
38% identity, 93% coverage: 28:443/449 of query aligns to 51:492/505 of 5cwaA
- active site: Q248 (= Q204), E301 (= E253), A317 (= A269), E345 (= E296), H382 (= H333), T409 (= T360), Y433 (= Y384), R453 (= R404), G469 (= G420), E482 (= E433), K486 (= K437)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y384), I452 (= I403), A466 (= A417), G467 (= G418), K486 (= K437)
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
34% identity, 94% coverage: 25:445/449 of query aligns to 28:435/437 of 1k0eA
- active site: E256 (= E253), K272 (≠ A269), E286 (= E296), H323 (= H333), S350 (≠ T360), W374 (≠ Y384), R394 (= R404), G410 (= G420), E423 (= E433), K427 (= K437)
- binding tryptophan: L32 (= L29), H33 (≠ Q30), S34 (= S31), Y41 (≠ Q38), F44 (= F41), P238 (= P235), F239 (= F236), S240 (≠ A237)
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)
36% identity, 93% coverage: 28:443/449 of query aligns to 71:513/524 of A0QX93
- K355 (≠ R285) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
35% identity, 79% coverage: 95:449/449 of query aligns to 189:589/595 of P32068
- D341 (= D217) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
38% identity, 85% coverage: 64:443/449 of query aligns to 89:488/499 of 7bvdA
- active site: Q248 (= Q204), E301 (= E253), A317 (= A269), E341 (= E296), H378 (= H333), T405 (= T360), Y429 (= Y384), R449 (= R404), G465 (= G420), E478 (= E433), K482 (= K437)
- binding pyruvic acid: S93 (≠ H68), G94 (≠ A69), A100 (= A75)
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)
33% identity, 96% coverage: 13:445/449 of query aligns to 31:474/489 of O94582
- S390 (≠ T362) modified: Phosphoserine
- S392 (≠ C364) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
35% identity, 80% coverage: 91:449/449 of query aligns to 165:571/577 of Q94GF1
- D323 (= D217) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
37% identity, 79% coverage: 95:448/449 of query aligns to 141:509/512 of 1i1qA
- active site: Q259 (= Q204), E305 (= E253), A323 (= A269), E357 (= E296), H394 (= H333), T421 (= T360), Y445 (= Y384), R465 (= R404), G481 (= G420), E494 (= E433), K498 (= K437)
- binding tryptophan: P287 (= P235), Y288 (≠ F236), M289 (≠ A237), G450 (= G389), C461 (≠ N400)
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, 79% coverage: 95:448/449 of query aligns to 145:513/520 of P00898
- C174 (≠ L127) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N232) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P233) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A237) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ G238) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S249) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N337) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G395) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N400) 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
- 128 R→H: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 94% coverage: 25:445/449 of query aligns to 30:418/420 of 1k0gA
- active site: E258 (= E253), K274 (= K292), E278 (= E296), S333 (≠ T360), W357 (≠ Y384), R377 (= R404), G393 (= G420), E406 (= E433), K410 (= K437)
- binding phosphate ion: D113 (≠ E106), R116 (≠ G109), D347 (≠ H374), R353 (≠ P380)
- binding tryptophan: L34 (= L29), H35 (≠ Q30), S36 (= S31), Y43 (≠ Q38), S44 (≠ A39), F46 (= F41), P240 (= P235), F241 (= F236), S242 (≠ A237)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
43% identity, 58% coverage: 190:448/449 of query aligns to 246:510/517 of 1i7qA
- active site: Q260 (= Q204), E306 (= E253), A324 (= A269), E358 (= E296), H395 (= H333), T422 (= T360), Y446 (= Y384), R466 (= R404), G482 (= G420), E495 (= E433), K499 (= K437)
- binding magnesium ion: E358 (= E296), E495 (= E433)
- binding pyruvic acid: Y446 (= Y384), I465 (= I403), R466 (= R404), A479 (= A417), G480 (= G418), K499 (= K437)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
43% identity, 58% coverage: 190:448/449 of query aligns to 240:504/511 of 1i7sA
- active site: Q254 (= Q204), E300 (= E253), A318 (= A269), E352 (= E296), H389 (= H333), T416 (= T360), Y440 (= Y384), R460 (= R404), G476 (= G420), E489 (= E433), K493 (= K437)
- binding tryptophan: P282 (= P235), Y283 (≠ F236), M284 (≠ A237), V444 (≠ L388), G445 (= G389), D454 (= D398), C456 (≠ N400)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
42% identity, 58% coverage: 190:448/449 of query aligns to 248:512/519 of P00897
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 94% coverage: 25:445/449 of query aligns to 30:415/415 of 1k0gB
- active site: E258 (= E253), K274 (≠ A269), E277 (= E296), S330 (≠ T360), W354 (≠ Y384), R374 (= R404), G390 (= G420), E403 (= E433), K407 (= K437)
- binding phosphate ion: Y112 (= Y105), D113 (≠ E106), R116 (≠ G109), D344 (≠ H374), R350 (≠ P380)
- binding tryptophan: L34 (= L29), H35 (≠ Q30), S36 (= S31), Y43 (≠ Q38), S44 (≠ A39), R45 (= R40), F46 (= F41), P240 (= P235), F241 (= F236)
6za5B M. Tuberculosis salicylate synthase mbti in complex with salicylate and mg2+ (see paper)
36% identity, 54% coverage: 180:422/449 of query aligns to 172:414/440 of 6za5B
Sites not aligning to the query:
Query Sequence
>N515DRAFT_2823 N515DRAFT_2823 anthranilate synthase component 1
MTSIRRTLHGRRDLLAPAAAFPERYPCLLQSVVRGTPQARFDLLFAFPRDRLTLHADGRV
LDGQGAEHAGGFLHALDAAWQAERLPRDADDGLPFHGGWVLFLAYELAGEIEPRLRLAPH
EVLPVALALRCPAAAIVDHERERTVLIAEPGCEDLLEQMAADLEAQPPIAPLPAPLERDE
DDPQLFRDGVARIHEHLHAGDIFQVNLSRAWRARFADAPTPASLYASLRMANPAPFAGLL
QQPDWAVVSSSPERLVEARGGVAQTRPIAGTRPRTPADDELARIRELRTHPKERAEHVML
IDLERNDLGRVCVPGSVQVDELMVVESYAHVHHIVSNVRGKLRPGVTPGQVIAATFPGGT
ITGCPKVRCMEIIHALEDAPRGAYTGALGYLDRNGDLDLNILIRTLTLAGTQVSLRAGAG
IVADSVAEKELDETRAKARGLLRALGVAD
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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