SitesBLAST
Comparing 15930 FitnessBrowser__Keio:15930 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)
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)
100% identity, 100% coverage: 1:453/453 of query aligns to 1:453/453 of P05041
- S36 (= S36) binding
- E258 (= E258) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K274) 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 (= G275) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R311) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R316) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S322) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H339) 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)
97% identity, 100% coverage: 3:453/453 of query aligns to 1:437/437 of 1k0eA
- active site: E256 (= E258), K272 (= K274), E286 (= E302), H323 (= H339), S350 (= S366), W374 (= W390), R394 (= R410), G410 (= G426), E423 (= E439), K427 (= K443)
- binding tryptophan: L32 (= L34), H33 (= H35), S34 (= S36), Y41 (= Y43), F44 (= F46), P238 (= P240), F239 (= F241), S240 (= S242)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
93% identity, 100% coverage: 1:453/453 of query aligns to 1:420/420 of 1k0gA
- active site: E258 (= E258), K274 (= K298), E278 (= E302), S333 (= S366), W357 (= W390), R377 (= R410), G393 (= G426), E406 (= E439), K410 (= K443)
- binding phosphate ion: D113 (= D113), R116 (= R116), D347 (= D380), R353 (= R386)
- binding tryptophan: L34 (= L34), H35 (= H35), S36 (= S36), Y43 (= Y43), S44 (= S44), F46 (= F46), P240 (= P240), F241 (= F241), S242 (= S242)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
92% identity, 100% coverage: 1:451/453 of query aligns to 1:415/415 of 1k0gB
- active site: E258 (= E258), K274 (= K274), E277 (= E302), S330 (= S366), W354 (= W390), R374 (= R410), G390 (= G426), E403 (= E439), K407 (= K443)
- binding phosphate ion: Y112 (= Y112), D113 (= D113), R116 (= R116), D344 (= D380), R350 (= R386)
- binding tryptophan: L34 (= L34), H35 (= H35), S36 (= S36), Y43 (= Y43), S44 (= S44), R45 (= R45), F46 (= F46), P240 (= P240), F241 (= F241)
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: 44:452/453 of query aligns to 41:461/470 of P28820
- A283 (≠ K274) 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
33% identity, 90% coverage: 44:452/453 of query aligns to 39:454/459 of 7pi1DDD
Sites not aligning to the query:
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)
31% identity, 90% coverage: 45:452/453 of query aligns to 127:586/595 of P32068
- D341 (= D225) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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)
33% identity, 95% coverage: 21:449/453 of query aligns to 59:513/524 of A0QX93
- K355 (≠ V291) 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)
33% identity, 95% coverage: 21:449/453 of query aligns to 39:492/505 of 5cwaA
- active site: Q248 (= Q211), E301 (= E258), A317 (≠ K274), E345 (= E302), H382 (= H339), T409 (≠ S366), Y433 (≠ W390), R453 (= R410), G469 (= G426), E482 (= E439), K486 (= K443)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (≠ W390), I452 (= I409), A466 (= A423), G467 (= G424), K486 (= K443)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 90% coverage: 45:452/453 of query aligns to 111:568/577 of Q94GF1
- D323 (= D225) mutation to N: Insensitive to feedback inhibition by tryptophan.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
33% identity, 95% coverage: 21:449/453 of query aligns to 39:488/499 of 7bvdA
- active site: Q248 (= Q211), E301 (= E258), A317 (≠ K274), E341 (= E302), H378 (= H339), T405 (≠ S366), Y429 (≠ W390), R449 (= R410), G465 (= G426), E478 (= E439), K482 (= K443)
- binding pyruvic acid: S93 (≠ T75), G94 (≠ T76), A100 (≠ V82)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
34% identity, 85% coverage: 66:452/453 of query aligns to 268:671/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
33% identity, 85% coverage: 66:452/453 of query aligns to 226:632/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I273), K454 (= K274), G455 (= G275), T456 (= T276), M547 (≠ I367), Y570 (≠ W390), R590 (= R410), V603 (≠ A423), G604 (= G424), G605 (= G425), A606 (≠ G426), E619 (= E439), K623 (= K443)
- binding tryptophan: P419 (= P240), Y420 (≠ F241), G421 (≠ S242), L574 (≠ I394), G575 (= G395)
Sites not aligning to the query:
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, 83% coverage: 78:453/453 of query aligns to 81:476/489 of O94582
- S390 (≠ T368) modified: Phosphoserine
- S392 (≠ A370) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
32% identity, 83% coverage: 78:451/453 of query aligns to 121:506/512 of 1i1qA
- active site: Q259 (= Q211), E305 (= E258), A323 (≠ K274), E357 (= E302), H394 (= H339), T421 (≠ S366), Y445 (≠ W390), R465 (= R410), G481 (= G426), E494 (= E439), K498 (= K443)
- binding tryptophan: P287 (= P240), Y288 (≠ F241), M289 (≠ S242), G450 (= G395), C461 (≠ S406)
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)
32% identity, 83% coverage: 78:451/453 of query aligns to 125:510/520 of P00898
- R128 (≠ Q81) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ A135) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N237) mutation to D: Decrease in feedback control by tryptophan.
- P289 (≠ R238) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S242) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A243) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S254) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T343) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G401) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S406) 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)
32% identity, 76% coverage: 108:451/453 of query aligns to 139:501/511 of 1i7sA
- active site: Q254 (= Q211), E300 (= E258), A318 (≠ K274), E352 (= E302), H389 (= H339), T416 (≠ S366), Y440 (≠ W390), R460 (= R410), G476 (= G426), E489 (= E439), K493 (= K443)
- binding tryptophan: P282 (= P240), Y283 (≠ F241), M284 (≠ S242), V444 (≠ I394), G445 (= G395), D454 (= D404), C456 (≠ S406)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 76% coverage: 108:451/453 of query aligns to 145:507/517 of 1i7qA
- active site: Q260 (= Q211), E306 (= E258), A324 (≠ K274), E358 (= E302), H395 (= H339), T422 (≠ S366), Y446 (≠ W390), R466 (= R410), G482 (= G426), E495 (= E439), K499 (= K443)
- binding magnesium ion: E358 (= E302), E495 (= E439)
- binding pyruvic acid: Y446 (≠ W390), I465 (= I409), R466 (= R410), A479 (= A423), G480 (= G424), K499 (= K443)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
31% identity, 76% coverage: 108:451/453 of query aligns to 147:509/519 of P00897
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)
26% identity, 59% coverage: 186:451/453 of query aligns to 142:406/408 of 2fn1A
- active site: K167 (≠ Q211), E214 (= E258), A230 (≠ K274), E258 (= E302), H295 (= H339), T322 (≠ S366), Y346 (≠ W390), R365 (= R410), G381 (= G426), E394 (= E439), K398 (= K443)
- binding magnesium ion: E258 (= E302), E394 (= E439)
- binding pyruvic acid: Y346 (≠ W390), L364 (≠ I409), R365 (= R410), A378 (= A423), G379 (= G424), K398 (= K443)
Query Sequence
>15930 FitnessBrowser__Keio:15930
MKTLSPAVITLLWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVAEPICTLTTF
GKETVVSESEKRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFES
LPEIAEQDIVLPDMAVGIYDWALIVDHQRHTVSLLSHNDVNARRAWLESQQFSPQEDFTL
TSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAP
FSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAVKLANSAKDR
AENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITAQLPEQLHASDLLRA
AFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIF
CSAGGGIVADSQEEAEYQETFDKVNRILKQLEK
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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