SitesBLAST
Comparing 3608396 FitnessBrowser__Dino:3608396 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)
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)
43% identity, 96% coverage: 1:491/509 of query aligns to 23:511/524 of A0QX93
- K355 (≠ A335) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
39% identity, 96% coverage: 11:498/509 of query aligns to 12:477/489 of O94582
- S390 (= S412) modified: Phosphoserine
- S392 (≠ A414) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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, 92% coverage: 31:496/509 of query aligns to 16:461/470 of P28820
- A283 (= A318) 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
39% identity, 92% coverage: 31:496/509 of query aligns to 14:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G470), E438 (= E480)
- binding tryptophan: L33 (= L50), E34 (= E51), S35 (= S52), G39 (= G56), Y41 (= Y62), P242 (= P284), Y243 (≠ F285), M244 (= M286), Q406 (≠ D448), N408 (≠ C450)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 96% coverage: 1:491/509 of query aligns to 3:486/499 of 7bvdA
- active site: Q248 (= Q255), E301 (= E302), A317 (= A318), E341 (= E346), H378 (= H383), T405 (= T410), Y429 (= Y434), R449 (= R454), G465 (= G470), E478 (= E483), K482 (= K487)
- binding pyruvic acid: S93 (vs. gap), G94 (vs. gap), A100 (= A103)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
43% identity, 92% coverage: 22:491/509 of query aligns to 24:490/505 of 5cwaA
- active site: Q248 (= Q255), E301 (= E302), A317 (= A318), E345 (= E346), H382 (= H383), T409 (= T410), Y433 (= Y434), R453 (= R454), G469 (= G470), E482 (= E483), K486 (= K487)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y434), I452 (≠ L453), A466 (= A467), G467 (= G468), K486 (= K487)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
40% identity, 87% coverage: 47:488/509 of query aligns to 94:560/577 of Q94GF1
- D323 (≠ P269) 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, 92% coverage: 22:488/509 of query aligns to 82:578/595 of P32068
- D341 (≠ P269) 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)
39% identity, 72% coverage: 128:491/509 of query aligns to 144:502/512 of 1i1qA
- active site: Q259 (= Q255), E305 (= E302), A323 (= A318), E357 (= E346), H394 (= H383), T421 (= T410), Y445 (= Y434), R465 (= R454), G481 (= G470), E494 (= E483), K498 (= K487)
- binding tryptophan: P287 (= P284), Y288 (≠ F285), M289 (= M286), G450 (= G439), C461 (= C450)
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)
39% identity, 72% coverage: 128:491/509 of query aligns to 148:506/520 of P00898
- C174 (≠ V155) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N281) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P282) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M286) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F287) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G298) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N387) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G445) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C450) 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.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
34% identity, 90% coverage: 33:491/509 of query aligns to 18:503/517 of 1i7qA
- active site: Q260 (= Q255), E306 (= E302), A324 (= A318), E358 (= E346), H395 (= H383), T422 (= T410), Y446 (= Y434), R466 (= R454), G482 (= G470), E495 (= E483), K499 (= K487)
- binding magnesium ion: E358 (= E346), E495 (= E483)
- binding pyruvic acid: Y446 (= Y434), I465 (≠ L453), R466 (= R454), A479 (= A467), G480 (= G468), K499 (= K487)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
38% identity, 76% coverage: 103:491/509 of query aligns to 117:497/511 of 1i7sA
- active site: Q254 (= Q255), E300 (= E302), A318 (= A318), E352 (= E346), H389 (= H383), T416 (= T410), Y440 (= Y434), R460 (= R454), G476 (= G470), E489 (= E483), K493 (= K487)
- binding tryptophan: P282 (= P284), Y283 (≠ F285), M284 (= M286), V444 (≠ C438), G445 (= G439), D454 (= D448), C456 (= C450)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
34% identity, 90% coverage: 33:491/509 of query aligns to 20:505/519 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)
33% identity, 77% coverage: 99:491/509 of query aligns to 78:447/453 of P05041
- E258 (= E302) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A318) 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 (= G319) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R355) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R360) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T366) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H383) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 77% coverage: 99:491/509 of query aligns to 76:431/437 of 1k0eA
- active site: E256 (= E302), K272 (≠ A318), E286 (= E346), H323 (= H383), S350 (≠ T410), W374 (≠ Y434), R394 (= R454), G410 (= G470), E423 (= E483), K427 (= K487)
- binding tryptophan: P238 (= P284), F239 (= F285), S240 (≠ M286)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 77% coverage: 99:491/509 of query aligns to 78:414/420 of 1k0gA
- active site: E258 (= E302), K274 (= K342), E278 (= E346), S333 (≠ T410), W357 (≠ Y434), R377 (= R454), G393 (= G470), E406 (= E483), K410 (= K487)
- binding phosphate ion: D113 (= D133), R116 (= R136), D347 (= D424), R353 (≠ K430)
- binding tryptophan: P240 (= P284), F241 (= F285), S242 (≠ M286)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
34% identity, 77% coverage: 104:494/509 of query aligns to 244:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I317), K454 (≠ A318), G455 (= G319), T456 (= T320), M547 (≠ V411), Y570 (= Y434), R590 (= R454), V603 (≠ A467), G604 (= G468), G605 (= G469), A606 (≠ G470), E619 (= E483), K623 (= K487)
- binding tryptophan: P419 (= P284), Y420 (≠ F285), G421 (≠ M286), L574 (≠ C438), G575 (= G439)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 77% coverage: 99:491/509 of query aligns to 78:411/415 of 1k0gB
- active site: E258 (= E302), K274 (≠ A318), E277 (= E346), S330 (≠ T410), W354 (≠ Y434), R374 (= R454), G390 (= G470), E403 (= E483), K407 (= K487)
- binding phosphate ion: Y112 (= Y132), D113 (= D133), R116 (= R136), D344 (= D424), R350 (≠ K430)
- binding tryptophan: P240 (= P284), F241 (= F285)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
38% identity, 51% coverage: 237:494/509 of query aligns to 411:669/673 of 8hx8A
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)
33% identity, 50% coverage: 237:491/509 of query aligns to 149:402/408 of 2fn1A
- active site: K167 (≠ Q255), E214 (= E302), A230 (= A318), E258 (= E346), H295 (= H383), T322 (= T410), Y346 (= Y434), R365 (= R454), G381 (= G470), E394 (= E483), K398 (= K487)
- binding magnesium ion: E258 (= E346), E394 (= E483)
- binding pyruvic acid: Y346 (= Y434), L364 (= L453), R365 (= R454), A378 (= A467), G379 (= G468), K398 (= K487)
Query Sequence
>3608396 FitnessBrowser__Dino:3608396
MALTPSFDAFEAAHGRGENQVVYTRLAADLDTPVSLMLKLAGARKDSFMLESVTGGEVRG
RYSVVGLKPDLIWECRGTGARINRSARFDAEAFEDIPGDPLAALRALIAESRIEMPDELP
AIAAGLFGYLGYDMIRLVEHLPNVNPDPLGLPDAVLVRPSVVAVLDGVKGEVTVVSPVWA
NGSAGGGQSARAAYAQAAERVMDAVRDLERSAMAERRDLGEAAELGEPVSNFAHADYLAA
VERAKDYIRAGDIFQVVPSQRWSQAFPLPPFALYRSLRRTNPSPFMFYFNFGGFQIVGAS
PEILVRVFGREVTIRPIAGTRPRGATPAEDDALEADLLADAKECAEHLMLLDLGRNDVGR
VAKIGTVRPTEQFIIERYSHVMHIVSNVVGELSEEHDALSALLAGLPAGTVSGAPKVRAM
EIIDELEPEKRGVYGGGCGYFAANGDMDMCIALRTAVVKDETLYIQAGGGVVYDSDPEAE
FQETVNKAKAIRMAAQQAGLFAGPAGRNG
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