SitesBLAST
Comparing BWI76_RS17865 FitnessBrowser__Koxy:BWI76_RS17865 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)
76% identity, 100% coverage: 2:451/451 of query aligns to 4:453/453 of P05041
- S36 (= S34) binding
- E258 (= E256) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K272) 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 (= G273) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R309) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R314) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S320) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H337) 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)
74% identity, 100% coverage: 2:451/451 of query aligns to 2:437/437 of 1k0eA
- active site: E256 (= E256), K272 (= K272), E286 (= E300), H323 (= H337), S350 (= S364), W374 (= W388), R394 (= R408), G410 (= G424), E423 (= E437), K427 (= K441)
- binding tryptophan: L32 (= L32), H33 (= H33), S34 (= S34), Y41 (≠ H41), F44 (= F44), P238 (= P238), F239 (= F239), S240 (= S240)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
70% identity, 100% coverage: 2:451/451 of query aligns to 4:420/420 of 1k0gA
- active site: E258 (= E256), K274 (= K296), E278 (= E300), S333 (= S364), W357 (= W388), R377 (= R408), G393 (= G424), E406 (= E437), K410 (= K441)
- binding phosphate ion: D113 (= D111), R116 (= R114), D347 (= D378), R353 (= R384)
- binding tryptophan: L34 (= L32), H35 (= H33), S36 (= S34), Y43 (≠ H41), S44 (≠ N42), F46 (= F44), P240 (= P238), F241 (= F239), S242 (= S240)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
69% identity, 99% coverage: 2:449/451 of query aligns to 4:415/415 of 1k0gB
- active site: E258 (= E256), K274 (= K272), E277 (= E300), S330 (= S364), W354 (= W388), R374 (= R408), G390 (= G424), E403 (= E437), K407 (= K441)
- binding phosphate ion: Y112 (= Y110), D113 (= D111), R116 (= R114), D344 (= D378), R350 (= R384)
- binding tryptophan: L34 (= L32), H35 (= H33), S36 (= S34), Y43 (≠ H41), S44 (≠ N42), R45 (= R43), F46 (= F44), P240 (= P238), F241 (= F239)
7pi1DDD Aminodeoxychorismate synthase component 1
34% identity, 99% coverage: 4:450/451 of query aligns to 4:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G424), E438 (= E434)
- binding tryptophan: L33 (= L32), E34 (≠ H33), S35 (= S34), G39 (≠ N42), Y41 (≠ F44), P242 (= P238), Y243 (≠ F239), M244 (≠ S240), Q406 (≠ D402), N408 (≠ S404)
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)
34% identity, 99% coverage: 4:450/451 of query aligns to 6:461/470 of P28820
- A283 (≠ K272) 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.
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)
33% identity, 88% coverage: 43:441/451 of query aligns to 127:577/595 of P32068
- D341 (= D223) 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)
33% identity, 88% coverage: 43:441/451 of query aligns to 111:559/577 of Q94GF1
- D323 (= D223) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
34% identity, 95% coverage: 19:447/451 of query aligns to 59:513/524 of A0QX93
- K355 (≠ Q289) 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, 95% coverage: 19:447/451 of query aligns to 39:492/505 of 5cwaA
- active site: Q248 (= Q209), E301 (= E256), A317 (≠ K272), E345 (= E300), H382 (= H337), T409 (≠ S364), Y433 (≠ W388), R453 (= R408), G469 (= G424), E482 (= E437), K486 (= K441)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (≠ W388), I452 (= I407), A466 (= A421), G467 (= G422), K486 (= K441)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
34% identity, 95% coverage: 19:447/451 of query aligns to 39:488/499 of 7bvdA
- active site: Q248 (= Q209), E301 (= E256), A317 (≠ K272), E341 (= E300), H378 (= H337), T405 (≠ S364), Y429 (≠ W388), R449 (= R408), G465 (= G424), E478 (= E437), K482 (= K441)
- binding pyruvic acid: S93 (= S73), G94 (≠ A74), A100 (≠ L80)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
35% identity, 88% coverage: 56:451/451 of query aligns to 261:672/673 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, 88% coverage: 56:450/451 of query aligns to 219:632/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I271), K454 (= K272), G455 (= G273), T456 (= T274), M547 (≠ I365), Y570 (≠ W388), R590 (= R408), V603 (≠ A421), G604 (= G422), G605 (= G423), A606 (≠ G424), E619 (= E437), K623 (= K441)
- binding tryptophan: P419 (= P238), Y420 (≠ F239), G421 (≠ S240), L574 (≠ I392), G575 (= G393)
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, 84% coverage: 70:450/451 of query aligns to 75:475/489 of O94582
- S390 (≠ T366) modified: Phosphoserine
- S392 (≠ A368) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
33% identity, 77% coverage: 106:451/451 of query aligns to 148:512/520 of P00898
- C174 (≠ A133) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N235) mutation to D: Decrease in feedback control by tryptophan.
- P289 (≠ R236) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S240) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A241) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S252) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T341) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G399) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S404) 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
33% identity, 77% coverage: 106:451/451 of query aligns to 144:508/512 of 1i1qA
- active site: Q259 (= Q209), E305 (= E256), A323 (≠ K272), E357 (= E300), H394 (= H337), T421 (≠ S364), Y445 (≠ W388), R465 (= R408), G481 (= G424), E494 (= E437), K498 (= K441)
- binding tryptophan: P287 (= P238), Y288 (≠ F239), M289 (≠ S240), G450 (= G393), C461 (≠ S404)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 77% coverage: 106:451/451 of query aligns to 145:509/517 of 1i7qA
- active site: Q260 (= Q209), E306 (= E256), A324 (≠ K272), E358 (= E300), H395 (= H337), T422 (≠ S364), Y446 (≠ W388), R466 (= R408), G482 (= G424), E495 (= E437), K499 (= K441)
- binding magnesium ion: E358 (= E300), E495 (= E437)
- binding pyruvic acid: Y446 (≠ W388), I465 (= I407), R466 (= R408), A479 (= A421), G480 (= G422), K499 (= K441)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
32% identity, 77% coverage: 106:451/451 of query aligns to 139:503/511 of 1i7sA
- active site: Q254 (= Q209), E300 (= E256), A318 (≠ K272), E352 (= E300), H389 (= H337), T416 (≠ S364), Y440 (≠ W388), R460 (= R408), G476 (= G424), E489 (= E437), K493 (= K441)
- binding tryptophan: P282 (= P238), Y283 (≠ F239), M284 (≠ S240), V444 (≠ I392), G445 (= G393), D454 (= D402), C456 (≠ S404)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
32% identity, 76% coverage: 106:446/451 of query aligns to 147:506/519 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, 68% coverage: 138:445/451 of query aligns to 110:402/408 of 2fn1A
- active site: K167 (≠ Q209), E214 (= E256), A230 (≠ K272), E258 (= E300), H295 (= H337), T322 (≠ S364), Y346 (≠ W388), R365 (= R408), G381 (= G424), E394 (= E437), K398 (= K441)
- binding magnesium ion: E258 (= E300), E394 (= E437)
- binding pyruvic acid: Y346 (≠ W388), L364 (≠ I407), R365 (= R408), A378 (= A421), G379 (= G422), K398 (= K441)
Query Sequence
>BWI76_RS17865 FitnessBrowser__Koxy:BWI76_RS17865
MLSPAMLSLPWRPDAAEDYFSPLSSQPWAMLLHSGFAEHPHNRFDIVVAQPRATLVTRGN
MTVINDGETVSTSAADPLTLVHQQLARFNLQPQAHPQLPFLGGALGLFGYDLGRRFENLP
AQAEADIDLPDMAVGIYDWALIVDHQRREVSLFSYGDPQARLAWLEAQAEPAAAPFALTS
GWRSNMSRAEYGEKFRQVQAYLHSGDCYQVNLAQRFTASYRGDEWLAFRQLNRVNRAPFS
AFIRLQEGAILSLSPERFIQLRQGEIQTRPIKGTLPRLADPEQDALQAQKLANSAKDRAE
NLMIVDLMRNDIGRVAVPGSVRVPELFVVEPFPAVHHLVSTVTARLPAHLHAADLLRAAF
PGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTACRGRIYCS
AGGGIVADSEEAAEYQETFDKVNRILHQLES
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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