SitesBLAST
Comparing GFF3583 FitnessBrowser__psRCH2:GFF3583 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)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
44% identity, 98% coverage: 3:488/494 of query aligns to 47:571/577 of Q94GF1
- D323 (≠ A258) 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)
45% identity, 97% coverage: 2:481/494 of query aligns to 28:512/524 of A0QX93
- K355 (≠ Q324) 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)
45% identity, 97% coverage: 2:481/494 of query aligns to 8:491/505 of 5cwaA
- active site: Q248 (= Q244), E301 (= E291), A317 (= A307), E345 (= E335), H382 (= H372), T409 (= T399), Y433 (= Y423), R453 (= R443), G469 (= G459), E482 (= E472), K486 (= K476)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y423), I452 (= I442), A466 (= A456), G467 (= G457), K486 (= K476)
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)
41% identity, 97% coverage: 11:489/494 of query aligns to 14:479/489 of O94582
- S390 (= S401) modified: Phosphoserine
- S392 (≠ A403) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
44% identity, 97% coverage: 2:481/494 of query aligns to 8:487/499 of 7bvdA
- active site: Q248 (= Q244), E301 (= E291), A317 (= A307), E341 (= E335), H378 (= H372), T405 (= T399), Y429 (= Y423), R449 (= R443), G465 (= G459), E478 (= E472), K482 (= K476)
- binding pyruvic acid: S93 (≠ E89), G94 (≠ V90), A100 (≠ F96)
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)
41% identity, 97% coverage: 10:488/494 of query aligns to 73:589/595 of P32068
- D341 (≠ A258) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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)
39% identity, 94% coverage: 28:492/494 of query aligns to 16:468/470 of P28820
- A283 (= A307) 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, 94% coverage: 28:490/494 of query aligns to 14:459/459 of 7pi1DDD
- binding magnesium ion: G428 (= G459), E438 (= E469)
- binding tryptophan: L33 (= L46), E34 (= E47), S35 (= S48), G39 (= G52), Y41 (= Y58), P242 (= P273), Y243 (= Y274), M244 (= M275), Q406 (≠ D437), N408 (≠ A439)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
39% identity, 76% coverage: 119:492/494 of query aligns to 137:509/511 of 1i7sA
- active site: Q254 (= Q244), E300 (= E291), A318 (= A307), E352 (= E335), H389 (= H372), T416 (= T399), Y440 (= Y423), R460 (= R443), G476 (= G459), E489 (= E472), K493 (= K476)
- binding tryptophan: P282 (= P273), Y283 (= Y274), M284 (= M275), V444 (= V427), G445 (= G428), D454 (= D437), C456 (≠ A439)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
39% identity, 76% coverage: 119:492/494 of query aligns to 143:515/517 of 1i7qA
- active site: Q260 (= Q244), E306 (= E291), A324 (= A307), E358 (= E335), H395 (= H372), T422 (= T399), Y446 (= Y423), R466 (= R443), G482 (= G459), E495 (= E472), K499 (= K476)
- binding magnesium ion: E358 (= E335), E495 (= E472)
- binding pyruvic acid: Y446 (= Y423), I465 (= I442), R466 (= R443), A479 (= A456), G480 (= G457), K499 (= K476)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
38% identity, 76% coverage: 119:492/494 of query aligns to 145:517/519 of P00897
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)
38% identity, 77% coverage: 115:492/494 of query aligns to 145:518/520 of P00898
- C174 (≠ L150) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N270) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P271) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M275) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y276) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G287) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N376) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G434) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A439) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (≠ R489) mutation to Y: Almost no change in feedback control by tryptophan.
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.
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)
34% identity, 90% coverage: 34:476/494 of query aligns to 22:443/453 of P05041
- S36 (= S48) binding
- E258 (= E291) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A307) 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 (= G308) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R344) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R349) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T355) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H372) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
38% identity, 76% coverage: 115:489/494 of query aligns to 141:511/512 of 1i1qA
- active site: Q259 (= Q244), E305 (= E291), A323 (= A307), E357 (= E335), H394 (= H372), T421 (= T399), Y445 (= Y423), R465 (= R443), G481 (= G459), E494 (= E472), K498 (= K476)
- binding tryptophan: P287 (= P273), Y288 (= Y274), M289 (= M275), G450 (= G428), C461 (≠ A439)
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
34% identity, 90% coverage: 34:476/494 of query aligns to 20:427/437 of 1k0eA
- active site: E256 (= E291), K272 (≠ A307), E286 (= E335), H323 (= H372), S350 (≠ T399), W374 (≠ Y423), R394 (= R443), G410 (= G459), E423 (= E472), K427 (= K476)
- binding tryptophan: L32 (= L46), H33 (≠ E47), S34 (= S48), Y41 (≠ W55), F44 (≠ Y58), P238 (= P273), F239 (≠ Y274), S240 (≠ M275)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 90% coverage: 34:476/494 of query aligns to 22:410/420 of 1k0gA
- active site: E258 (= E291), K274 (= K331), E278 (= E335), S333 (≠ T399), W357 (≠ Y423), R377 (= R443), G393 (= G459), E406 (= E472), K410 (= K476)
- binding phosphate ion: D113 (= D126), R116 (= R129), D347 (= D413), R353 (≠ K419)
- binding tryptophan: L34 (= L46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), F46 (≠ Y58), P240 (= P273), F241 (≠ Y274), S242 (≠ M275)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 90% coverage: 34:476/494 of query aligns to 22:407/415 of 1k0gB
- active site: E258 (= E291), K274 (≠ A307), E277 (= E335), S330 (≠ T399), W354 (≠ Y423), R374 (= R443), G390 (= G459), E403 (= E472), K407 (= K476)
- binding phosphate ion: Y112 (= Y125), D113 (= D126), R116 (= R129), D344 (= D413), R350 (≠ K419)
- binding tryptophan: L34 (= L46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), R45 (= R57), F46 (≠ Y58), P240 (= P273), F241 (≠ Y274)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 90% coverage: 42:484/494 of query aligns to 185:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I306), K454 (≠ A307), G455 (= G308), T456 (= T309), M547 (≠ L400), Y570 (= Y423), R590 (= R443), V603 (≠ A456), G604 (= G457), G605 (≠ A458), A606 (≠ G459), E619 (= E472), K623 (= K476)
- binding tryptophan: L189 (= L46), D190 (≠ E47), S191 (= S48), S199 (≠ G56), F201 (≠ Y58), P419 (= P273), Y420 (= Y274), G421 (≠ M275), L574 (≠ V427), G575 (= G428)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
33% identity, 90% coverage: 42:484/494 of query aligns to 227:670/673 of 8hx8A
- binding magnesium ion: E521 (= E335), E655 (= E469), E658 (= E472)
- binding tryptophan: L231 (= L46), D232 (≠ E47), S233 (= S48), S241 (≠ G56), F243 (≠ Y58), P458 (= P273), Y459 (= Y274), G460 (≠ M275), G614 (= G428)
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)
31% identity, 60% coverage: 180:476/494 of query aligns to 105:398/408 of 2fn1A
- active site: K167 (≠ Q244), E214 (= E291), A230 (= A307), E258 (= E335), H295 (= H372), T322 (= T399), Y346 (= Y423), R365 (= R443), G381 (= G459), E394 (= E472), K398 (= K476)
- binding magnesium ion: E258 (= E335), E394 (= E472)
- binding pyruvic acid: Y346 (= Y423), L364 (≠ I442), R365 (= R443), A378 (= A456), G379 (= G457), K398 (= K476)
Query Sequence
>GFF3583 FitnessBrowser__psRCH2:GFF3583
MTREEFLRLAAEGHNRIPLSFETLADFDTPLSLYLKLADAPNSYLLESVQGGEKWGRYSI
IGLPCRTVLRVRDHRISVTTDGIETEACEVEDPLAFVESFQQRYRVAPVEGLPRFNGGLV
GYFGYDSVRYVERKLGNCPNPDPLGTPDILLMVSDAVVVFDNLAGKLHCIVLVDPSQPEA
YEAGQARLQALRAKLRQSITPRLGLDFEKSNGAEPTFRSSFSREDYEQAVNRIKDYILAG
DCMQVVISQRMSIPFKAAPIDLYRALRCFNPTPYMYFFNFGDFHVVGSSPEVLVRVEEGL
VTVRPIAGTRPRGASEEADLALEQDLLSDAKELAEHLMLIDLGRNDVGRVAETGTVRLTE
KMVIERYSNVMHIVSNVTGQLKAPLTAMDALRAILPAGTLSGAPKIRAMEIIDELEPVKR
GVYGGAVGYLAWNGNMDTAIAIRTAVIKDGELHVQAGAGIVADSQPALEWEETLNKRRAM
FRAVALAERDQQEN
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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