SitesBLAST
Comparing 209401 MicrobesOnline__882:209401 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
38% identity, 80% coverage: 96:523/532 of query aligns to 31:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G497), E438 (= E507)
- binding tryptophan: L33 (= L98), E34 (= E99), S35 (= S100), G39 (= G108), Y41 (= Y110), P242 (= P308), Y243 (= Y309), M244 (= M310), Q406 (≠ D475), N408 (≠ G477)
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)
38% identity, 80% coverage: 96:523/532 of query aligns to 33:461/470 of P28820
- A283 (= A342) 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.
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)
39% identity, 91% coverage: 36:518/532 of query aligns to 7:511/524 of A0QX93
- K355 (≠ A359) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
40% identity, 83% coverage: 77:518/532 of query aligns to 30:486/499 of 7bvdA
- active site: Q248 (= Q279), E301 (= E326), A317 (= A342), E341 (= E370), H378 (= H407), T405 (= T434), Y429 (= Y458), R449 (= R481), G465 (= G497), E478 (= E510), K482 (= K514)
- binding pyruvic acid: S93 (≠ F148), G94 (vs. gap), A100 (≠ G151)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
39% identity, 83% coverage: 78:518/532 of query aligns to 31:490/505 of 5cwaA
- active site: Q248 (= Q279), E301 (= E326), A317 (= A342), E345 (= E370), H382 (= H407), T409 (= T434), Y433 (= Y458), R453 (= R481), G469 (= G497), E482 (= E510), K486 (= K514)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y458), I452 (= I480), A466 (= A494), G467 (= G495), K486 (= K514)
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)
34% identity, 86% coverage: 67:523/532 of query aligns to 94:586/595 of P32068
- D341 (= D293) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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)
34% identity, 85% coverage: 74:523/532 of query aligns to 27:475/489 of O94582
- S390 (= S436) modified: Phosphoserine
- S392 (≠ A438) 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)
34% identity, 86% coverage: 67:523/532 of query aligns to 78:568/577 of Q94GF1
- D323 (= D293) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
40% identity, 61% coverage: 203:527/532 of query aligns to 168:511/512 of 1i1qA
- active site: Q259 (= Q279), E305 (= E326), A323 (= A342), E357 (= E370), H394 (= H407), T421 (= T434), Y445 (= Y458), R465 (= R481), G481 (= G497), E494 (= E510), K498 (= K514)
- binding tryptophan: P287 (= P308), Y288 (= Y309), M289 (= M310), G450 (= G463), C461 (≠ G477)
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)
40% identity, 61% coverage: 203:527/532 of query aligns to 172:515/520 of P00898
- C174 (= C205) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N305) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P306) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M310) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F311) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G322) mutation to S: Decrease in feedback control by tryptophan.
- R402 (= R411) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (≠ R469) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ G477) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (= H527) 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)
32% identity, 81% coverage: 95:523/532 of query aligns to 31:452/453 of P05041
- S36 (= S100) binding
- E258 (= E326) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A342) 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 (= G343) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R379) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R384) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T390) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H407) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
44% identity, 51% coverage: 258:527/532 of query aligns to 239:512/517 of 1i7qA
- active site: Q260 (= Q279), E306 (= E326), A324 (= A342), E358 (= E370), H395 (= H407), T422 (= T434), Y446 (= Y458), R466 (= R481), G482 (= G497), E495 (= E510), K499 (= K514)
- binding magnesium ion: E358 (= E370), E495 (= E510)
- binding pyruvic acid: Y446 (= Y458), I465 (= I480), R466 (= R481), A479 (= A494), G480 (= G495), K499 (= K514)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
44% identity, 51% coverage: 258:527/532 of query aligns to 233:506/511 of 1i7sA
- active site: Q254 (= Q279), E300 (= E326), A318 (= A342), E352 (= E370), H389 (= H407), T416 (= T434), Y440 (= Y458), R460 (= R481), G476 (= G497), E489 (= E510), K493 (= K514)
- binding tryptophan: P282 (= P308), Y283 (= Y309), M284 (= M310), V444 (≠ I462), G445 (= G463), D454 (= D475), C456 (≠ G477)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
44% identity, 51% coverage: 258:527/532 of query aligns to 241:514/519 of P00897
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
31% identity, 81% coverage: 95:523/532 of query aligns to 29:436/437 of 1k0eA
- active site: E256 (= E326), K272 (≠ A342), E286 (= E370), H323 (= H407), S350 (≠ T434), W374 (≠ Y458), R394 (= R481), G410 (= G497), E423 (= E510), K427 (= K514)
- binding tryptophan: L32 (= L98), H33 (≠ E99), S34 (= S100), Y41 (≠ W107), F44 (≠ Y110), P238 (= P308), F239 (≠ Y309), S240 (≠ M310)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
35% identity, 69% coverage: 157:524/532 of query aligns to 293:672/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
35% identity, 69% coverage: 157:523/532 of query aligns to 251:632/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I341), K454 (≠ A342), G455 (= G343), T456 (= T344), M547 (≠ V435), Y570 (= Y458), R590 (= R481), V603 (≠ A494), G604 (= G495), G605 (≠ A496), A606 (≠ G497), E619 (= E510), K623 (= K514)
- binding tryptophan: P419 (= P308), Y420 (= Y309), G421 (≠ M310), L574 (≠ I462), G575 (= G463)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 81% coverage: 95:523/532 of query aligns to 31:419/420 of 1k0gA
- active site: E258 (= E326), K274 (= K366), E278 (= E370), S333 (≠ T434), W357 (≠ Y458), R377 (= R481), G393 (= G497), E406 (= E510), K410 (= K514)
- binding phosphate ion: D113 (≠ G184), R116 (≠ G187), D347 (≠ A448), R353 (≠ P454)
- binding tryptophan: L34 (= L98), H35 (≠ E99), S36 (= S100), Y43 (≠ W107), S44 (≠ G108), F46 (≠ Y110), P240 (= P308), F241 (≠ Y309), S242 (≠ M310)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 79% coverage: 95:514/532 of query aligns to 31:407/415 of 1k0gB
- active site: E258 (= E326), K274 (≠ A342), E277 (= E370), S330 (≠ T434), W354 (≠ Y458), R374 (= R481), G390 (= G497), E403 (= E510), K407 (= K514)
- binding phosphate ion: Y112 (= Y183), D113 (≠ G184), R116 (≠ G187), D344 (≠ A448), R350 (≠ P454)
- binding tryptophan: L34 (= L98), H35 (≠ E99), S36 (= S100), Y43 (≠ W107), S44 (≠ G108), R45 (= R109), F46 (≠ Y110), P240 (= P308), F241 (≠ Y309)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
36% identity, 49% coverage: 260:518/532 of query aligns to 148:402/408 of 2fn1A
- active site: K167 (≠ Q279), E214 (= E326), A230 (= A342), E258 (= E370), H295 (= H407), T322 (= T434), Y346 (= Y458), R365 (= R481), G381 (= G497), E394 (= E510), K398 (= K514)
- binding magnesium ion: E258 (= E370), E394 (= E510)
- binding pyruvic acid: Y346 (= Y458), L364 (≠ I480), R365 (= R481), A378 (= A494), G379 (= G495), K398 (= K514)
Query Sequence
>209401 MicrobesOnline__882:209401
MEMDDAKRPAGAKRRTGGEEDAGRVAGHATTQDNAHAMPSTQAGTQAGGAGAHADANPAG
CPDGRIVLRQSCSLLEGDVDTPISLFLGMVGSGQGILLESAEVDGRWGRYSIIGFNFLLR
LGCAAGRLEVAVRDPRLAALKELEGMPFIEGVRAVMRRLTIEPDPDFANQPPITRALYGY
MGYGVAGLLEPKLAPVLRAEAAEACLALPGTVVVFDHLYNRLTMLSLTDRNGLRIDRSVL
DRAPQTPEVGPTRAVPDESAYKRAVERTREMIRQGEAIQVVLSTRFQASFNGDPFTLYRR
LRRINPSPYMFFMRLPGVSLLGSSPEVMVRCSKGRLQVSPIAGTRPRGVDDVEDARLAAE
LLDDPKERAEHVMLVDLGRNDLGRIAAPGTVQVERFMEVEKFSHVMHLTSRVTADLAEGH
DALDVLTATFPAGTVSGAPKVRAMEIIAEAEGQPRGPYAGCIGWFGLDRDSVSLDTGITI
RSMWVREGQVHWQAGAGIVFDSKPAAEWKECCNKAAAMRAALDGGCHVPAHR
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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