SitesBLAST
Comparing Synpcc7942_1334 FitnessBrowser__SynE:Synpcc7942_1334 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
37% identity, 95% coverage: 23:465/465 of query aligns to 18:456/459 of 7pi1DDD
- binding magnesium ion: G428 (= G437), E438 (= E447)
- binding tryptophan: L33 (= L37), E34 (≠ D38), S35 (≠ A43), G39 (≠ S47), Y41 (= Y49), P242 (= P250), Y243 (≠ F251), M244 (≠ S252), Q406 (≠ D415), N408 (≠ S417)
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, 95% coverage: 23:465/465 of query aligns to 20:463/470 of P28820
- A283 (≠ K285) 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.
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)
39% identity, 94% coverage: 25:463/465 of query aligns to 22:452/453 of P05041
- S36 (≠ L39) binding
- E258 (= E268) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K285) 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 (= G286) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R322) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R327) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S333) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H350) 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)
38% identity, 94% coverage: 25:463/465 of query aligns to 20:436/437 of 1k0eA
- active site: E256 (= E268), K272 (= K285), E286 (= E313), H323 (= H350), S350 (= S377), W374 (≠ Y401), R394 (= R421), G410 (= G437), E423 (= E450), K427 (= K454)
- binding tryptophan: L32 (= L37), H33 (≠ D38), S34 (≠ L39), Y41 (≠ E46), F44 (≠ Y49), P238 (= P250), F239 (= F251), S240 (= S252)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
36% identity, 94% coverage: 25:463/465 of query aligns to 22:419/420 of 1k0gA
- active site: E258 (= E268), K274 (= K285), E278 (= E313), S333 (= S377), W357 (≠ Y401), R377 (= R421), G393 (= G437), E406 (= E450), K410 (= K454)
- binding phosphate ion: D113 (≠ E106), R116 (≠ A109), D347 (≠ H391), R353 (≠ P397)
- binding tryptophan: L34 (= L37), H35 (≠ D38), S36 (≠ L39), Y43 (≠ E46), S44 (= S47), F46 (≠ Y49), P240 (= P250), F241 (= F251), S242 (= S252)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
36% identity, 94% coverage: 25:462/465 of query aligns to 22:415/415 of 1k0gB
- active site: E258 (= E268), K274 (= K285), E277 (= E313), S330 (= S377), W354 (≠ Y401), R374 (= R421), G390 (= G437), E403 (= E450), K407 (= K454)
- binding phosphate ion: Y112 (= Y105), D113 (≠ E106), R116 (≠ A109), D344 (≠ H391), R350 (≠ P397)
- binding tryptophan: L34 (= L37), H35 (≠ D38), S36 (≠ L39), Y43 (≠ E46), S44 (= S47), R45 (= R48), F46 (≠ Y49), P240 (= P250), F241 (= F251)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 79% coverage: 95:462/465 of query aligns to 263:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I284), K454 (= K285), G455 (= G286), T456 (= T287), M547 (≠ I378), Y570 (= Y401), R590 (= R421), V603 (≠ A434), G604 (= G435), G605 (≠ C436), A606 (≠ G437), E619 (= E450), K623 (= K454)
- binding tryptophan: P419 (= P250), Y420 (≠ F251), G421 (≠ S252), L574 (= L405), G575 (≠ F406)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 80% coverage: 95:465/465 of query aligns to 305:673/673 of 8hx8A
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)
34% identity, 90% coverage: 47:465/465 of query aligns to 62:477/489 of O94582
- S390 (≠ T379) modified: Phosphoserine
- S392 (≠ A381) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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, 98% coverage: 3:460/465 of query aligns to 36:513/524 of A0QX93
- K355 (≠ T302) 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, 99% coverage: 1:460/465 of query aligns to 14:492/505 of 5cwaA
- active site: Q248 (= Q219), E301 (= E268), A317 (≠ K285), E345 (= E313), H382 (= H350), T409 (≠ S377), Y433 (= Y401), R453 (= R421), G469 (= G437), E482 (= E450), K486 (= K454)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y401), I452 (= I420), A466 (= A434), G467 (= G435), K486 (= K454)
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, 80% coverage: 91:462/465 of query aligns to 184:585/595 of P32068
- D341 (= D233) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
35% identity, 84% coverage: 69:460/465 of query aligns to 95:488/499 of 7bvdA
- active site: Q248 (= Q219), E301 (= E268), A317 (≠ K285), E341 (= E313), H378 (= H350), T405 (≠ S377), Y429 (= Y401), R449 (= R421), G465 (= G437), E478 (= E450), K482 (= K454)
- binding pyruvic acid: A100 (= A74)
Sites not aligning to the query:
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
34% identity, 79% coverage: 95:462/465 of query aligns to 171:567/577 of Q94GF1
- D323 (= D233) mutation to N: Insensitive to feedback inhibition by tryptophan.
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, 78% coverage: 101:462/465 of query aligns to 148:510/520 of P00898
- C174 (≠ S128) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ S247) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P248) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S252) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A253) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S264) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ Q354) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G412) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S417) 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, 78% coverage: 101:462/465 of query aligns to 144:506/512 of 1i1qA
- active site: Q259 (= Q219), E305 (= E268), A323 (≠ K285), E357 (= E313), H394 (= H350), T421 (≠ S377), Y445 (= Y401), R465 (= R421), G481 (= G437), E494 (= E450), K498 (= K454)
- binding tryptophan: P287 (= P250), Y288 (≠ F251), M289 (≠ S252), G450 (≠ F406), C461 (≠ S417)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
30% identity, 87% coverage: 58:462/465 of query aligns to 101:501/511 of 1i7sA
- active site: Q254 (= Q219), E300 (= E268), A318 (≠ K285), E352 (= E313), H389 (= H350), T416 (≠ S377), Y440 (= Y401), R460 (= R421), G476 (= G437), E489 (= E450), K493 (= K454)
- binding tryptophan: P282 (= P250), Y283 (≠ F251), M284 (≠ S252), V444 (≠ L405), G445 (≠ F406), D454 (= D415), C456 (≠ S417)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
30% identity, 87% coverage: 58:462/465 of query aligns to 107:507/517 of 1i7qA
- active site: Q260 (= Q219), E306 (= E268), A324 (≠ K285), E358 (= E313), H395 (= H350), T422 (≠ S377), Y446 (= Y401), R466 (= R421), G482 (= G437), E495 (= E450), K499 (= K454)
- binding magnesium ion: E358 (= E313), E495 (= E450)
- binding pyruvic acid: Y446 (= Y401), I465 (= I420), R466 (= R421), A479 (= A434), G480 (= G435), K499 (= K454)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
30% identity, 87% coverage: 58:462/465 of query aligns to 109:509/519 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)
30% identity, 58% coverage: 188:458/465 of query aligns to 137:402/408 of 2fn1A
- active site: K167 (≠ Q219), E214 (= E268), A230 (≠ K285), E258 (= E313), H295 (= H350), T322 (≠ S377), Y346 (= Y401), R365 (= R421), G381 (= G437), E394 (= E450), K398 (= K454)
- binding magnesium ion: E258 (= E313), E394 (= E450)
- binding pyruvic acid: Y346 (= Y401), L364 (≠ I420), R365 (= R421), A378 (= A434), G379 (= G435), K398 (= K454)
Query Sequence
>Synpcc7942_1334 FitnessBrowser__SynE:Synpcc7942_1334
MTAIARRVVQPLVREIAWCDPQQAFAPFAQDPHAVLLDLGEPATPESRYAYLCLSPYATQ
RGDRLVTEADPFQALATSLATVDWQTNSDSDLPPFQGGICGFLSYECGAWLERLPTPKPV
EPRLPLWSLSLYDLVVACDRQQRRTWIFSSGLPLQDPRDRQQRAEQRLQWVCDRLQSALP
SQSPDWQPQADWQALQTEADFCQAVDQVKCHIRAGDIFQANLTTAFRASQPKDLSPWQLY
RRLYQLSPEPFSAYFAGGDFQLLSVSPERFLRLDRDGWVETRPIKGTRPRSADPAHDRQL
ATELQASEKDRAENVMIVDLLRNDLGRVCRPRSIQVPQLCQLESYEHVHHLTSQVIGQLR
SGLTAVDLLRATFPGGSITGAPKIRSMEIIHELEPIPRQAYCGSLFWLGFDGSLDASILI
RTLQISQGQVLAQAGCGIVADSDPLDECAEMQVKVQPLLRSLQPS
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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