SitesBLAST
Comparing 5209798 FitnessBrowser__PV4:5209798 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)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
56% identity, 96% coverage: 18:511/517 of query aligns to 17:510/520 of P00898
- E39 (= E40) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S41) binding ; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (= A42) mutation to V: Decrease in feedback control by tryptophan.
- K50 (= K51) binding
- R128 (= R128) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ L176) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N289) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P290) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M294) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F295) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G306) mutation to S: Decrease in feedback control by tryptophan.
- R402 (= R403) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G461) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C466) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
Sites not aligning to the query:
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
55% identity, 96% coverage: 18:511/517 of query aligns to 13:506/512 of 1i1qA
- active site: Q259 (= Q264), E305 (= E310), A323 (= A328), E357 (= E362), H394 (= H399), T421 (= T426), Y445 (= Y450), R465 (= R470), G481 (= G486), E494 (= E499), K498 (= K503)
- binding tryptophan: L34 (= L39), E35 (= E40), S36 (= S41), K46 (= K51), P287 (= P292), Y288 (= Y293), M289 (= M294), G450 (= G455), C461 (= C466)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
53% identity, 97% coverage: 12:511/517 of query aligns to 8:507/517 of 1i7qA
- active site: Q260 (= Q264), E306 (= E310), A324 (= A328), E358 (= E362), H395 (= H399), T422 (= T426), Y446 (= Y450), R466 (= R470), G482 (= G486), E495 (= E499), K499 (= K503)
- binding magnesium ion: E358 (= E362), E495 (= E499)
- binding pyruvic acid: Y446 (= Y450), I465 (= I469), R466 (= R470), A479 (= A483), G480 (= G484), K499 (= K503)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
53% identity, 97% coverage: 12:511/517 of query aligns to 10:509/519 of P00897
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
53% identity, 97% coverage: 12:511/517 of query aligns to 8:501/511 of 1i7sA
- active site: Q254 (= Q264), E300 (= E310), A318 (= A328), E352 (= E362), H389 (= H399), T416 (= T426), Y440 (= Y450), R460 (= R470), G476 (= G486), E489 (= E499), K493 (= K503)
- binding tryptophan: L35 (= L39), E36 (= E40), S37 (= S41), P282 (= P292), Y283 (= Y293), M284 (= M294), V444 (= V454), G445 (= G455), D454 (= D464), C456 (= C466)
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, 76% coverage: 121:512/517 of query aligns to 80:475/489 of O94582
- S390 (≠ T428) modified: Phosphoserine
- S392 (≠ A430) 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)
36% identity, 97% coverage: 9:509/517 of query aligns to 42:513/524 of A0QX93
- K355 (≠ L351) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 97% coverage: 9:509/517 of query aligns to 22:488/499 of 7bvdA
- active site: Q248 (= Q264), E301 (= E310), A317 (= A328), E341 (= E362), H378 (= H399), T405 (= T426), Y429 (= Y450), R449 (= R470), G465 (= G486), E478 (= E499), K482 (= K503)
- binding pyruvic acid: S93 (≠ F89), G94 (= G90), A100 (≠ G126)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
35% identity, 95% coverage: 20:509/517 of query aligns to 33:492/505 of 5cwaA
- active site: Q248 (= Q264), E301 (= E310), A317 (= A328), E345 (= E362), H382 (= H399), T409 (= T426), Y433 (= Y450), R453 (= R470), G469 (= G486), E482 (= E499), K486 (= K503)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y450), I452 (= I469), A466 (= A483), G467 (= G484), K486 (= K503)
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)
36% identity, 71% coverage: 146:514/517 of query aligns to 189:588/595 of P32068
- D341 (≠ L273) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7pi1DDD Aminodeoxychorismate synthase component 1
33% identity, 96% coverage: 20:513/517 of query aligns to 14:455/459 of 7pi1DDD
- binding magnesium ion: G428 (= G486), E438 (= E496)
- binding tryptophan: L33 (= L39), E34 (= E40), S35 (= S41), G39 (≠ E65), Y41 (= Y67), P242 (= P292), Y243 (= Y293), M244 (= M294), Q406 (≠ D464), N408 (≠ C466)
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)
33% identity, 96% coverage: 20:513/517 of query aligns to 16:462/470 of P28820
- A283 (= A328) 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.
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
34% identity, 76% coverage: 123:514/517 of query aligns to 148:570/577 of Q94GF1
- D323 (≠ N277) mutation to N: Insensitive to feedback inhibition 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)
29% identity, 79% coverage: 107:512/517 of query aligns to 62:452/453 of P05041
- E258 (= E310) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A328) 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 (= G329) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R371) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R376) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T382) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H399) 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)
28% identity, 79% coverage: 107:512/517 of query aligns to 60:436/437 of 1k0eA
- active site: E256 (= E310), K272 (≠ A328), E286 (= E362), H323 (= H399), S350 (≠ T426), W374 (≠ Y450), R394 (= R470), G410 (= G486), E423 (= E499), K427 (= K503)
- binding tryptophan: P238 (= P292), F239 (≠ Y293), S240 (≠ M294)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
27% identity, 79% coverage: 107:512/517 of query aligns to 62:419/420 of 1k0gA
- active site: E258 (= E310), K274 (= K358), E278 (= E362), S333 (≠ T426), W357 (≠ Y450), R377 (= R470), G393 (= G486), E406 (= E499), K410 (= K503)
- binding phosphate ion: D113 (= D154), R116 (≠ D157), D347 (≠ R440), R353 (= R446)
- binding tryptophan: P240 (= P292), F241 (≠ Y293), S242 (≠ M294)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
27% identity, 78% coverage: 107:511/517 of query aligns to 62:415/415 of 1k0gB
- active site: E258 (= E310), K274 (≠ A328), E277 (= E362), S330 (≠ T426), W354 (≠ Y450), R374 (= R470), G390 (= G486), E403 (= E499), K407 (= K503)
- binding phosphate ion: Y112 (≠ F153), D113 (= D154), R116 (≠ D157), D344 (≠ R440), R350 (= R446)
- binding tryptophan: P240 (= P292), F241 (≠ Y293)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
30% identity, 66% coverage: 173:511/517 of query aligns to 290:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I327), K454 (≠ A328), G455 (= G329), T456 (= T330), M547 (≠ L427), Y570 (= Y450), R590 (= R470), V603 (≠ A483), G604 (= G484), G605 (≠ A485), A606 (≠ G486), E619 (= E499), K623 (= K503)
- binding tryptophan: P419 (= P292), Y420 (= Y293), G421 (≠ M294), L574 (≠ V454), G575 (= G455)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
30% identity, 66% coverage: 173:511/517 of query aligns to 332:670/673 of 8hx8A
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
31% identity, 56% coverage: 221:507/517 of query aligns to 142:418/424 of 5jy9B
- active site: K183 (≠ Q264), E230 (= E310), A246 (= A328), E274 (= E362), H311 (= H399), T338 (= T426), Y362 (= Y450), R381 (= R470), G397 (= G486), E410 (= E499), K414 (= K503)
- binding fe (ii) ion: E274 (= E362), E410 (= E499)
Query Sequence
>5209798 FitnessBrowser__PV4:5209798
MGQEFLASVNTIKERITYHDDPLQLYQHLTQDAAHTMLLESAEIDSKDHLKSIIMTHAAL
AIRCEGYQLSFTALSDNGQALLVPIACFFGEDENLVDGKALTLGLQKDTSLLDEDARLKS
TSPLDGLRSLIKHIDMGDDAQFESLFLGGVLAFDLIDTVEPLPKVSQSANTCPDYLFYLA
ETLILVDHQARSADIISHNFTQQAEVKAALAERVTQLHQACSSLPDIAPLCPVDAETQVN
VSDDEFKNIVTDLKSHIVAGDIFQVVPSRSFSLPCPNALGAYRALRLTNPSPYMFYFRGD
DFTLFGASPESALKYEASTNQVEIYPIAGTRKRGKTASGEIDFDLDSRIELELRLDKKEL
SEHLMLVDLARNDVARISQSGTRKVAELLKVDRYSHVMHLVSRVTGQLRSDLDALHAYQA
CMNMGTLTGAPKVSAAQLIRGAEKTRRGSYGGAVGYLNGLGDMDTCIVIRSAFVKEGTAH
IQAGAGVVYDSDPQAEADETRQKAQAVISAIKMGGGQ
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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