SitesBLAST
Comparing WP_086511656.1 NCBI__GCF_002151265.1:WP_086511656.1 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)
48% identity, 95% coverage: 19:453/459 of query aligns to 21:453/453 of P05041
- S36 (= S34) binding
- E258 (= E257) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K274) 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 (= G275) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R311) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R316) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S322) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H339) 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)
47% identity, 95% coverage: 19:453/459 of query aligns to 19:437/437 of 1k0eA
- active site: E256 (= E257), K272 (= K274), E286 (= E302), H323 (= H339), S350 (= S366), W374 (≠ Y390), R394 (= R410), G410 (= G426), E423 (= E439), K427 (= K443)
- binding tryptophan: L32 (= L32), H33 (≠ D33), S34 (= S34), Y41 (≠ G41), F44 (≠ Y44), P238 (= P235), F239 (= F236), S240 (≠ A237)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
44% identity, 95% coverage: 19:453/459 of query aligns to 21:420/420 of 1k0gA
- active site: E258 (= E257), K274 (= K274), E278 (= E302), S333 (= S366), W357 (≠ Y390), R377 (= R410), G393 (= G426), E406 (= E439), K410 (= K443)
- binding phosphate ion: D113 (= D108), R116 (= R111), D347 (= D380), R353 (= R386)
- binding tryptophan: L34 (= L32), H35 (≠ D33), S36 (= S34), Y43 (≠ G41), S44 (≠ G42), F46 (≠ Y44), P240 (= P235), F241 (= F236), S242 (≠ A237)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
44% identity, 94% coverage: 19:451/459 of query aligns to 21:415/415 of 1k0gB
- active site: E258 (= E257), K274 (= K274), E277 (= E302), S330 (= S366), W354 (≠ Y390), R374 (= R410), G390 (= G426), E403 (= E439), K407 (= K443)
- binding phosphate ion: Y112 (= Y107), D113 (= D108), R116 (= R111), D344 (= D380), R350 (= R386)
- binding tryptophan: L34 (= L32), H35 (≠ D33), S36 (= S34), Y43 (≠ G41), S44 (≠ G42), R45 (= R43), F46 (≠ Y44), P240 (= P235), F241 (= F236)
7pi1DDD Aminodeoxychorismate synthase component 1
37% identity, 96% coverage: 10:451/459 of query aligns to 9:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G426), E438 (= E436)
- binding tryptophan: L33 (= L32), E34 (≠ D33), S35 (= S34), G39 (= G42), Y41 (= Y44), P242 (= P235), Y243 (≠ F236), M244 (≠ A237), Q406 (≠ D404), N408 (≠ S406)
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)
36% identity, 96% coverage: 10:451/459 of query aligns to 11:460/470 of P28820
- A283 (≠ K274) 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.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
38% identity, 92% coverage: 32:451/459 of query aligns to 231:670/673 of 8hx8A
- binding magnesium ion: E521 (= E302), E655 (= E436), E658 (= E439)
- binding tryptophan: L231 (= L32), D232 (= D33), S233 (= S34), S241 (≠ G42), F243 (≠ Y44), P458 (= P235), Y459 (≠ F236), G460 (≠ A237), G614 (= G395)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
38% identity, 92% coverage: 32:451/459 of query aligns to 189:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I273), K454 (= K274), G455 (= G275), T456 (= T276), M547 (≠ I367), Y570 (= Y390), R590 (= R410), V603 (≠ G423), G604 (= G424), G605 (= G425), A606 (≠ G426), E619 (= E439), K623 (= K443)
- binding tryptophan: L189 (= L32), D190 (= D33), S191 (= S34), S199 (≠ G42), F201 (≠ Y44), P419 (= P235), Y420 (≠ F236), G421 (≠ A237), L574 (= L394), G575 (= G395)
Sites not aligning to the query:
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, 96% coverage: 10:449/459 of query aligns to 49:513/524 of A0QX93
- K355 (≠ M291) 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)
36% identity, 95% coverage: 14:449/459 of query aligns to 33:492/505 of 5cwaA
- active site: Q248 (= Q206), E301 (= E257), A317 (≠ K274), E345 (= E302), H382 (= H339), T409 (≠ S366), Y433 (= Y390), R453 (= R410), G469 (= G426), E482 (= E439), K486 (= K443)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y390), I452 (= I409), A466 (≠ G423), G467 (= G424), K486 (= K443)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
35% identity, 95% coverage: 14:449/459 of query aligns to 33:488/499 of 7bvdA
- active site: Q248 (= Q206), E301 (= E257), A317 (≠ K274), E341 (= E302), H378 (= H339), T405 (≠ S366), Y429 (= Y390), R449 (= R410), G465 (= G426), E478 (= E439), K482 (= K443)
- binding pyruvic acid: S93 (≠ Q71), G94 (= G72), A100 (= A78)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 92% coverage: 32:451/459 of query aligns to 100:567/577 of Q94GF1
- D323 (= D220) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
31% identity, 95% coverage: 17:451/459 of query aligns to 37:474/489 of O94582
- S390 (≠ T368) modified: Phosphoserine
- S392 (≠ A370) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
30% identity, 92% coverage: 32:451/459 of query aligns to 116:585/595 of P32068
- D341 (= D220) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
32% identity, 82% coverage: 82:459/459 of query aligns to 129:518/520 of P00898
- C174 (= C129) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ T232) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P233) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A237) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ G238) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S253) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ V343) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G401) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S406) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (= H456) 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
31% identity, 82% coverage: 82:456/459 of query aligns to 125:511/512 of 1i1qA
- active site: Q259 (= Q206), E305 (= E257), A323 (≠ K274), E357 (= E302), H394 (= H339), T421 (≠ S366), Y445 (= Y390), R465 (= R410), G481 (= G426), E494 (= E439), K498 (= K443)
- binding tryptophan: P287 (= P235), Y288 (≠ F236), M289 (≠ A237), G450 (= G395), C461 (≠ S406)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
34% identity, 79% coverage: 97:459/459 of query aligns to 136:509/511 of 1i7sA
- active site: Q254 (= Q206), E300 (= E257), A318 (≠ K274), E352 (= E302), H389 (= H339), T416 (≠ S366), Y440 (= Y390), R460 (= R410), G476 (= G426), E489 (= E439), K493 (= K443)
- binding tryptophan: P282 (= P235), Y283 (≠ F236), M284 (≠ A237), V444 (≠ L394), G445 (= G395), D454 (= D404), C456 (≠ S406)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
34% identity, 79% coverage: 97:459/459 of query aligns to 142:515/517 of 1i7qA
- active site: Q260 (= Q206), E306 (= E257), A324 (≠ K274), E358 (= E302), H395 (= H339), T422 (≠ S366), Y446 (= Y390), R466 (= R410), G482 (= G426), E495 (= E439), K499 (= K443)
- binding magnesium ion: E358 (= E302), E495 (= E439)
- binding pyruvic acid: Y446 (= Y390), I465 (= I409), R466 (= R410), A479 (≠ G423), G480 (= G424), K499 (= K443)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
33% identity, 84% coverage: 76:459/459 of query aligns to 123:517/519 of P00897
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
30% identity, 63% coverage: 155:444/459 of query aligns to 143:415/424 of 5jy9B
- active site: K183 (≠ Q206), E230 (= E257), A246 (≠ K274), E274 (= E302), H311 (= H339), T338 (≠ S366), Y362 (= Y390), R381 (= R410), G397 (= G426), E410 (= E439), K414 (= K443)
- binding fe (ii) ion: E274 (= E302), E410 (= E439)
Query Sequence
>WP_086511656.1 NCBI__GCF_002151265.1:WP_086511656.1
MTARLEITPLPYGEDPLAYFQALRQRPGAVLLDSGKPAAPGGRYDIISSDPVSAFTVDGK
GVIRIDGEVQQGRDPFMAQQTLLEGLALDVPSSDLPFLGGLIGYWGYDLGRSLEPVGNSA
QERVCLPACRTGLYDWALIQDHQRQESWLVATAERRLQVMEWLRHSAAPTLPFGLLAPFE
GEMDRDGYARRFAAVQDYIRAGDCYQINLAQRFSAPYSGDLWDAYLRLRLATPTPFAGFM
AWPSERGEQAILSLSPERFLLCESDGHVETRPIKGTRPRGSTPEEDWQLAMELISSLKDR
AENVMIVDLLRNDLGRVCQPGSVRVPQLCGLESYANVHHLVSVVCGRLAAEKRPLDLLAA
AFPGGSITGAPKVRAMQIIDELEPSRRSVYCGSLGFVDVRGNMDTSIAIRTAVADGERIH
LWGGGGLVADSSVEAEYVETLDKIRHLMQALAKPKHQQE
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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