SitesBLAST
Comparing PP_2329 FitnessBrowser__Putida:PP_2329 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)
45% identity, 96% coverage: 18:444/446 of query aligns to 21:452/453 of P05041
- S36 (= S33) binding
- E258 (= E250) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K266) 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 (= G267) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R303) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R308) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S314) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H331) 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)
44% identity, 96% coverage: 18:444/446 of query aligns to 19:436/437 of 1k0eA
- active site: E256 (= E250), K272 (= K266), E286 (= E294), H323 (= H331), S350 (= S358), W374 (≠ Y382), R394 (= R402), G410 (≠ A418), E423 (= E431), K427 (= K435)
- binding tryptophan: L32 (= L31), H33 (≠ D32), S34 (= S33), Y41 (≠ R40), F44 (= F43), P238 (= P231), F239 (= F232), S240 (= S233)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
42% identity, 96% coverage: 18:444/446 of query aligns to 21:419/420 of 1k0gA
- active site: E258 (= E250), K274 (= K266), E278 (= E294), S333 (= S358), W357 (≠ Y382), R377 (= R402), G393 (≠ A418), E406 (= E431), K410 (= K435)
- binding phosphate ion: D113 (= D100), R116 (= R103), D347 (= D372), R353 (= R378)
- binding tryptophan: L34 (= L31), H35 (≠ D32), S36 (= S33), Y43 (≠ R40), S44 (≠ G41), F46 (= F43), P240 (= P231), F241 (= F232), S242 (= S233)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
41% identity, 96% coverage: 18:443/446 of query aligns to 21:415/415 of 1k0gB
- active site: E258 (= E250), K274 (= K266), E277 (= E294), S330 (= S358), W354 (≠ Y382), R374 (= R402), G390 (≠ A418), E403 (= E431), K407 (= K435)
- binding phosphate ion: Y112 (= Y99), D113 (= D100), R116 (= R103), D344 (= D372), R350 (= R378)
- binding tryptophan: L34 (= L31), H35 (≠ D32), S36 (= S33), Y43 (≠ R40), S44 (≠ G41), R45 (= R42), F46 (= F43), P240 (= P231), F241 (= F232)
7pi1DDD Aminodeoxychorismate synthase component 1
34% identity, 98% coverage: 9:444/446 of query aligns to 9:454/459 of 7pi1DDD
- binding magnesium ion: G428 (≠ A418), E438 (= E428)
- binding tryptophan: L33 (= L31), E34 (≠ D32), S35 (= S33), G39 (= G37), Y41 (≠ F43), P242 (= P231), Y243 (≠ F232), M244 (≠ S233), Q406 (≠ D396), N408 (≠ S398)
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)
34% identity, 98% coverage: 9:444/446 of query aligns to 11:461/470 of P28820
- A283 (≠ K266) 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)
36% identity, 96% coverage: 16:441/446 of query aligns to 57:513/524 of A0QX93
- K355 (≠ Q283) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
39% identity, 79% coverage: 88:441/446 of query aligns to 118:488/499 of 7bvdA
- active site: Q248 (= Q202), E301 (= E250), A317 (≠ K266), E341 (= E294), H378 (= H331), T405 (≠ S358), Y429 (= Y382), R449 (= R402), G465 (≠ A418), E478 (= E431), K482 (= K435)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
35% identity, 96% coverage: 16:441/446 of query aligns to 37:492/505 of 5cwaA
- active site: Q248 (= Q202), E301 (= E250), A317 (≠ K266), E345 (= E294), H382 (= H331), T409 (≠ S358), Y433 (= Y382), R453 (= R402), G469 (≠ A418), E482 (= E431), K486 (= K435)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y382), I452 (= I401), A466 (≠ G415), G467 (= G416), K486 (= K435)
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)
32% identity, 92% coverage: 23:431/446 of query aligns to 106:573/595 of P32068
- D341 (= D216) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 83% coverage: 75:445/446 of query aligns to 289:672/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 83% coverage: 75:443/446 of query aligns to 247:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I265), K454 (= K266), G455 (= G267), T456 (= T268), M547 (≠ I359), Y570 (= Y382), R590 (= R402), V603 (≠ G415), G604 (= G416), G605 (= G417), A606 (= A418), E619 (= E431), K623 (= K435)
- binding tryptophan: P419 (= P231), Y420 (≠ F232), G421 (≠ S233), L574 (= L386), G575 (≠ L387)
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)
31% identity, 93% coverage: 23:435/446 of query aligns to 90:559/577 of Q94GF1
- D323 (= D216) 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: 15:437/446 of query aligns to 35:468/489 of O94582
- S390 (≠ T360) modified: Phosphoserine
- S392 (≠ A362) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
33% identity, 80% coverage: 86:443/446 of query aligns to 138:506/512 of 1i1qA
- active site: Q259 (= Q202), E305 (= E250), A323 (≠ K266), E357 (= E294), H394 (= H331), T421 (≠ S358), Y445 (= Y382), R465 (= R402), G481 (≠ A418), E494 (= E431), K498 (= K435)
- binding tryptophan: P287 (= P231), Y288 (≠ F232), M289 (≠ S233), G450 (≠ L387), C461 (≠ S398)
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)
33% identity, 80% coverage: 86:443/446 of query aligns to 142:510/520 of P00898
- C174 (≠ Q122) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ C228) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P229) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S233) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ G234) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S246) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ S335) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G393) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S398) 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.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
33% identity, 78% coverage: 95:443/446 of query aligns to 139:501/511 of 1i7sA
- active site: Q254 (= Q202), E300 (= E250), A318 (≠ K266), E352 (= E294), H389 (= H331), T416 (≠ S358), Y440 (= Y382), R460 (= R402), G476 (≠ A418), E489 (= E431), K493 (= K435)
- binding tryptophan: P282 (= P231), Y283 (≠ F232), M284 (≠ S233), V444 (≠ L386), G445 (≠ L387), D454 (= D396), C456 (≠ S398)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
33% identity, 78% coverage: 95:443/446 of query aligns to 145:507/517 of 1i7qA
- active site: Q260 (= Q202), E306 (= E250), A324 (≠ K266), E358 (= E294), H395 (= H331), T422 (≠ S358), Y446 (= Y382), R466 (= R402), G482 (≠ A418), E495 (= E431), K499 (= K435)
- binding magnesium ion: E358 (= E294), E495 (= E431)
- binding pyruvic acid: Y446 (= Y382), I465 (= I401), R466 (= R402), A479 (≠ G415), G480 (= G416), K499 (= K435)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
33% identity, 78% coverage: 95:443/446 of query aligns to 147:509/519 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)
32% identity, 59% coverage: 173:436/446 of query aligns to 136:399/408 of 2fn1A
- active site: K167 (≠ Q202), E214 (= E250), A230 (≠ K266), E258 (= E294), H295 (= H331), T322 (≠ S358), Y346 (= Y382), R365 (= R402), G381 (≠ A418), E394 (= E431), K398 (= K435)
- binding magnesium ion: E258 (= E294), E394 (= E431)
- binding pyruvic acid: Y346 (= Y382), L364 (≠ I401), R365 (= R402), A378 (≠ G415), G379 (= G416), K398 (= K435)
Query Sequence
>PP_2329 FitnessBrowser__Putida:PP_2329
MPTCTLHPLPYQPDPAAYFAHLRQAPGAILLDSARPGAERGRFDLLSAWPLQQLQAQPDE
DGRVFLQRLRAGLAQLGHADLPNGVELPFAGGLIGYLSYDFGRRLEHLPSLAVDDLGLPD
AQLGLYAWALVSDHLLGTSQLVFHPSLAGDERERLISLFQDTSATTGDFRLLAPMAGDLE
PEQYKTAFDQVQRYIQAGDCYQINLTQRFRAPCQGDPWRAYQALRQACPTPFSGYQQLAD
GSTLLSFSPERFIRVSQGQVETRPIKGTRPRASDPAQDQRNAQELLHSPKDRSENLMIVD
LLRNDLGRTCEIGSVKVPELFSLESYPNVHHLVSSITGQLASDKDALDLIGDSFPGGSIT
GAPKIRAMQIIDELEPARRALYCGSLLYVDVRGEMDSSIAIRSLLIKDGQVSCWGGGAVV
ADSQWQAEYEESIAKVRVLMQTLQGL
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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