SitesBLAST
Comparing AO356_20840 FitnessBrowser__pseudo5_N2C3_1:AO356_20840 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
47% identity, 99% coverage: 5:446/447 of query aligns to 7:453/453 of P05041
- S36 (= S33) binding
- E258 (= E251) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K267) 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 (= G268) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R304) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R309) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S315) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H332) 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)
46% identity, 99% coverage: 5:446/447 of query aligns to 5:437/437 of 1k0eA
- active site: E256 (= E251), K272 (= K267), E286 (= E295), H323 (= H332), S350 (= S359), W374 (≠ Y383), R394 (= R403), G410 (= G419), E423 (= E432), K427 (= K436)
- binding tryptophan: L32 (= L31), H33 (≠ D32), S34 (= S33), Y41 (≠ R40), F44 (≠ Y43), P238 (= P232), F239 (= F233), S240 (= S234)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
43% identity, 99% coverage: 5:446/447 of query aligns to 7:420/420 of 1k0gA
- active site: E258 (= E251), K274 (= K267), E278 (= E295), S333 (= S359), W357 (≠ Y383), R377 (= R403), G393 (= G419), E406 (= E432), K410 (= K436)
- binding phosphate ion: D113 (= D100), R116 (= R103), D347 (= D373), R353 (= R379)
- binding tryptophan: L34 (= L31), H35 (≠ D32), S36 (= S33), Y43 (≠ R40), S44 (≠ G41), F46 (≠ Y43), P240 (= P232), F241 (= F233), S242 (= S234)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
43% identity, 98% coverage: 5:444/447 of query aligns to 7:415/415 of 1k0gB
- active site: E258 (= E251), K274 (= K267), E277 (= E295), S330 (= S359), W354 (≠ Y383), R374 (= R403), G390 (= G419), E403 (= E432), K407 (= K436)
- binding phosphate ion: Y112 (= Y99), D113 (= D100), R116 (= R103), D344 (= D373), R350 (= R379)
- binding tryptophan: L34 (= L31), H35 (≠ D32), S36 (= S33), Y43 (≠ R40), S44 (≠ G41), R45 (= R42), F46 (≠ Y43), P240 (= P232), F241 (= F233)
7pi1DDD Aminodeoxychorismate synthase component 1
38% identity, 91% coverage: 37:445/447 of query aligns to 35:454/459 of 7pi1DDD
Sites not aligning to the query:
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)
37% identity, 91% coverage: 37:445/447 of query aligns to 37:461/470 of P28820
- A283 (≠ K267) 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)
40% identity, 93% coverage: 26:442/447 of query aligns to 67:513/524 of A0QX93
- K355 (≠ A284) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
40% identity, 93% coverage: 26:442/447 of query aligns to 47:488/499 of 7bvdA
- active site: Q248 (= Q203), E301 (= E251), A317 (≠ K267), E341 (= E295), H378 (= H332), T405 (≠ S359), Y429 (= Y383), R449 (= R403), G465 (= G419), E478 (= E432), K482 (= K436)
- binding pyruvic acid: S93 (= S61), G94 (= G62), A100 (≠ R68)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
39% identity, 93% coverage: 26:442/447 of query aligns to 47:492/505 of 5cwaA
- active site: Q248 (= Q203), E301 (= E251), A317 (≠ K267), E345 (= E295), H382 (= H332), T409 (≠ S359), Y433 (= Y383), R453 (= R403), G469 (= G419), E482 (= E432), K486 (= K436)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y383), I452 (= I402), A466 (≠ G416), G467 (= G417), K486 (= K436)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
39% identity, 83% coverage: 75:444/447 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 (= I266), K454 (= K267), G455 (= G268), T456 (= T269), M547 (≠ I360), Y570 (= Y383), R590 (= R403), V603 (≠ G416), G604 (= G417), G605 (= G418), A606 (≠ G419), E619 (= E432), K623 (= K436)
- binding tryptophan: P419 (= P232), Y420 (≠ F233), G421 (≠ S234), L574 (= L387), G575 (≠ L388)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
39% identity, 83% coverage: 75:444/447 of query aligns to 289:670/673 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)
33% identity, 98% coverage: 1:438/447 of query aligns to 22:468/489 of O94582
- S390 (≠ T361) modified: Phosphoserine
- S392 (≠ A363) 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)
31% identity, 93% coverage: 23:436/447 of query aligns to 106:577/595 of P32068
- D341 (= D217) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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: 23:436/447 of query aligns to 90:559/577 of Q94GF1
- D323 (= D217) 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)
35% identity, 80% coverage: 89:446/447 of query aligns to 145:512/520 of P00898
- C174 (≠ R122) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ C229) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P230) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S234) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ G235) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S247) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ S336) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G394) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S399) 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)
35% identity, 80% coverage: 89:446/447 of query aligns to 141:508/512 of 1i1qA
- active site: Q259 (= Q203), E305 (= E251), A323 (≠ K267), E357 (= E295), H394 (= H332), T421 (≠ S359), Y445 (= Y383), R465 (= R403), G481 (= G419), E494 (= E432), K498 (= K436)
- binding tryptophan: P287 (= P232), Y288 (≠ F233), M289 (≠ S234), G450 (≠ L388), C461 (≠ S399)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
35% identity, 78% coverage: 95:444/447 of query aligns to 145:507/517 of 1i7qA
- active site: Q260 (= Q203), E306 (= E251), A324 (≠ K267), E358 (= E295), H395 (= H332), T422 (≠ S359), Y446 (= Y383), R466 (= R403), G482 (= G419), E495 (= E432), K499 (= K436)
- binding magnesium ion: E358 (= E295), E495 (= E432)
- binding pyruvic acid: Y446 (= Y383), I465 (= I402), R466 (= R403), A479 (≠ G416), G480 (= G417), K499 (= K436)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
35% identity, 79% coverage: 95:446/447 of query aligns to 139:503/511 of 1i7sA
- active site: Q254 (= Q203), E300 (= E251), A318 (≠ K267), E352 (= E295), H389 (= H332), T416 (≠ S359), Y440 (= Y383), R460 (= R403), G476 (= G419), E489 (= E432), K493 (= K436)
- binding tryptophan: P282 (= P232), Y283 (≠ F233), M284 (≠ S234), V444 (≠ L387), G445 (≠ L388), D454 (= D397), C456 (≠ S399)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
35% identity, 78% coverage: 95:444/447 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)
36% identity, 59% coverage: 173:437/447 of query aligns to 135:399/408 of 2fn1A
- active site: K167 (≠ Q203), E214 (= E251), A230 (≠ K267), E258 (= E295), H295 (= H332), T322 (≠ S359), Y346 (= Y383), R365 (= R403), G381 (= G419), E394 (= E432), K398 (= K436)
- binding magnesium ion: E258 (= E295), E394 (= E432)
- binding pyruvic acid: Y346 (= Y383), L364 (≠ I402), R365 (= R403), A378 (≠ G416), G379 (= G417), K398 (= K436)
Query Sequence
>AO356_20840 FitnessBrowser__pseudo5_N2C3_1:AO356_20840
MPTCSVHPLPYRTNPAEYFAAIRHAPGSVLLDSGRPSAKRGRYDLLSAWPLAQLAVLPNE
SGSDFLQRLRIQLTQLGDAVLPATVQLPFAGGLIGYLSYDFGRHLETLPSHAQDDLQLPD
ARFGVYDWALISDHQAGTSQLVFHPHCGEDERQRLIALFSQPTTAAVPSFSLEGPMTPDL
SAEAYRQAFERIQAYIQAGDCYQVNFAQRFRAPCQGDAWAAYQALRAACPTPFSGFQSLP
EGGAVLSLSPERFVKVSEGQVETRPIKGTRPRGTTPEEDAAHAAELLASPKDRAENLMIV
DLLRNDLGRTCRIGSVRVPELFSLESYPNVHHLVSSVTGELADDKDALDLIAGSFPGGSI
TGAPKIRAMQIIDELEPTRRGLYCGSLLYLDVRGEMDSSIAIRSLLVKDGQVCCWGGGGI
VADSDWEAEYQESITKVRVLLETLQSL
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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