SitesBLAST
Comparing Pf1N1B4_3814 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3814 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)
46% identity, 100% coverage: 2:444/445 of query aligns to 4:453/453 of P05041
- S36 (= S33) binding L-tryptophan
- E258 (= E249) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K265) 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 (= G266) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R302) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R307) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S313) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H330) 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, 100% coverage: 2:444/445 of query aligns to 2:437/437 of 1k0eA
- active site: E256 (= E249), K272 (= K265), E286 (= E293), H323 (= H330), S350 (= S357), W374 (≠ Y381), R394 (= R401), G410 (= G417), E423 (= E430), K427 (= K434)
- binding tryptophan: L32 (= L31), H33 (≠ D32), S34 (= S33), Y41 (≠ R40), F44 (≠ Y43), P238 (= P230), F239 (= F231), S240 (= S232)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
43% identity, 100% coverage: 2:444/445 of query aligns to 4:420/420 of 1k0gA
- active site: E258 (= E249), K274 (= K265), E278 (= E293), S333 (= S357), W357 (≠ Y381), R377 (= R401), G393 (= G417), E406 (= E430), K410 (= K434)
- binding phosphate ion: D113 (= D98), R116 (= R101), D347 (= D371), R353 (= R377)
- binding tryptophan: L34 (= L31), H35 (≠ D32), S36 (= S33), Y43 (≠ R40), S44 (≠ G41), F46 (≠ Y43), P240 (= P230), F241 (= F231), S242 (= S232)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
43% identity, 99% coverage: 2:442/445 of query aligns to 4:415/415 of 1k0gB
- active site: E258 (= E249), K274 (= K265), E277 (= E293), S330 (= S357), W354 (≠ Y381), R374 (= R401), G390 (= G417), E403 (= E430), K407 (= K434)
- binding phosphate ion: Y112 (= Y97), D113 (= D98), R116 (= R101), D344 (= D371), R350 (= R377)
- binding tryptophan: L34 (= L31), H35 (≠ D32), S36 (= S33), Y43 (≠ R40), S44 (≠ G41), R45 (= R42), F46 (≠ Y43), P240 (= P230), F241 (= F231)
7pi1DDD Aminodeoxychorismate synthase component 1
43% identity, 78% coverage: 87:434/445 of query aligns to 96:445/459 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)
42% identity, 78% coverage: 87:434/445 of query aligns to 98:452/470 of P28820
- A283 (≠ K265) 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)
39% identity, 92% coverage: 30:440/445 of query aligns to 86:513/524 of A0QX93
- K355 (≠ A282) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
39% identity, 92% coverage: 30:440/445 of query aligns to 65:488/499 of 7bvdA
- active site: Q248 (= Q201), E301 (= E249), A317 (≠ K265), E341 (= E293), H378 (= H330), T405 (≠ S357), Y429 (= Y381), R449 (= R401), G465 (= G417), E478 (= E430), K482 (= K434)
- 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)
37% identity, 93% coverage: 26:440/445 of query aligns to 47:492/505 of 5cwaA
- active site: Q248 (= Q201), E301 (= E249), A317 (≠ K265), E345 (= E293), H382 (= H330), T409 (≠ S357), Y433 (= Y381), R453 (= R401), G469 (= G417), E482 (= E430), K486 (= K434)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y381), I452 (= I400), A466 (≠ G414), G467 (= G415), K486 (= K434)
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)
36% identity, 83% coverage: 66:436/445 of query aligns to 83:468/489 of O94582
- S390 (≠ T359) modified: Phosphoserine
- S392 (≠ A361) 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)
33% identity, 93% coverage: 23:434/445 of query aligns to 106:577/595 of P32068
- D341 (= D215) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
37% identity, 85% coverage: 65:442/445 of query aligns to 240:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I264), K454 (= K265), G455 (= G266), T456 (= T267), M547 (≠ I358), Y570 (= Y381), R590 (= R401), V603 (≠ G414), G604 (= G415), G605 (= G416), A606 (≠ G417), E619 (= E430), K623 (= K434)
- binding tryptophan: P419 (= P230), Y420 (≠ F231), G421 (≠ S232), L574 (= L385), G575 (≠ L386)
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, 85% coverage: 65:442/445 of query aligns to 282:670/673 of 8hx8A
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)
30% identity, 93% coverage: 23:434/445 of query aligns to 90:559/577 of Q94GF1
- D323 (= D215) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
36% identity, 79% coverage: 87:439/445 of query aligns to 141:503/512 of 1i1qA
- active site: Q259 (= Q201), E305 (= E249), A323 (≠ K265), E357 (= E293), H394 (= H330), T421 (≠ S357), Y445 (= Y381), R465 (= R401), G481 (= G417), E494 (= E430), K498 (= K434)
- binding tryptophan: P287 (= P230), Y288 (≠ F231), M289 (≠ S232), G450 (≠ L386), C461 (≠ S397)
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)
36% identity, 79% coverage: 87:439/445 of query aligns to 145:507/520 of P00898
- C174 (≠ R120) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ C227) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P228) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S232) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ G233) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S245) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ S334) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G392) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S397) 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 L-tryptophan; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding L-tryptophan
- 128 R→H: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
35% identity, 80% coverage: 82:439/445 of query aligns to 136:506/519 of P00897
- PYM 290:292 (≠ PFS 230:232) binding L-tryptophan
- E360 (= E293) binding Mg(2+)
- E497 (= E430) binding Mg(2+)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
35% identity, 80% coverage: 82:439/445 of query aligns to 134:504/517 of 1i7qA
- active site: Q260 (= Q201), E306 (= E249), A324 (≠ K265), E358 (= E293), H395 (= H330), T422 (≠ S357), Y446 (= Y381), R466 (= R401), G482 (= G417), E495 (= E430), K499 (= K434)
- binding magnesium ion: E358 (= E293), E495 (= E430)
- binding pyruvic acid: Y446 (= Y381), I465 (= I400), R466 (= R401), A479 (≠ G414), G480 (= G415), K499 (= K434)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
35% identity, 80% coverage: 82:439/445 of query aligns to 128:498/511 of 1i7sA
- active site: Q254 (= Q201), E300 (= E249), A318 (≠ K265), E352 (= E293), H389 (= H330), T416 (≠ S357), Y440 (= Y381), R460 (= R401), G476 (= G417), E489 (= E430), K493 (= K434)
- binding tryptophan: P282 (= P230), Y283 (≠ F231), M284 (≠ S232), V444 (≠ L385), G445 (≠ L386), D454 (= D395), C456 (≠ S397)
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)
33% identity, 60% coverage: 171:435/445 of query aligns to 135:399/408 of 2fn1A
- active site: K167 (≠ Q201), E214 (= E249), A230 (≠ K265), E258 (= E293), H295 (= H330), T322 (≠ S357), Y346 (= Y381), R365 (= R401), G381 (= G417), E394 (= E430), K398 (= K434)
- binding magnesium ion: E258 (= E293), E394 (= E430)
- binding pyruvic acid: Y346 (= Y381), L364 (≠ I400), R365 (= R401), A378 (≠ G414), G379 (= G415), K398 (= K434)
Query Sequence
>Pf1N1B4_3814 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3814
MLTCSVHPLPYRANPAEYFAAIRHAPGAVLLDSGRPSAERGRYDLLSAWPLEQLAVLPDE
SGSHFLQRLRDTLKRLGKATVPFDLPFAGGLIGYLSYDFGRHLENLPSQARDDLQLPDAR
FGLYDWALISDHHLATSQLVFHPALIDSERQRLLELFTQPAPQKIEPFKLDGPMSADLSA
DDYRQAFERIQQYIQAGDCYQVNFAQRFRAQCQGDPWAAYCALRAACPTPFSGFQSLPDG
DAVLSLSPERFVKVSGRHVETRPIKGTRPRGLTAAEDAANAAELLASPKDRAENLMIVDL
LRNDLGRTCRIGSVRVPELFSLESYPNVHHLVSSVTGELADDKDALDLIAGSFPGGSITG
APKIRAMQIIDELEPTRRGLYCGSLLYLDVRGEMDSSIAIRSLLVKDGQVCCWGGGGIVA
DSDWQAEYQESITKVKVLLDTLQNL
Or try a new SitesBLAST search
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