SitesBLAST
Comparing WP_006747508.1 NCBI__GCF_000227685.2:WP_006747508.1 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)
7pi1DDD Aminodeoxychorismate synthase component 1
40% identity, 84% coverage: 70:433/435 of query aligns to 86:453/459 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)
41% identity, 84% coverage: 70:433/435 of query aligns to 88:460/470 of P28820
- A283 (= A255) 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.
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)
39% identity, 83% coverage: 71:433/435 of query aligns to 94:451/453 of P05041
- E258 (= E239) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A255) 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 (= G256) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R292) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R297) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S303) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H320) 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)
39% identity, 83% coverage: 71:433/435 of query aligns to 92:435/437 of 1k0eA
- active site: E256 (= E239), K272 (≠ A255), E286 (= E283), H323 (= H320), S350 (≠ T347), W374 (≠ Y372), R394 (= R392), G410 (= G408), E423 (= E421), K427 (= K425)
- binding tryptophan: P238 (= P221), F239 (= F222), S240 (≠ A223)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 83% coverage: 75:433/435 of query aligns to 299:670/673 of 8hx8A
Sites not aligning to the query:
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, 84% coverage: 70:433/435 of query aligns to 178:585/595 of P32068
- D341 (= D206) 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)
35% identity, 84% coverage: 70:433/435 of query aligns to 160:567/577 of Q94GF1
- D323 (= D206) mutation to N: Insensitive to feedback inhibition by tryptophan.
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
35% identity, 83% coverage: 75:433/435 of query aligns to 257:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I254), K454 (≠ A255), G455 (= G256), T456 (= T257), M547 (≠ I348), Y570 (= Y372), R590 (= R392), V603 (≠ T405), G604 (= G406), G605 (≠ A407), A606 (≠ G408), E619 (= E421), K623 (= K425)
- binding tryptophan: P419 (= P221), Y420 (≠ F222), G421 (≠ A223), L574 (≠ C376), G575 (= G377)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
37% identity, 83% coverage: 71:433/435 of query aligns to 94:415/415 of 1k0gB
- active site: E258 (= E239), K274 (≠ A255), E277 (= E283), S330 (≠ T347), W354 (≠ Y372), R374 (= R392), G390 (= G408), E403 (= E421), K407 (= K425)
- binding phosphate ion: Y112 (= Y89), D113 (≠ E90), R116 (≠ W93), D344 (≠ R361), R350 (≠ S368)
- binding tryptophan: P240 (= P221), F241 (= F222)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
37% identity, 83% coverage: 71:433/435 of query aligns to 94:418/420 of 1k0gA
- active site: E258 (= E239), K274 (= K279), E278 (= E283), S333 (≠ T347), W357 (≠ Y372), R377 (= R392), G393 (= G408), E406 (= E421), K410 (= K425)
- binding phosphate ion: D113 (≠ E90), R116 (≠ W93), D347 (≠ R361), R353 (≠ S368)
- binding tryptophan: P240 (= P221), F241 (= F222), S242 (≠ A223)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
41% identity, 60% coverage: 170:431/435 of query aligns to 228:492/505 of 5cwaA
- active site: Q248 (= Q190), E301 (= E239), A317 (= A255), E345 (= E283), H382 (= H320), T409 (= T347), Y433 (= Y372), R453 (= R392), G469 (= G408), E482 (= E421), K486 (= K425)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y372), I452 (= I391), A466 (≠ T405), G467 (= G406), K486 (= K425)
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)
42% identity, 60% coverage: 170:431/435 of query aligns to 249:513/524 of A0QX93
- K355 (≠ S272) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
41% identity, 60% coverage: 170:431/435 of query aligns to 228:488/499 of 7bvdA
- active site: Q248 (= Q190), E301 (= E239), A317 (= A255), E341 (= E283), H378 (= H320), T405 (= T347), Y429 (= Y372), R449 (= R392), G465 (= G408), E478 (= E421), K482 (= K425)
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)
32% identity, 96% coverage: 15:433/435 of query aligns to 40:474/489 of O94582
- S390 (≠ T349) modified: Phosphoserine
- S392 (≠ C351) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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, 87% coverage: 59:435/435 of query aligns to 118:512/520 of P00898
- R128 (= R69) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ W107) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N218) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P219) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A223) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A224) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S235) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ S324) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G383) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N388) 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
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
33% identity, 87% coverage: 59:435/435 of query aligns to 114:508/512 of 1i1qA
- active site: Q259 (= Q190), E305 (= E239), A323 (= A255), E357 (= E283), H394 (= H320), T421 (= T347), Y445 (= Y372), R465 (= R392), G481 (= G408), E494 (= E421), K498 (= K425)
- binding tryptophan: P287 (= P221), Y288 (≠ F222), M289 (≠ A223), G450 (= G377), C461 (≠ N388)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
32% identity, 88% coverage: 53:435/435 of query aligns to 100:503/511 of 1i7sA
- active site: Q254 (= Q190), E300 (= E239), A318 (= A255), E352 (= E283), H389 (= H320), T416 (= T347), Y440 (= Y372), R460 (= R392), G476 (= G408), E489 (= E421), K493 (= K425)
- binding tryptophan: P282 (= P221), Y283 (≠ F222), M284 (≠ A223), V444 (≠ C376), G445 (= G377), D454 (= D386), C456 (≠ N388)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 88% coverage: 53:435/435 of query aligns to 106:509/517 of 1i7qA
- active site: Q260 (= Q190), E306 (= E239), A324 (= A255), E358 (= E283), H395 (= H320), T422 (= T347), Y446 (= Y372), R466 (= R392), G482 (= G408), E495 (= E421), K499 (= K425)
- binding magnesium ion: E358 (= E283), E495 (= E421)
- binding pyruvic acid: Y446 (= Y372), I465 (= I391), R466 (= R392), A479 (≠ T405), G480 (= G406), K499 (= K425)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
32% identity, 88% coverage: 53:435/435 of query aligns to 108:511/519 of P00897
- PYM 290:292 (≠ PFA 221:223) binding L-tryptophan
- E360 (= E283) binding Mg(2+)
- E497 (= E421) binding Mg(2+)
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, 61% coverage: 161:425/435 of query aligns to 137:398/408 of 2fn1A
- active site: K167 (≠ Q190), E214 (= E239), A230 (= A255), E258 (= E283), H295 (= H320), T322 (= T347), Y346 (= Y372), R365 (= R392), G381 (= G408), E394 (= E421), K398 (= K425)
- binding magnesium ion: E258 (= E283), E394 (= E421)
- binding pyruvic acid: Y346 (= Y372), L364 (≠ I391), R365 (= R392), A378 (≠ T405), G379 (= G406), K398 (= K425)
Query Sequence
>WP_006747508.1 NCBI__GCF_000227685.2:WP_006747508.1
MSVRPLATGADLWALARSHPQRYPHLLDTALIGQAPARFSILFAFPGAQLTGDAVLDGLA
GIGPFDAMREPEPPPGLPFAGGWFVYLGYELAWSIEPSLGACTPDPWLPSAVLTRFPAAL
IVDHWERRSYFVDEDDDPQRWDQVRADLAGVGDADPAEWPPMQLDEDDPEDYRQAVRRAL
RYIRDGDCFQANLSREWRIRSSRPWDTADVYARLRRANPAPFAAWLRLPGGEVLSSSPER
LVAVRHGVAETRPIAGTRRRDADAMKDHALSSDLKVNRKEIAEHVMLVDLERNDLGRVAV
PGSVCVPEFMTIESYRRVHHIVSSVQARLRPGATPADLLRACFPGGTITGCPKIRSMQII
RELEQGASRGAYTGSCGYISRDGRMDTNILIRTFVVRGQDLRFRTGAGIVADSDPEAELQ
ETRHKAQGLLDALTS
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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