SitesBLAST
Comparing WP_004322780.1 NCBI__GCF_000310185.1:WP_004322780.1 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)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
42% identity, 98% coverage: 3:483/490 of query aligns to 50:571/577 of Q94GF1
- D323 (≠ S253) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
44% identity, 96% coverage: 5:476/490 of query aligns to 31:512/524 of A0QX93
- K355 (≠ Q319) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7pi1DDD Aminodeoxychorismate synthase component 1
40% identity, 96% coverage: 15:483/490 of query aligns to 7:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G454), E438 (= E464)
- binding tryptophan: L33 (= L46), E34 (= E47), S35 (= S48), G39 (= G52), Y41 (= Y58), P242 (= P268), Y243 (= Y269), M244 (≠ L270), Q406 (≠ D432), N408 (≠ A434)
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, 96% coverage: 15:483/490 of query aligns to 9:464/470 of P28820
- A283 (= A302) 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.
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)
39% identity, 98% coverage: 8:486/490 of query aligns to 71:592/595 of P32068
- D341 (≠ S253) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
45% identity, 96% coverage: 5:476/490 of query aligns to 11:491/505 of 5cwaA
- active site: Q248 (= Q239), E301 (= E286), A317 (= A302), E345 (= E330), H382 (= H367), T409 (= T394), Y433 (= Y418), R453 (= R438), G469 (= G454), E482 (= E467), K486 (= K471)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y418), I452 (= I437), A466 (= A451), G467 (= G452), K486 (= K471)
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)
40% identity, 96% coverage: 15:483/490 of query aligns to 20:478/489 of O94582
- S390 (= S396) modified: Phosphoserine
- S392 (≠ A398) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
44% identity, 96% coverage: 5:476/490 of query aligns to 11:487/499 of 7bvdA
- active site: Q248 (= Q239), E301 (= E286), A317 (= A302), E341 (= E330), H378 (= H367), T405 (= T394), Y429 (= Y418), R449 (= R438), G465 (= G454), E478 (= E467), K482 (= K471)
- binding pyruvic acid: S93 (≠ D89), G94 (≠ Y90), A100 (≠ F96)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
40% identity, 79% coverage: 104:488/490 of query aligns to 134:519/520 of P00898
- C174 (≠ L150) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N265) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P266) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L270) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F271) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G282) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N371) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G429) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A434) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (≠ G484) 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 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
40% identity, 78% coverage: 104:483/490 of query aligns to 130:510/512 of 1i1qA
- active site: Q259 (= Q239), E305 (= E286), A323 (= A302), E357 (= E330), H394 (= H367), T421 (= T394), Y445 (= Y418), R465 (= R438), G481 (= G454), E494 (= E467), K498 (= K471)
- binding tryptophan: P287 (= P268), Y288 (= Y269), M289 (≠ L270), G450 (= G423), C461 (≠ A434)
Sites not aligning to the query:
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)
32% identity, 91% coverage: 34:480/490 of query aligns to 22:452/453 of P05041
- S36 (= S48) binding L-tryptophan
- E258 (= E286) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A302) 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 (= G303) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R339) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R344) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T350) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H367) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
39% identity, 76% coverage: 114:483/490 of query aligns to 138:511/517 of 1i7qA
- active site: Q260 (= Q239), E306 (= E286), A324 (= A302), E358 (= E330), H395 (= H367), T422 (= T394), Y446 (= Y418), R466 (= R438), G482 (= G454), E495 (= E467), K499 (= K471)
- binding magnesium ion: E358 (= E330), E495 (= E467)
- binding pyruvic acid: Y446 (= Y418), I465 (= I437), R466 (= R438), A479 (= A451), G480 (= G452), K499 (= K471)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
39% identity, 76% coverage: 114:483/490 of query aligns to 132:505/511 of 1i7sA
- active site: Q254 (= Q239), E300 (= E286), A318 (= A302), E352 (= E330), H389 (= H367), T416 (= T394), Y440 (= Y418), R460 (= R438), G476 (= G454), E489 (= E467), K493 (= K471)
- binding tryptophan: P282 (= P268), Y283 (= Y269), M284 (≠ L270), V444 (= V422), G445 (= G423), D454 (= D432), C456 (≠ A434)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
39% identity, 76% coverage: 114:483/490 of query aligns to 140:513/519 of P00897
- PYM 290:292 (≠ PYL 268:270) binding L-tryptophan
- E360 (= E330) binding Mg(2+)
- E497 (= E467) binding Mg(2+)
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
31% identity, 91% coverage: 34:480/490 of query aligns to 20:436/437 of 1k0eA
- active site: E256 (= E286), K272 (≠ A302), E286 (= E330), H323 (= H367), S350 (≠ T394), W374 (≠ Y418), R394 (= R438), G410 (= G454), E423 (= E467), K427 (= K471)
- binding tryptophan: L32 (= L46), H33 (≠ E47), S34 (= S48), Y41 (≠ F55), F44 (≠ Y58), P238 (= P268), F239 (≠ Y269), S240 (≠ L270)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 34:480/490 of query aligns to 22:419/420 of 1k0gA
- active site: E258 (= E286), K274 (= K326), E278 (= E330), S333 (≠ T394), W357 (≠ Y418), R377 (= R438), G393 (= G454), E406 (= E467), K410 (= K471)
- binding phosphate ion: D113 (= D126), R116 (= R129), D347 (= D408), R353 (≠ K414)
- binding tryptophan: L34 (= L46), H35 (≠ E47), S36 (= S48), Y43 (≠ F55), S44 (≠ G56), F46 (≠ Y58), P240 (= P268), F241 (≠ Y269), S242 (≠ L270)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
33% identity, 90% coverage: 37:478/490 of query aligns to 180:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I301), K454 (≠ A302), G455 (= G303), T456 (= T304), M547 (≠ V395), Y570 (= Y418), R590 (= R438), V603 (≠ A451), G604 (= G452), G605 (≠ A453), A606 (≠ G454), E619 (= E467), K623 (= K471)
- binding tryptophan: L189 (= L46), D190 (≠ E47), S191 (= S48), S199 (≠ G56), F201 (≠ Y58), P419 (= P268), Y420 (= Y269), G421 (≠ L270), L574 (≠ V422), G575 (= G423)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 91% coverage: 34:477/490 of query aligns to 22:413/415 of 1k0gB
- active site: E258 (= E286), K274 (≠ A302), E277 (= E330), S330 (≠ T394), W354 (≠ Y418), R374 (= R438), G390 (= G454), E403 (= E467), K407 (= K471)
- binding phosphate ion: Y112 (= Y125), D113 (= D126), R116 (= R129), D344 (= D408), R350 (≠ K414)
- binding tryptophan: L34 (= L46), H35 (≠ E47), S36 (= S48), Y43 (≠ F55), S44 (≠ G56), R45 (= R57), F46 (≠ Y58), P240 (= P268), F241 (≠ Y269)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
33% identity, 90% coverage: 37:478/490 of query aligns to 222:669/673 of 8hx8A
- binding magnesium ion: E521 (= E330), E655 (= E464), E658 (= E467)
- binding tryptophan: L231 (= L46), D232 (≠ E47), S233 (= S48), S241 (≠ G56), F243 (≠ Y58), P458 (= P268), Y459 (= Y269), G460 (≠ L270), G614 (= G423)
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, 53% coverage: 214:471/490 of query aligns to 142:398/408 of 2fn1A
- active site: K167 (≠ Q239), E214 (= E286), A230 (= A302), E258 (= E330), H295 (= H367), T322 (= T394), Y346 (= Y418), R365 (= R438), G381 (= G454), E394 (= E467), K398 (= K471)
- binding magnesium ion: E258 (= E330), E394 (= E467)
- binding pyruvic acid: Y346 (= Y418), L364 (≠ I437), R365 (= R438), A378 (= A451), G379 (= G452), K398 (= K471)
Query Sequence
>WP_004322780.1 NCBI__GCF_000310185.1:WP_004322780.1
MLEHEFNALAAEGYNRIPLTLETFADLDTPLSIYLKLANEPYTYLLESVQGGERFGRYSF
IGLSSPTRIEVYGRSALLLTGNRLVERRDYGDPLNFVAEFMNRIKVPPRQHLPRFAGGLV
GCFGYDTVRYIEPRLAKTEKADTVGTPDILLLLSEEVAIVDNLSGKLTLVVYAEPEVPGA
YKRAQRRLRELLARLREAVAIPEEFRGESAEPVSSFGEEAFKDAVRRAKQYIVDGDLMQV
VLSQRMSKPYAASPMALYRAIRSLNPSPYLFYFNLEDFHVVGASPEILTRLEDDVVTVRP
IAGTRKRGATPAEDLALEQELLADQKEIAEHVQLLDLGRNDAGRVSEVGTVRVTERFTVE
RYSHVMHIVSNVEGKLREGLDALAVLRATFPAGTVSGAPKVRAMEIIDELEPVKRGIYAG
AVGYLGFHGDMDLAIAIRTAVVKDGQIHVQAGAGIVADSDPDAEWNETQSKARAMLRAAE
MAEGGLDTRF
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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