SitesBLAST
Comparing WP_015798522.1 NCBI__GCF_000023265.1:WP_015798522.1 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)
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, 97% coverage: 4:482/495 of query aligns to 40:511/524 of A0QX93
- K355 (≠ E319) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
44% identity, 97% coverage: 4:482/495 of query aligns to 20:486/499 of 7bvdA
- active site: Q248 (= Q239), E301 (= E286), A317 (= A302), E341 (= E330), H378 (= H367), T405 (= T394), Y429 (= Y418), R449 (= R444), G465 (= G461), E478 (= E474), K482 (= K478)
- binding pyruvic acid: S93 (≠ G81), G94 (vs. gap), A100 (≠ G85)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
43% identity, 97% coverage: 4:482/495 of query aligns to 20:490/505 of 5cwaA
- active site: Q248 (= Q239), E301 (= E286), A317 (= A302), E345 (= E330), H382 (= H367), T409 (= T394), Y433 (= Y418), R453 (= R444), G469 (= G461), E482 (= E474), K486 (= K478)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y418), I452 (= I443), A466 (= A458), G467 (= G459), K486 (= K478)
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)
36% identity, 96% coverage: 20:495/495 of query aligns to 19:469/470 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.
7pi1DDD Aminodeoxychorismate synthase component 1
36% identity, 95% coverage: 20:490/495 of query aligns to 17:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G461), E438 (= E471)
- binding tryptophan: L33 (= L36), E34 (= E37), S35 (= S38), G39 (≠ S46), Y41 (= Y48), P242 (= P268), Y243 (= Y269), M244 (= M270), Q406 (≠ D438), N408 (≠ A440)
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)
36% identity, 98% coverage: 4:490/495 of query aligns to 78:589/595 of P32068
- D341 (≠ N253) 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)
38% identity, 96% coverage: 14:490/495 of query aligns to 72:571/577 of Q94GF1
- D323 (≠ N253) 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)
37% identity, 97% coverage: 14:492/495 of query aligns to 30:480/489 of O94582
- S390 (= S396) modified: Phosphoserine
- S392 (≠ A398) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
41% identity, 71% coverage: 137:489/495 of query aligns to 165:509/512 of 1i1qA
- active site: Q259 (= Q239), E305 (= E286), A323 (= A302), E357 (= E330), H394 (= H367), T421 (= T394), Y445 (= Y418), R465 (= R444), G481 (= G461), E494 (= E474), K498 (= K478)
- binding tryptophan: P287 (= P268), Y288 (= Y269), M289 (= M270), G450 (= G423), C461 (≠ A440)
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)
41% identity, 71% coverage: 137:489/495 of query aligns to 169:513/520 of P00898
- C174 (≠ R142) 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 (= M270) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y271) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G282) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ S371) 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 (≠ A440) 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.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
40% identity, 73% coverage: 135:495/495 of query aligns to 158:510/511 of 1i7sA
- active site: Q254 (= Q239), E300 (= E286), A318 (= A302), E352 (= E330), H389 (= H367), T416 (= T394), Y440 (= Y418), R460 (= R444), G476 (= G461), E489 (= E474), K493 (= K478)
- binding tryptophan: P282 (= P268), Y283 (= Y269), M284 (= M270), V444 (= V422), G445 (= G423), D454 (= D438), C456 (≠ A440)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
40% identity, 73% coverage: 135:495/495 of query aligns to 164:516/517 of 1i7qA
- active site: Q260 (= Q239), E306 (= E286), A324 (= A302), E358 (= E330), H395 (= H367), T422 (= T394), Y446 (= Y418), R466 (= R444), G482 (= G461), E495 (= E474), K499 (= K478)
- binding magnesium ion: E358 (= E330), E495 (= E474)
- binding pyruvic acid: Y446 (= Y418), I465 (= I443), R466 (= R444), A479 (= A458), G480 (= G459), K499 (= K478)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
34% identity, 100% coverage: 2:495/495 of query aligns to 6:518/519 of P00897
- S39 (= S38) binding L-tryptophan
- PYM 290:292 (= PYM 268:270) binding L-tryptophan
- E360 (= E330) binding Mg(2+)
- E497 (= E474) binding Mg(2+)
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)
34% identity, 77% coverage: 107:486/495 of query aligns to 101:451/453 of P05041
- 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 (= S350) 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.
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
34% identity, 77% coverage: 107:486/495 of query aligns to 99:435/437 of 1k0eA
- active site: E256 (= E286), K272 (≠ A302), E286 (= E330), H323 (= H367), S350 (≠ T394), W374 (≠ Y418), R394 (= R444), G410 (= G461), E423 (= E474), K427 (= K478)
- binding tryptophan: P238 (= P268), F239 (≠ Y269), S240 (≠ M270)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
33% identity, 95% coverage: 15:486/495 of query aligns to 167:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I301), K454 (≠ A302), G455 (= G303), T456 (≠ S304), M547 (≠ L395), Y570 (= Y418), R590 (= R444), V603 (≠ A458), G604 (= G459), G605 (≠ A460), A606 (≠ G461), E619 (= E474), K623 (= K478)
- binding tryptophan: L189 (= L36), D190 (≠ E37), S191 (= S38), S199 (= S46), F201 (≠ Y48), P419 (= P268), Y420 (= Y269), G421 (≠ M270), L574 (≠ V422), G575 (= G423)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
33% identity, 95% coverage: 15:486/495 of query aligns to 209:670/673 of 8hx8A
- binding magnesium ion: E521 (= E330), E655 (= E471), E658 (= E474)
- binding tryptophan: L231 (= L36), D232 (≠ E37), S233 (= S38), S241 (= S46), F243 (≠ Y48), P458 (= P268), Y459 (= Y269), G460 (≠ M270), G614 (= G423)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 77% coverage: 107:486/495 of query aligns to 101:418/420 of 1k0gA
- active site: E258 (= E286), K274 (= K326), E278 (= E330), S333 (≠ T394), W357 (≠ Y418), R377 (= R444), G393 (= G461), E406 (= E474), K410 (= K478)
- binding phosphate ion: D113 (≠ E119), R116 (= R122), D347 (= D408), R353 (= R414)
- binding tryptophan: P240 (= P268), F241 (≠ Y269), S242 (≠ M270)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 77% coverage: 107:486/495 of query aligns to 101:415/415 of 1k0gB
- active site: E258 (= E286), K274 (≠ A302), E277 (= E330), S330 (≠ T394), W354 (≠ Y418), R374 (= R444), G390 (= G461), E403 (= E474), K407 (= K478)
- binding phosphate ion: Y112 (= Y118), D113 (≠ E119), R116 (= R122), D344 (= D408), R350 (= R414)
- binding tryptophan: P240 (= P268), F241 (≠ Y269)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
33% identity, 58% coverage: 197:483/495 of query aligns to 149:419/424 of 5jy9B
- active site: K183 (≠ Q239), E230 (= E286), A246 (= A302), E274 (= E330), H311 (= H367), T338 (= T394), Y362 (= Y418), R381 (= R444), G397 (= G461), E410 (= E474), K414 (= K478)
- binding fe (ii) ion: E274 (= E330), E410 (= E474)
Query Sequence
>WP_015798522.1 NCBI__GCF_000023265.1:WP_015798522.1
MRLRLVQVRARYVADALTPIEVFERLVAPGEAGFILESVDQQGRWSRYSVVGRRPLARVI
GEVGHARLEAADGSVLDEAPGILDGLRRWSEGLEVDAVDDGCPMAGPFSAAFVGHVGYEA
VREREPSVPSSHPDDVGLPEARLLLAGDLAVIDHWAQSLTLSSALLVEDDPVGAAAAARA
ALSRLEADLESAVGRPVRAWPLGDDPSEGVALLDQGFREPFAHAVRLAKQAIDEGEVFQV
VLSHRFELTTRANPLALYRALRLTNPSPYMYLITDAGGAIVGSSPEALATVRDGVVWTRP
IAGSRPRGSGGASDEALIEELLADPKERAEHLMLVDLARNDVGRVARFGSVVVDEFMVPE
RFARVIHLTSSVHGQLTDGVGPIDALAATLPAGTLSGAPKVRAMQLIDELESKRRVVYGG
VVGYVGRDGTDPESAVMDFAIAIRTAVWLENGRVLLQAGAGIVAGSDPEREATECVAKAA
AVARAVAVADRLIEV
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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