SitesBLAST
Comparing WP_015945221.1 NCBI__GCF_000021925.1:WP_015945221.1 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)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 99% coverage: 3:715/721 of query aligns to 7:670/673 of 8hx8A
- binding magnesium ion: I175 (= I172), S177 (≠ T174), E521 (= E566), E655 (= E700), E658 (= E703)
- binding tryptophan: L231 (= L231), D232 (= D232), S233 (= S233), S241 (≠ G241), F243 (≠ Y243), P458 (= P503), Y459 (≠ F504), G460 (≠ A505), G614 (= G659)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
35% identity, 99% coverage: 3:715/721 of query aligns to 6:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I537), K454 (= K538), G455 (= G539), T456 (= T540), M547 (≠ I631), Y570 (= Y654), R590 (= R674), V603 (≠ G687), G604 (= G688), G605 (= G689), A606 (≠ G690), E619 (= E703), K623 (= K707)
- binding magnesium ion: S134 (≠ T174), D135 (≠ E175)
- binding tryptophan: L189 (= L231), D190 (= D232), S191 (= S233), S199 (≠ G241), F201 (≠ Y243), P419 (= P503), Y420 (≠ F504), G421 (≠ A505), L574 (≠ I658), G575 (= G659)
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, 70% coverage: 211:715/721 of query aligns to 11:460/470 of P28820
- A283 (≠ K538) 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
35% identity, 70% coverage: 211:715/721 of query aligns to 9:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G690), E438 (= E700)
- binding tryptophan: L33 (= L231), E34 (≠ D232), S35 (= S233), G39 (= G241), Y41 (= Y243), P242 (= P503), Y243 (≠ F504), M244 (≠ A505), Q406 (≠ D668), N408 (= N670)
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, 59% coverage: 292:715/721 of query aligns to 78:451/453 of P05041
- E258 (= E521) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K538) 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 (= G539) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R575) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R580) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S586) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H603) 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)
38% identity, 59% coverage: 292:715/721 of query aligns to 76:435/437 of 1k0eA
- active site: E256 (= E521), K272 (= K538), E286 (= E566), H323 (= H603), S350 (= S630), W374 (≠ Y654), R394 (= R674), G410 (= G690), E423 (= E703), K427 (= K707)
- binding tryptophan: P238 (= P503), F239 (= F504), S240 (≠ A505)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
35% identity, 67% coverage: 229:712/721 of query aligns to 50:491/505 of 5cwaA
- active site: Q248 (= Q474), E301 (= E521), A317 (≠ K538), E345 (= E566), H382 (= H603), T409 (≠ S630), Y433 (= Y654), R453 (= R674), G469 (= G690), E482 (= E703), K486 (= K707)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y654), I452 (= I673), A466 (≠ G687), G467 (= G688), K486 (= K707)
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)
33% identity, 67% coverage: 229:712/721 of query aligns to 70:512/524 of A0QX93
- K355 (≠ R555) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
34% identity, 55% coverage: 314:710/721 of query aligns to 104:469/489 of O94582
- S390 (≠ T632) modified: Phosphoserine
- S392 (≠ A634) 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, 68% coverage: 224:715/721 of query aligns to 105:585/595 of P32068
- D341 (≠ E488) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
58% identity, 25% coverage: 1:183/721 of query aligns to 1:183/187 of P00903
- C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H168) mutation to Q: Loss of activity.
- E170 (= E170) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
35% identity, 59% coverage: 292:715/721 of query aligns to 78:418/420 of 1k0gA
- active site: E258 (= E521), K274 (= K562), E278 (= E566), S333 (= S630), W357 (≠ Y654), R377 (= R674), G393 (= G690), E406 (= E703), K410 (= K707)
- binding phosphate ion: D113 (= D325), R116 (≠ D328), D347 (≠ E644), R353 (≠ K650)
- binding tryptophan: P240 (= P503), F241 (= F504), S242 (≠ A505)
Sites not aligning to the query:
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 55% coverage: 313:712/721 of query aligns to 118:487/499 of 7bvdA
- active site: Q248 (= Q474), E301 (= E521), A317 (≠ K538), E341 (= E566), H378 (= H603), T405 (≠ S630), Y429 (= Y654), R449 (= R674), G465 (= G690), E478 (= E703), K482 (= K707)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
35% identity, 59% coverage: 292:715/721 of query aligns to 78:415/415 of 1k0gB
- active site: E258 (= E521), K274 (= K538), E277 (= E566), S330 (= S630), W354 (≠ Y654), R374 (= R674), G390 (= G690), E403 (= E703), K407 (= K707)
- binding phosphate ion: Y112 (= Y324), D113 (= D325), R116 (≠ D328), D344 (≠ E644), R350 (≠ K650)
- binding tryptophan: P240 (= P503), F241 (= F504)
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, 68% coverage: 224:715/721 of query aligns to 89:567/577 of Q94GF1
- D323 (≠ E488) 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)
38% identity, 38% coverage: 443:716/721 of query aligns to 232:511/520 of P00898
- N288 (= N500) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P501) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A505) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A506) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S517) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T607) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G665) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N670) 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.
- 174 C→Y: 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)
38% identity, 38% coverage: 443:716/721 of query aligns to 228:507/512 of 1i1qA
- active site: Q259 (= Q474), E305 (= E521), A323 (≠ K538), E357 (= E566), H394 (= H603), T421 (≠ S630), Y445 (= Y654), R465 (= R674), G481 (= G690), E494 (= E703), K498 (= K707)
- binding tryptophan: P287 (= P503), Y288 (≠ F504), M289 (≠ A505), G450 (= G659), C461 (≠ N670)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
37% identity, 37% coverage: 452:716/721 of query aligns to 238:508/517 of 1i7qA
- active site: Q260 (= Q474), E306 (= E521), A324 (≠ K538), E358 (= E566), H395 (= H603), T422 (≠ S630), Y446 (= Y654), R466 (= R674), G482 (= G690), E495 (= E703), K499 (= K707)
- binding magnesium ion: E358 (= E566), E495 (= E703)
- binding pyruvic acid: Y446 (= Y654), I465 (= I673), R466 (= R674), A479 (≠ G687), G480 (= G688), K499 (= K707)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
37% identity, 37% coverage: 452:716/721 of query aligns to 232:502/511 of 1i7sA
- active site: Q254 (= Q474), E300 (= E521), A318 (≠ K538), E352 (= E566), H389 (= H603), T416 (≠ S630), Y440 (= Y654), R460 (= R674), G476 (= G690), E489 (= E703), K493 (= K707)
- binding tryptophan: P282 (= P503), Y283 (≠ F504), M284 (≠ A505), V444 (≠ I658), G445 (= G659), D454 (= D668), C456 (≠ N670)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
36% identity, 37% coverage: 452:716/721 of query aligns to 240:510/519 of P00897
Sites not aligning to the query:
Query Sequence
>WP_015945221.1 NCBI__GCF_000021925.1:WP_015945221.1
MIFILDNFDSFTFNLYQYFGELGEEVVALRRDQCTIDAIEELKPELIVISPGPCAPRDTQ
FTLTVIDYFKGKVPILGVCLGHQAIGEILGGEVIRAKAPVHGKVSEIHHDGQGVFFQLPN
PLTVTRYHSLALRRESLPEELLITAETADGEIMGIRHRELPLEGVQFHPEAILTEKGHDL
LGNAVKNARTWWQAQGQSGHNSPWVIQELAIDLQPIELLEAFKESEYPFFLDSGRNYGGL
GRYSFMGAFPFLQASACRDGVEVKRFAGEEEGSKEDLSSLIGQEWLAYPEGESLKILDDL
VERYRVPNPTEFPFVGGAVGFWTYDLKDELEKMPQSGINDLDLPLWRFSWYDGIVVYDHE
NRRYTLLACGMTESGECRRALAQARVERLVGVLEGFLEGRGGKGDHPGTAAAYQRQIGAR
IGTQQERSGTYQGHDESQDMEQPQERVHYTVSKEQYLLDLQRVIDYIYAGDIYQANLTQR
FQFPYTKEPMALYKALHAHNPAPFAAFLPYEDFQILSSSPERFVQISAQGEIETRPIKGT
RPRGKTPEEDEAYARELTESTKDRAELTMIIDLQRNDLGRICRYGSVRVTDLIRLEQYPT
VWHLVSTIVGKLKPELKTSEILKAIFPGGSITGAPKIRAMEIIEELEPYKRGLYTGSIGY
MGFDGAWDTNIVIRTILLKDGQAYFNGGGGIVADSVPEEEYQEALQKVKALLRVLSYPSI
G
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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