SitesBLAST
Comparing WP_011814994.1 NCBI__GCF_000015585.1:WP_011814994.1 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)
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)
48% identity, 93% coverage: 23:449/461 of query aligns to 25:452/453 of P05041
- S36 (= S34) binding L-tryptophan
- E258 (= E254) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K271) 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 (= G272) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R308) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ K313) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S319) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H336) 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)
47% identity, 93% coverage: 23:449/461 of query aligns to 23:436/437 of 1k0eA
- active site: E256 (= E254), K272 (= K271), E286 (= E299), H323 (= H336), S350 (= S363), W374 (≠ Y387), R394 (= R407), G410 (= G423), E423 (= E436), K427 (= K440)
- binding tryptophan: L32 (= L32), H33 (≠ D33), S34 (= S34), Y41 (≠ G41), F44 (≠ Y44), P238 (= P236), F239 (= F237), S240 (≠ A238)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
44% identity, 93% coverage: 23:449/461 of query aligns to 25:419/420 of 1k0gA
- active site: E258 (= E254), K274 (= K271), E278 (= E299), S333 (= S363), W357 (≠ Y387), R377 (= R407), G393 (= G423), E406 (= E436), K410 (= K440)
- binding phosphate ion: D113 (= D110), R116 (= R113), D347 (≠ T377), R353 (≠ P383)
- binding tryptophan: L34 (= L32), H35 (≠ D33), S36 (= S34), Y43 (≠ G41), S44 (≠ A42), F46 (≠ Y44), P240 (= P236), F241 (= F237), S242 (≠ A238)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
44% identity, 92% coverage: 23:446/461 of query aligns to 25:413/415 of 1k0gB
- active site: E258 (= E254), K274 (= K271), E277 (= E299), S330 (= S363), W354 (≠ Y387), R374 (= R407), G390 (= G423), E403 (= E436), K407 (= K440)
- binding phosphate ion: Y112 (= Y109), D113 (= D110), R116 (= R113), D344 (≠ T377), R350 (≠ P383)
- binding tryptophan: L34 (= L32), H35 (≠ D33), S36 (= S34), Y43 (≠ G41), S44 (≠ A42), R45 (= R43), F46 (≠ Y44), P240 (= P236), F241 (= F237)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
39% identity, 97% coverage: 5:450/461 of query aligns to 203:672/673 of 8hx8A
- binding magnesium ion: E521 (= E299), E655 (= E433), E658 (= E436)
- binding tryptophan: L231 (= L32), D232 (= D33), S233 (= S34), S241 (≠ A42), F243 (≠ Y44), P458 (= P236), Y459 (≠ F237), G460 (≠ A238), G614 (= G392)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
38% identity, 96% coverage: 5:446/461 of query aligns to 161:629/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I270), K454 (= K271), G455 (= G272), T456 (= T273), M547 (≠ I364), Y570 (= Y387), R590 (= R407), V603 (≠ A420), G604 (= G421), G605 (= G422), A606 (≠ G423), E619 (= E436), K623 (= K440)
- binding tryptophan: L189 (= L32), D190 (= D33), S191 (= S34), S199 (≠ A42), F201 (≠ Y44), P419 (= P236), Y420 (≠ F237), G421 (≠ A238), L574 (≠ I391), G575 (= G392)
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)
33% identity, 93% coverage: 32:458/461 of query aligns to 35:470/470 of P28820
- A283 (≠ K271) 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
34% identity, 87% coverage: 41:441/461 of query aligns to 38:446/459 of 7pi1DDD
Sites not aligning to the query:
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)
37% identity, 81% coverage: 75:446/461 of query aligns to 116:513/524 of A0QX93
- K355 (≠ R288) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
37% identity, 81% coverage: 75:446/461 of query aligns to 95:488/499 of 7bvdA
- active site: Q248 (= Q207), E301 (= E254), A317 (≠ K271), E341 (= E299), H378 (= H336), T405 (≠ S363), Y429 (= Y387), R449 (= R407), G465 (= G423), E478 (= E436), K482 (= K440)
- binding pyruvic acid: A100 (≠ H80)
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)
33% identity, 91% coverage: 20:440/461 of query aligns to 40:466/489 of O94582
- S390 (≠ T365) modified: Phosphoserine
- S392 (≠ A367) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
34% identity, 92% coverage: 21:446/461 of query aligns to 41:492/505 of 5cwaA
- active site: Q248 (= Q207), E301 (= E254), A317 (≠ K271), E345 (= E299), H382 (= H336), T409 (≠ S363), Y433 (= Y387), R453 (= R407), G469 (= G423), E482 (= E436), K486 (= K440)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y387), I452 (= I406), A466 (= A420), G467 (= G421), K486 (= K440)
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)
30% identity, 89% coverage: 43:451/461 of query aligns to 127:591/595 of P32068
- D341 (= D221) 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)
32% identity, 91% coverage: 32:450/461 of query aligns to 100:572/577 of Q94GF1
- D323 (= D221) 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)
35% identity, 74% coverage: 105:445/461 of query aligns to 148:507/520 of P00898
- C174 (≠ A129) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ S233) mutation to D: Decrease in feedback control by tryptophan.
- P289 (≠ S234) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A238) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A239) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S250) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T340) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G398) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S403) 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
33% identity, 74% coverage: 105:445/461 of query aligns to 144:503/512 of 1i1qA
- active site: Q259 (= Q207), E305 (= E254), A323 (≠ K271), E357 (= E299), H394 (= H336), T421 (≠ S363), Y445 (= Y387), R465 (= R407), G481 (= G423), E494 (= E436), K498 (= K440)
- binding tryptophan: P287 (= P236), Y288 (≠ F237), M289 (≠ A238), G450 (= G392), C461 (≠ S403)
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, 56% coverage: 187:445/461 of query aligns to 242:506/519 of P00897
- PYM 290:292 (≠ PFA 236:238) binding L-tryptophan
- E360 (= E299) binding Mg(2+)
- E497 (= E436) binding Mg(2+)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
36% identity, 56% coverage: 187:445/461 of query aligns to 240:504/517 of 1i7qA
- active site: Q260 (= Q207), E306 (= E254), A324 (≠ K271), E358 (= E299), H395 (= H336), T422 (≠ S363), Y446 (= Y387), R466 (= R407), G482 (= G423), E495 (= E436), K499 (= K440)
- binding magnesium ion: E358 (= E299), E495 (= E436)
- binding pyruvic acid: Y446 (= Y387), I465 (= I406), R466 (= R407), A479 (= A420), G480 (= G421), K499 (= K440)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
36% identity, 56% coverage: 187:445/461 of query aligns to 234:498/511 of 1i7sA
- active site: Q254 (= Q207), E300 (= E254), A318 (≠ K271), E352 (= E299), H389 (= H336), T416 (≠ S363), Y440 (= Y387), R460 (= R407), G476 (= G423), E489 (= E436), K493 (= K440)
- binding tryptophan: P282 (= P236), Y283 (≠ F237), M284 (≠ A238), V444 (≠ I391), G445 (= G392), D454 (= D401), C456 (≠ S403)
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)
31% identity, 56% coverage: 185:444/461 of query aligns to 145:402/408 of 2fn1A
- active site: K167 (≠ Q207), E214 (= E254), A230 (≠ K271), E258 (= E299), H295 (= H336), T322 (≠ S363), Y346 (= Y387), R365 (= R407), G381 (= G423), E394 (= E436), K398 (= K440)
- binding magnesium ion: E258 (= E299), E394 (= E436)
- binding pyruvic acid: Y346 (= Y387), L364 (≠ I406), R365 (= R407), A378 (= A420), G379 (= G421), K398 (= K440)
Query Sequence
>WP_011814994.1 NCBI__GCF_000015585.1:WP_011814994.1
MSLPLQSRSLPYIGDGATAMRVLGGEPWSAWLDSGHGGCAGARYDILVARPTVTLIAAGG
QTTIRRGERVERRHGDPLAHLAAELDALGPLPVDPRWPFTGGAVGYFGYDLGRRLMGVPG
ADPALPEMAVGIYEHAVITDHRHECSTAVGRRLDEAWLADVACRRETGARPQPWSTAGPV
LREPDADGYAAAFRRVQGYLHAGDCYQVNLARRFSVPCCGDPQAAYLALRAASSAPFAAW
LRFPGGDVLSLSPERFLHIDGDGRVTTEPIKGTRPRFTDPAEDEAARRDLLGSAKDRAEN
VMIVDLLRNDLGKGCEVGSVRVPSLCRAERFASVHHLVSTVTGRLAPGRRATDLLRDCLP
GGSITGAPKRRAMEIITELEPGPRGVYCGAIGYLGLDGRMDTSIAIRTATCSDGSMTYWA
GGGVVADSTAAAELQETEDKAAGFLSLAEGGQAAAGVRPRR
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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