SitesBLAST
Comparing WP_012606589.1 NCBI__GCF_000021485.1:WP_012606589.1 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)
44% identity, 95% coverage: 15:455/462 of query aligns to 15:451/453 of P05041
- S36 (= S35) binding L-tryptophan
- E258 (= E262) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K278) 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 (= G279) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R315) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R320) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S326) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H343) 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)
42% identity, 95% coverage: 15:455/462 of query aligns to 13:435/437 of 1k0eA
- active site: E256 (= E262), K272 (= K278), E286 (= E306), H323 (= H343), S350 (= S370), W374 (≠ Y394), R394 (= R414), G410 (= G430), E423 (= E443), K427 (= K447)
- binding tryptophan: L32 (= L33), H33 (≠ D34), S34 (= S35), Y41 (≠ Q42), F44 (≠ Y45), P238 (= P244), F239 (= F245), S240 (= S246)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
40% identity, 95% coverage: 15:455/462 of query aligns to 15:418/420 of 1k0gA
- active site: E258 (= E262), K274 (= K278), E278 (= E306), S333 (= S370), W357 (≠ Y394), R377 (= R414), G393 (= G430), E406 (= E443), K410 (= K447)
- binding phosphate ion: D113 (= D113), R116 (≠ L116), D347 (≠ A384), R353 (≠ A390)
- binding tryptophan: L34 (= L33), H35 (≠ D34), S36 (= S35), Y43 (≠ Q42), S44 (≠ G43), F46 (≠ Y45), P240 (= P244), F241 (= F245), S242 (= S246)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
40% identity, 95% coverage: 15:455/462 of query aligns to 15:415/415 of 1k0gB
- active site: E258 (= E262), K274 (= K278), E277 (= E306), S330 (= S370), W354 (≠ Y394), R374 (= R414), G390 (= G430), E403 (= E443), K407 (= K447)
- binding phosphate ion: Y112 (= Y112), D113 (= D113), R116 (≠ L116), D344 (≠ A384), R350 (≠ A390)
- binding tryptophan: L34 (= L33), H35 (≠ D34), S36 (= S35), Y43 (≠ Q42), S44 (≠ G43), R45 (= R44), F46 (≠ Y45), P240 (= P244), F241 (= F245)
7pi1DDD Aminodeoxychorismate synthase component 1
38% identity, 77% coverage: 99:455/462 of query aligns to 92:453/459 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)
38% identity, 77% coverage: 99:455/462 of query aligns to 94:460/470 of P28820
- A283 (≠ K278) 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.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 90% coverage: 30:447/462 of query aligns to 228:662/673 of 8hx8A
- binding magnesium ion: E521 (= E306), E655 (= E440), E658 (= E443)
- binding tryptophan: L231 (= L33), D232 (= D34), S233 (= S35), S241 (≠ G43), F243 (≠ Y45), P458 (= P244), Y459 (≠ F245), G460 (≠ S246), G614 (= G399)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 90% coverage: 30:447/462 of query aligns to 186:623/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I277), K454 (= K278), G455 (= G279), T456 (= T280), M547 (≠ I371), Y570 (= Y394), R590 (= R414), V603 (≠ A427), G604 (= G428), G605 (= G429), A606 (≠ G430), E619 (= E443), K623 (= K447)
- binding tryptophan: L189 (= L33), D190 (= D34), S191 (= S35), S199 (≠ G43), F201 (≠ Y45), P419 (= P244), Y420 (≠ F245), G421 (≠ S246), L574 (≠ V398), G575 (= G399)
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)
33% identity, 89% coverage: 43:455/462 of query aligns to 110:567/577 of Q94GF1
- D323 (≠ S229) 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)
33% identity, 91% coverage: 29:448/462 of query aligns to 48:467/489 of O94582
- S390 (≠ T372) modified: Phosphoserine
- S392 (≠ A374) 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: 25:447/462 of query aligns to 44:486/505 of 5cwaA
- active site: Q248 (= Q215), E301 (= E262), A317 (≠ K278), E345 (= E306), H382 (= H343), T409 (≠ S370), Y433 (= Y394), R453 (= R414), G469 (= G430), E482 (= E443), K486 (= K447)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y394), I452 (= I413), A466 (= A427), G467 (= G428), K486 (= K447)
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, 92% coverage: 30:455/462 of query aligns to 110:585/595 of P32068
- D341 (≠ S229) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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)
43% identity, 55% coverage: 196:447/462 of query aligns to 250:507/524 of A0QX93
- K355 (≠ Q295) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 55% coverage: 193:447/462 of query aligns to 226:482/499 of 7bvdA
- active site: Q248 (= Q215), E301 (= E262), A317 (≠ K278), E341 (= E306), H378 (= H343), T405 (≠ S370), Y429 (= Y394), R449 (= R414), G465 (= G430), E478 (= E443), K482 (= K447)
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)
33% identity, 84% coverage: 69:457/462 of query aligns to 113:512/520 of P00898
- R128 (= R84) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ A133) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N241) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P242) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S246) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A247) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S258) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ V347) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G405) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N410) 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, 84% coverage: 69:457/462 of query aligns to 109:508/512 of 1i1qA
- active site: Q259 (= Q215), E305 (= E262), A323 (≠ K278), E357 (= E306), H394 (= H343), T421 (≠ S370), Y445 (= Y394), R465 (= R414), G481 (= G430), E494 (= E443), K498 (= K447)
- binding tryptophan: P287 (= P244), Y288 (≠ F245), M289 (≠ S246), G450 (= G399), C461 (≠ N410)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 84% coverage: 69:457/462 of query aligns to 110:509/517 of 1i7qA
- active site: Q260 (= Q215), E306 (= E262), A324 (≠ K278), E358 (= E306), H395 (= H343), T422 (≠ S370), Y446 (= Y394), R466 (= R414), G482 (= G430), E495 (= E443), K499 (= K447)
- binding magnesium ion: E358 (= E306), E495 (= E443)
- binding pyruvic acid: Y446 (= Y394), I465 (= I413), R466 (= R414), A479 (= A427), G480 (= G428), K499 (= K447)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
32% identity, 84% coverage: 69:457/462 of query aligns to 104:503/511 of 1i7sA
- active site: Q254 (= Q215), E300 (= E262), A318 (≠ K278), E352 (= E306), H389 (= H343), T416 (≠ S370), Y440 (= Y394), R460 (= R414), G476 (= G430), E489 (= E443), K493 (= K447)
- binding tryptophan: P282 (= P244), Y283 (≠ F245), M284 (≠ S246), V444 (= V398), G445 (= G399), D454 (= D408), C456 (≠ N410)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
31% identity, 84% coverage: 69:457/462 of query aligns to 112:511/519 of P00897
- PYM 290:292 (≠ PFS 244:246) binding L-tryptophan
- E360 (= E306) binding Mg(2+)
- E497 (= E443) binding Mg(2+)
Sites not aligning to the query:
5jy8A An iron-bound structure of the isochorismate synthase entc (see paper)
30% identity, 47% coverage: 233:451/462 of query aligns to 145:362/368 of 5jy8A
- active site: E175 (= E262), A191 (≠ K278), E219 (= E306), H254 (= H343), A281 (≠ S370), F305 (≠ Y394), R325 (= R414), G341 (= G430), E354 (= E443), K358 (= K447)
- binding fe (iii) ion: E219 (= E306), E237 (≠ S326), H239 (≠ Q328), E354 (= E443)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E175 (= E262), L190 (≠ I277), A191 (≠ K278), G192 (= G279), E219 (= E306), L282 (≠ I371), I324 (= I413), F337 (≠ W426), A338 (= A427), G339 (= G428), E354 (= E443), K358 (= K447)
Sites not aligning to the query:
Query Sequence
>WP_012606589.1 NCBI__GCF_000021485.1:WP_012606589.1
MPHSVLTRCAVPYPEDAATVFAPLASIPWSFFLDSSATVSLQGRYSMLVTAPRRRLWQEA
KQLWVADGDGPARRSALSLWEALRESVIRLPDAASLPAELPFAGGALGYLAYDFGLAGQG
IPPPPAQSLPEAAFGIYDTALLVDHHGRKAWLCAPEDRMVQALAEWQPRLACGKVYPHDP
SFQARGPVRPLWSRSEYAAAFARVHAYIQAGDCYQVNLAQPFVAPYAGSPWSLYQRLRTV
NPAPFSAYLSMPQGAVLSFSPERLLQVQKDRLQVRPIKGTRPRLKDRQEDQQMAQALLAS
PKDRAENVMIVDLLRNDLGRVAATGSVQVPQLCALESYAEVHHLVSVVEARLASGQDALS
ALKACFPGGSITGAPKRRAMEIIAELEAGARGLYCGSVGYLDQRGSLDMNIAIRSMTAVR
GELRFWAGGGIVADSDPDAEYQETLDKVAVFHRELAALAGEG
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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