SitesBLAST
Comparing GFF3346 FitnessBrowser__Marino:GFF3346 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)
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)
45% identity, 91% coverage: 35:501/513 of query aligns to 42:512/524 of A0QX93
- K355 (≠ A344) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
40% identity, 96% coverage: 18:511/513 of query aligns to 56:592/595 of P32068
- D341 (≠ P278) 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)
40% identity, 95% coverage: 23:511/513 of query aligns to 52:574/577 of Q94GF1
- D323 (≠ P278) mutation to N: Insensitive to feedback inhibition by tryptophan.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
43% identity, 94% coverage: 18:501/513 of query aligns to 6:491/505 of 5cwaA
- active site: Q248 (= Q264), E301 (= E311), A317 (= A327), E345 (= E355), H382 (= H392), T409 (= T419), Y433 (= Y443), R453 (= R463), G469 (= G479), E482 (= E492), K486 (= K496)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y443), I452 (= I462), A466 (= A476), G467 (= G477), K486 (= K496)
7pi1DDD Aminodeoxychorismate synthase component 1
41% identity, 93% coverage: 33:507/513 of query aligns to 1:456/459 of 7pi1DDD
- binding magnesium ion: G428 (= G479), E438 (= E489)
- binding tryptophan: L33 (≠ F64), E34 (= E65), S35 (= S66), G39 (= G70), Y41 (= Y76), P242 (= P293), Y243 (= Y294), M244 (= M295), Q406 (≠ D457), N408 (≠ A459)
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, 93% coverage: 33:507/513 of query aligns to 3:463/470 of P28820
- A283 (= A327) 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.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
44% identity, 91% coverage: 35:501/513 of query aligns to 22:487/499 of 7bvdA
- active site: Q248 (= Q264), E301 (= E311), A317 (= A327), E341 (= E355), H378 (= H392), T405 (= T419), Y429 (= Y443), R449 (= R463), G465 (= G479), E478 (= E492), K482 (= K496)
- binding pyruvic acid: S93 (≠ E107), G94 (≠ V108), A100 (≠ F114)
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)
39% identity, 95% coverage: 22:507/513 of query aligns to 8:477/489 of O94582
- S390 (= S421) modified: Phosphoserine
- S392 (≠ A423) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
1i7qA Anthranilate synthase from s. Marcescens (see paper)
37% identity, 73% coverage: 137:509/513 of query aligns to 143:512/517 of 1i7qA
- active site: Q260 (= Q264), E306 (= E311), A324 (= A327), E358 (= E355), H395 (= H392), T422 (= T419), Y446 (= Y443), R466 (= R463), G482 (= G479), E495 (= E492), K499 (= K496)
- binding magnesium ion: E358 (= E355), E495 (= E492)
- binding pyruvic acid: Y446 (= Y443), I465 (= I462), R466 (= R463), A479 (= A476), G480 (= G477), K499 (= K496)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
37% identity, 73% coverage: 137:509/513 of query aligns to 137:506/511 of 1i7sA
- active site: Q254 (= Q264), E300 (= E311), A318 (= A327), E352 (= E355), H389 (= H392), T416 (= T419), Y440 (= Y443), R460 (= R463), G476 (= G479), E489 (= E492), K493 (= K496)
- binding tryptophan: P282 (= P293), Y283 (= Y294), M284 (= M295), V444 (= V447), G445 (= G448), D454 (= D457), C456 (≠ A459)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
37% identity, 73% coverage: 137:509/513 of query aligns to 145:514/519 of P00897
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)
37% identity, 73% coverage: 133:509/513 of query aligns to 145:515/520 of P00898
- C174 (≠ L168) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N290) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P291) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M295) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y296) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G307) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N396) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G454) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A459) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (≠ N509) 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 ; 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
37% identity, 73% coverage: 133:509/513 of query aligns to 141:511/512 of 1i1qA
- active site: Q259 (= Q264), E305 (= E311), A323 (= A327), E357 (= E355), H394 (= H392), T421 (= T419), Y445 (= Y443), R465 (= R463), G481 (= G479), E494 (= E492), K498 (= K496)
- binding tryptophan: P287 (= P293), Y288 (= Y294), M289 (= M295), G450 (= G448), C461 (≠ A459)
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, 88% coverage: 52:504/513 of query aligns to 22:451/453 of P05041
- S36 (= S66) binding
- E258 (= E311) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A327) 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 (= G328) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R364) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R369) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T375) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H392) 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)
31% identity, 88% coverage: 52:504/513 of query aligns to 20:435/437 of 1k0eA
- active site: E256 (= E311), K272 (≠ A327), E286 (= E355), H323 (= H392), S350 (≠ T419), W374 (≠ Y443), R394 (= R463), G410 (= G479), E423 (= E492), K427 (= K496)
- binding tryptophan: L32 (≠ F64), H33 (≠ E65), S34 (= S66), Y41 (≠ W73), F44 (≠ Y76), P238 (= P293), F239 (≠ Y294), S240 (≠ M295)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 87% coverage: 61:504/513 of query aligns to 186:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I326), K454 (≠ A327), G455 (= G328), T456 (= T329), M547 (≠ L420), Y570 (= Y443), R590 (= R463), V603 (≠ A476), G604 (= G477), G605 (≠ A478), A606 (≠ G479), E619 (= E492), K623 (= K496)
- binding tryptophan: L189 (≠ F64), D190 (≠ E65), S191 (= S66), S199 (≠ G74), F201 (≠ Y76), P419 (= P293), Y420 (= Y294), G421 (≠ M295), L574 (≠ V447), G575 (= G448)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
31% identity, 87% coverage: 61:504/513 of query aligns to 228:670/673 of 8hx8A
- binding magnesium ion: E521 (= E355), E655 (= E489), E658 (= E492)
- binding tryptophan: L231 (≠ F64), D232 (≠ E65), S233 (= S66), S241 (≠ G74), F243 (≠ Y76), P458 (= P293), Y459 (= Y294), G460 (≠ M295), G614 (= G448)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 88% coverage: 52:504/513 of query aligns to 22:418/420 of 1k0gA
- active site: E258 (= E311), K274 (= K351), E278 (= E355), S333 (≠ T419), W357 (≠ Y443), R377 (= R463), G393 (= G479), E406 (= E492), K410 (= K496)
- binding phosphate ion: D113 (= D144), R116 (= R147), D347 (= D433), R353 (≠ K439)
- binding tryptophan: L34 (≠ F64), H35 (≠ E65), S36 (= S66), Y43 (≠ W73), S44 (≠ G74), F46 (≠ Y76), P240 (= P293), F241 (≠ Y294), S242 (≠ M295)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 88% coverage: 52:504/513 of query aligns to 22:415/415 of 1k0gB
- active site: E258 (= E311), K274 (≠ A327), E277 (= E355), S330 (≠ T419), W354 (≠ Y443), R374 (= R463), G390 (= G479), E403 (= E492), K407 (= K496)
- binding phosphate ion: Y112 (= Y143), D113 (= D144), R116 (= R147), D344 (= D433), R350 (≠ K439)
- binding tryptophan: L34 (≠ F64), H35 (≠ E65), S36 (= S66), Y43 (≠ W73), S44 (≠ G74), R45 (= R75), F46 (≠ Y76), P240 (= P293), F241 (≠ Y294)
6za5B M. Tuberculosis salicylate synthase mbti in complex with salicylate and mg2+ (see paper)
30% identity, 66% coverage: 141:481/513 of query aligns to 103:414/440 of 6za5B
Sites not aligning to the query:
Query Sequence
>GFF3346 FitnessBrowser__Marino:GFF3346
MEAQAFIHNADQISGNRTMTPEQFIELADAGFNRIPVYREVLADLDTPLSTYLKLASGPY
SYLFESVQGGEKWGRYSIIGLPSHEVLKVFDHRVEISRGGEVVETEEVDDPLAFVEAYQK
RFHAPDLDELPRFNGGLVGYFGYDTVRYIEKRLRKSCPPDKIGTPDILLMVSNEIVVFDN
LRGKLHLIVHADPAIEGAFETAQNRIDELENHLHRQTADAPRTPEHLRGKAVDESDFISG
FTQDKFEAAVDKIKGYVLDGDVMQTVISQRMSIPFEAPPLNLYRSLRVLNPSPYMYFLDL
GDFHIVGSSPEILARVEDEEVTVRPIAGTRKRGATDAEDKALEAELLADPKEIAEHLMLI
DLGRNDAGRVSETGTVRLTDKMIVERYSHVMHIVSNVTGRLKDNTSCLDVLRATLPAGTL
SGAPKIRAMEIIDELEPVKRGVYGGAVGYLSFNGNMDTAIAIRTAVIKDNTLHIQAGAGV
VADSVPRLEWKETMNKGRAIFRAVAMTYNDFDH
Or try a new SitesBLAST search
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