SitesBLAST
Comparing Synpcc7942_1003 FitnessBrowser__SynE:Synpcc7942_1003 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)
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)
39% identity, 97% coverage: 2:504/517 of query aligns to 63:585/595 of P32068
- D341 (= D267) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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, 97% coverage: 2:504/517 of query aligns to 3:474/489 of O94582
- S390 (= S417) modified: Phosphoserine
- S392 (≠ A419) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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: 10:504/517 of query aligns to 55:567/577 of Q94GF1
- D323 (= D267) mutation to N: Insensitive to feedback inhibition by tryptophan.
7pi1DDD Aminodeoxychorismate synthase component 1
38% identity, 92% coverage: 30:506/517 of query aligns to 14:455/459 of 7pi1DDD
- binding magnesium ion: G428 (= G479), E438 (= E489)
- binding tryptophan: L33 (= L49), E34 (= E50), S35 (= S51), G39 (= G55), Y41 (= Y61), P242 (= P282), Y243 (= Y283), M244 (= M284), Q406 (≠ N453), N408 (≠ A455)
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)
41% identity, 95% coverage: 9:501/517 of query aligns to 32:512/524 of A0QX93
- K355 (≠ T340) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 92% coverage: 30:506/517 of query aligns to 16:462/470 of P28820
- A283 (= A323) 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.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
41% identity, 96% coverage: 9:502/517 of query aligns to 12:492/505 of 5cwaA
- active site: Q248 (= Q253), E301 (= E300), A317 (= A323), E345 (= E351), H382 (= H388), T409 (= T415), Y433 (= Y439), R453 (= R459), G469 (= G479), E482 (= E492), K486 (= K496)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y439), I452 (= I458), A466 (= A476), G467 (= G477), K486 (= K496)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
41% identity, 95% coverage: 9:501/517 of query aligns to 12:487/499 of 7bvdA
- active site: Q248 (= Q253), E301 (= E300), A317 (= A323), E341 (= E351), H378 (= H388), T405 (= T415), Y429 (= Y439), R449 (= R459), G465 (= G479), E478 (= E492), K482 (= K496)
- binding pyruvic acid: S93 (= S92), G94 (= G93), A100 (= A98)
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, 92% coverage: 30:504/517 of query aligns to 19:510/520 of P00898
- E39 (= E50) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S51) binding ; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (≠ V52) mutation to V: Decrease in feedback control by tryptophan.
- K50 (≠ Y61) binding
- R128 (vs. gap) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (= C151) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N279) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P280) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M284) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A285) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G296) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N392) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G450) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A455) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
Sites not aligning to the query:
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
35% identity, 92% coverage: 30:504/517 of query aligns to 15:506/512 of 1i1qA
- active site: Q259 (= Q253), E305 (= E300), A323 (= A323), E357 (= E351), H394 (= H388), T421 (= T415), Y445 (= Y439), R465 (= R459), G481 (= G479), E494 (= E492), K498 (= K496)
- binding tryptophan: L34 (= L49), E35 (= E50), S36 (= S51), K46 (≠ Y61), P287 (= P282), Y288 (= Y283), M289 (= M284), G450 (= G444), C461 (≠ A455)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
33% identity, 91% coverage: 32:504/517 of query aligns to 18:507/517 of 1i7qA
- active site: Q260 (= Q253), E306 (= E300), A324 (= A323), E358 (= E351), H395 (= H388), T422 (= T415), Y446 (= Y439), R466 (= R459), G482 (= G479), E495 (= E492), K499 (= K496)
- binding magnesium ion: E358 (= E351), E495 (= E492)
- binding pyruvic acid: Y446 (= Y439), I465 (= I458), R466 (= R459), A479 (= A476), G480 (= G477), K499 (= K496)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
38% identity, 74% coverage: 121:504/517 of query aligns to 137:501/511 of 1i7sA
- active site: Q254 (= Q253), E300 (= E300), A318 (= A323), E352 (= E351), H389 (= H388), T416 (= T415), Y440 (= Y439), R460 (= R459), G476 (= G479), E489 (= E492), K493 (= K496)
- binding tryptophan: P282 (= P282), Y283 (= Y283), M284 (= M284), V444 (≠ Y443), G445 (= G444), D454 (≠ N453), C456 (≠ A455)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
33% identity, 91% coverage: 32:504/517 of query aligns to 20:509/519 of P00897
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)
33% identity, 89% coverage: 44:504/517 of query aligns to 29:451/453 of P05041
- S36 (= S51) binding
- E258 (= E300) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A323) 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 (= G324) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R360) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R365) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S371) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H388) 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)
33% identity, 89% coverage: 44:504/517 of query aligns to 27:435/437 of 1k0eA
- active site: E256 (= E300), K272 (≠ A323), E286 (= E351), H323 (= H388), S350 (≠ T415), W374 (≠ Y439), R394 (= R459), G410 (= G479), E423 (= E492), K427 (= K496)
- binding tryptophan: L32 (= L49), H33 (≠ E50), S34 (= S51), Y41 (≠ L58), F44 (≠ Y61), P238 (= P282), F239 (≠ Y283), S240 (≠ M284)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 89% coverage: 44:504/517 of query aligns to 29:418/420 of 1k0gA
- active site: E258 (= E300), K274 (= K347), E278 (= E351), S333 (≠ T415), W357 (≠ Y439), R377 (= R459), G393 (= G479), E406 (= E492), K410 (= K496)
- binding phosphate ion: D113 (≠ E128), R116 (= R131), D347 (≠ H429), R353 (= R435)
- binding tryptophan: L34 (= L49), H35 (≠ E50), S36 (= S51), Y43 (≠ L58), S44 (≠ G59), F46 (≠ Y61), P240 (= P282), F241 (≠ Y283), S242 (≠ M284)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 89% coverage: 44:504/517 of query aligns to 29:415/415 of 1k0gB
- active site: E258 (= E300), K274 (≠ A323), E277 (= E351), S330 (≠ T415), W354 (≠ Y439), R374 (= R459), G390 (= G479), E403 (= E492), K407 (= K496)
- binding phosphate ion: Y112 (= Y127), D113 (≠ E128), R116 (= R131), D344 (≠ H429), R350 (= R435)
- binding tryptophan: L34 (= L49), H35 (≠ E50), S36 (= S51), Y43 (≠ L58), S44 (≠ G59), R45 (= R60), F46 (≠ Y61), P240 (= P282), F241 (≠ Y283)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
31% identity, 89% coverage: 46:504/517 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 (= I322), K454 (≠ A323), G455 (= G324), T456 (= T325), M547 (≠ V416), Y570 (= Y439), R590 (= R459), V603 (≠ A476), G604 (= G477), G605 (≠ A478), A606 (≠ G479), E619 (= E492), K623 (= K496)
- binding tryptophan: L189 (= L49), D190 (≠ E50), S191 (= S51), S199 (≠ G59), F201 (≠ Y61), P419 (= P282), Y420 (= Y283), G421 (≠ M284), L574 (≠ Y443), G575 (= G444)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
32% identity, 89% coverage: 46:504/517 of query aligns to 228:670/673 of 8hx8A
- binding magnesium ion: E521 (= E351), E655 (= E489), E658 (= E492)
- binding tryptophan: L231 (= L49), D232 (≠ E50), S233 (= S51), S241 (≠ G59), F243 (≠ Y61), P458 (= P282), Y459 (= Y283), G460 (≠ M284), G614 (= G444)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
31% identity, 53% coverage: 223:496/517 of query aligns to 153:414/424 of 5jy9B
- active site: K183 (≠ Q253), E230 (= E300), A246 (= A323), E274 (= E351), H311 (= H388), T338 (= T415), Y362 (= Y439), R381 (= R459), G397 (= G479), E410 (= E492), K414 (= K496)
- binding fe (ii) ion: E274 (= E351), E410 (= E492)
Query Sequence
>Synpcc7942_1003 FitnessBrowser__SynE:Synpcc7942_1003
MIYPDFATFASLAEQGNFIPVYQEWVADLDTPVSAWYRICRDRPYSFLLESVEGGEHLGR
YSFLGCDPLWVLEARGDRTTRRFRDGSEEVFSGDPFAALKQCLAPYQPVHLPQLPSGVGG
LFGFWGYELMRWIEPRVPVHSGGENDLPDGCWMQVDSLMIFDQVKRRLYAIAYADLQAEP
DLHRAYALACNRVQELVNRFQGSLSASDRQLPWLPPQSAPSRPVDYQSNTTQEQFCANVL
TAQDYIRAGDIFQVVLSQRLTTHYSGDPFDLYRSLRLINPSPYMAFFRFGDWQLIGSSPE
VMVKAEQDPHQSDRQVATVRPIAGTRPRGRTAPEDAALATDLLADPKEVAEHVMLVDLGR
NDLGRVCEKGSVRVDELMVIERYSHVMHIVSNVVGLLDRDRDAWDLLRATFPAGTVSGAP
KIRAMEIIHELEGCRRGPYSGAYGYYDFEGQLNTAITIRTMIVQAEGSGHRVSVQAGAGV
VADSVPIKEYEETLNKARGLLEAIRCLQPPQVPVAAG
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