SitesBLAST
Comparing Echvi_2504 FitnessBrowser__Cola:Echvi_2504 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
34% identity, 95% coverage: 14:459/469 of query aligns to 46:511/524 of A0QX93
- K355 (≠ T305) 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)
34% identity, 93% coverage: 35:468/469 of query aligns to 30:465/470 of P28820
- A283 (= A288) 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, 93% coverage: 35:468/469 of query aligns to 28:458/459 of 7pi1DDD
- binding magnesium ion: G428 (= G438), E438 (= E448)
- binding tryptophan: L33 (= L40), E34 (= E41), S35 (= S42), G39 (≠ N50), Y41 (= Y52), P242 (= P254), Y243 (= Y255), M244 (≠ L256), Q406 (≠ N416), N408 (≠ A418)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
34% identity, 95% coverage: 14:459/469 of query aligns to 26:490/505 of 5cwaA
- active site: Q248 (= Q225), E301 (= E272), A317 (= A288), E345 (= E316), H382 (= H351), T409 (= T378), Y433 (= Y402), R453 (= R422), G469 (= G438), E482 (= E451), K486 (= K455)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y402), I452 (= I421), A466 (= A435), G467 (= G436), K486 (= K455)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
34% identity, 95% coverage: 14:459/469 of query aligns to 26:486/499 of 7bvdA
- active site: Q248 (= Q225), E301 (= E272), A317 (= A288), E341 (= E316), H378 (= H351), T405 (= T378), Y429 (= Y402), R449 (= R422), G465 (= G438), E478 (= E451), K482 (= K455)
- binding pyruvic acid: S93 (≠ E86), G94 (= G87), A100 (≠ K93)
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, 97% coverage: 13:467/469 of query aligns to 83:589/595 of P32068
- D341 (= D239) 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)
35% identity, 76% coverage: 112:467/469 of query aligns to 172:571/577 of Q94GF1
- D323 (= D239) 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)
32% identity, 97% coverage: 13:469/469 of query aligns to 25:480/489 of O94582
- S390 (= S380) modified: Phosphoserine
- S392 (≠ A382) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
29% identity, 87% coverage: 49:456/469 of query aligns to 40:444/453 of P05041
- E258 (= E272) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A288) 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 (= G289) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R325) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R330) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ E336) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H351) 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:
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
34% identity, 75% coverage: 117:466/469 of query aligns to 148:513/520 of P00898
- C174 (≠ F144) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N251) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P252) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L256) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F257) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G268) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ K355) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G413) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A418) 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.
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
34% identity, 75% coverage: 117:469/469 of query aligns to 144:512/512 of 1i1qA
- active site: Q259 (= Q225), E305 (= E272), A323 (= A288), E357 (= E316), H394 (= H351), T421 (= T378), Y445 (= Y402), R465 (= R422), G481 (= G438), E494 (= E451), K498 (= K455)
- binding tryptophan: P287 (= P254), Y288 (= Y255), M289 (≠ L256), G450 (= G407), C461 (≠ A418)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
28% identity, 95% coverage: 23:466/469 of query aligns to 18:510/517 of 1i7qA
- active site: Q260 (= Q225), E306 (= E272), A324 (= A288), E358 (= E316), H395 (= H351), T422 (= T378), Y446 (= Y402), R466 (= R422), G482 (= G438), E495 (= E451), K499 (= K455)
- binding magnesium ion: E358 (= E316), E495 (= E451)
- binding pyruvic acid: Y446 (= Y402), I465 (= I421), R466 (= R422), A479 (= A435), G480 (= G436), K499 (= K455)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
28% identity, 95% coverage: 23:466/469 of query aligns to 20:512/519 of P00897
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
32% identity, 80% coverage: 92:466/469 of query aligns to 116:504/511 of 1i7sA
- active site: Q254 (= Q225), E300 (= E272), A318 (= A288), E352 (= E316), H389 (= H351), T416 (= T378), Y440 (= Y402), R460 (= R422), G476 (= G438), E489 (= E451), K493 (= K455)
- binding tryptophan: P282 (= P254), Y283 (= Y255), M284 (≠ L256), V444 (≠ I406), G445 (= G407), D454 (≠ N416), C456 (≠ A418)
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
28% identity, 87% coverage: 49:456/469 of query aligns to 38:428/437 of 1k0eA
- active site: E256 (= E272), K272 (≠ A288), E286 (= E316), H323 (= H351), S350 (≠ T378), W374 (≠ Y402), R394 (= R422), G410 (= G438), E423 (= E451), K427 (= K455)
- binding tryptophan: Y41 (= Y52), F44 (vs. gap), P238 (= P254), F239 (≠ Y255), S240 (≠ L256)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 73% coverage: 114:456/469 of query aligns to 108:411/420 of 1k0gA
- active site: E258 (= E272), K274 (= K312), E278 (= E316), S333 (≠ T378), W357 (≠ Y402), R377 (= R422), G393 (= G438), E406 (= E451), K410 (= K455)
- binding phosphate ion: D113 (= D122), R116 (≠ G125), D347 (= D392), R353 (≠ S398)
- binding tryptophan: P240 (= P254), F241 (≠ Y255), S242 (≠ L256)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 73% coverage: 114:456/469 of query aligns to 108:408/415 of 1k0gB
- active site: E258 (= E272), K274 (≠ A288), E277 (= E316), S330 (≠ T378), W354 (≠ Y402), R374 (= R422), G390 (= G438), E403 (= E451), K407 (= K455)
- binding phosphate ion: Y112 (= Y118), D113 (= D122), R116 (≠ G125), D344 (= D392), R350 (≠ S398)
- binding tryptophan: P240 (= P254), F241 (≠ Y255)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
28% identity, 75% coverage: 114:463/469 of query aligns to 266:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I287), K454 (≠ A288), G455 (= G289), T456 (= T290), M547 (≠ L379), Y570 (= Y402), R590 (= R422), V603 (≠ A435), G604 (= G436), G605 (≠ A437), A606 (≠ G438), E619 (= E451), K623 (= K455)
- binding tryptophan: P419 (= P254), Y420 (= Y255), G421 (≠ L256), L574 (≠ I406), G575 (= G407)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
28% identity, 75% coverage: 114:466/469 of query aligns to 308:673/673 of 8hx8A
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
32% identity, 51% coverage: 220:459/469 of query aligns to 178:418/424 of 5jy9B
- active site: K183 (≠ Q225), E230 (= E272), A246 (= A288), E274 (= E316), H311 (= H351), T338 (= T378), Y362 (= Y402), R381 (= R422), G397 (= G438), E410 (= E451), K414 (= K455)
- binding fe (ii) ion: E274 (= E316), E410 (= E451)
Query Sequence
>Echvi_2504 FitnessBrowser__Cola:Echvi_2504
MDTRQHFKINTRYKKLLADTITPVSIYLQVRDKFKNPILLESSDYHGQDNSYSYICFNPM
ATFSFDGKTISETFPEEEKHQFDLKEGEKLVDKLKAFSSRFEEEANDFKFITNGLFGYMQ
YDTVGSFEDITLENTKESNVPQAFYAVYKNVIVVDHFKNELHIFDYHVNGEDDRVREIET
LLNNRNIPTYSFKLDGEETSNYTDNQFLDILRQGREHCFKGDVFQIVLSRCFTTGFKGDE
FNVYRALRSVNPSPYLFYFDYGSYKVFGSSPEAQIVVKGRKATIYPIAGTFKRTGNDLAD
AELATKLYDDPKENSEHVMLVDLARNDLSRSSEKVEVEVFKEIQYYSHVIHLVSKVTGVL
PETANPLQLVADTFPAGTLSGAPKYRAMEIIDKLENTSRKFYGGAIGFLGFNGDFNHAIL
IRSFVSENNRLRFQAGAGVVAKSSIESELQEVTNKLQALRVALKAAEQV
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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