SitesBLAST
Comparing 5209432 FitnessBrowser__PV4:5209432 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)
55% identity, 98% coverage: 10:475/477 of query aligns to 7:451/453 of P05041
- S36 (= S38) binding
- E258 (= E282) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K298) 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 (= G299) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R335) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ K340) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S346) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H363) 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)
54% identity, 98% coverage: 10:475/477 of query aligns to 5:435/437 of 1k0eA
- active site: E256 (= E282), K272 (= K298), E286 (= E326), H323 (= H363), S350 (= S390), W374 (≠ Y414), R394 (= R434), G410 (= G450), E423 (= E463), K427 (= K467)
- binding tryptophan: L32 (= L36), H33 (≠ D37), S34 (= S38), Y41 (≠ D45), F44 (≠ Y48), P238 (= P264), F239 (= F265), S240 (= S266)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
51% identity, 98% coverage: 10:475/477 of query aligns to 7:418/420 of 1k0gA
- active site: E258 (= E282), K274 (= K298), E278 (= E326), S333 (= S390), W357 (≠ Y414), R377 (= R434), G393 (= G450), E406 (= E463), K410 (= K467)
- binding phosphate ion: D113 (= D128), R116 (= R131), D347 (≠ E404), R353 (= R410)
- binding tryptophan: L34 (= L36), H35 (≠ D37), S36 (= S38), Y43 (≠ D45), S44 (≠ A46), F46 (≠ Y48), P240 (= P264), F241 (= F265), S242 (= S266)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
51% identity, 98% coverage: 10:475/477 of query aligns to 7:415/415 of 1k0gB
- active site: E258 (= E282), K274 (= K298), E277 (= E326), S330 (= S390), W354 (≠ Y414), R374 (= R434), G390 (= G450), E403 (= E463), K407 (= K467)
- binding phosphate ion: Y112 (= Y127), D113 (= D128), R116 (= R131), D344 (≠ E404), R350 (= R410)
- binding tryptophan: L34 (= L36), H35 (≠ D37), S36 (= S38), Y43 (≠ D45), S44 (≠ A46), R45 (= R47), F46 (≠ Y48), P240 (= P264), F241 (= F265)
7pi1DDD Aminodeoxychorismate synthase component 1
35% identity, 91% coverage: 34:467/477 of query aligns to 31:445/459 of 7pi1DDD
- binding magnesium ion: G428 (= G450), E438 (= E460)
- binding tryptophan: L33 (= L36), E34 (≠ D37), S35 (= S38), G39 (≠ A46), Y41 (= Y48), P242 (= P264), Y243 (≠ F265), M244 (≠ S266), Q406 (≠ D428), N408 (≠ S430)
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)
35% identity, 91% coverage: 34:467/477 of query aligns to 33:452/470 of P28820
- A283 (≠ K298) 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.
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)
32% identity, 89% coverage: 46:471/477 of query aligns to 126:581/595 of P32068
- D341 (= D249) 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)
33% identity, 93% coverage: 28:472/477 of query aligns to 64:512/524 of A0QX93
- K355 (≠ E315) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
35% identity, 80% coverage: 91:472/477 of query aligns to 93:487/499 of 7bvdA
- active site: Q248 (= Q235), E301 (= E282), A317 (≠ K298), E341 (= E326), H378 (= H363), T405 (≠ S390), Y429 (= Y414), R449 (= R434), G465 (= G450), E478 (= E463), K482 (= K467)
- binding pyruvic acid: S93 (= S91), G94 (≠ Q92), A100 (≠ I98)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 79% coverage: 94:471/477 of query aligns to 147:563/577 of Q94GF1
- D323 (= D249) 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)
33% identity, 79% coverage: 94:472/477 of query aligns to 97:491/505 of 5cwaA
- active site: Q248 (= Q235), E301 (= E282), A317 (≠ K298), E345 (= E326), H382 (= H363), T409 (≠ S390), Y433 (= Y414), R453 (= R434), G469 (= G450), E482 (= E463), K486 (= K467)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y414), I452 (= I433), A466 (= A447), G467 (= G448), K486 (= K467)
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, 79% coverage: 92:468/477 of query aligns to 79:467/489 of O94582
- S390 (≠ T392) modified: Phosphoserine
- S392 (≠ A394) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
41% identity, 55% coverage: 214:475/477 of query aligns to 369:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I297), K454 (= K298), G455 (= G299), T456 (= T300), M547 (≠ I391), Y570 (= Y414), R590 (= R434), V603 (≠ A447), G604 (= G448), G605 (= G449), A606 (≠ G450), E619 (= E463), K623 (= K467)
- binding tryptophan: P419 (= P264), Y420 (≠ F265), G421 (≠ S266), L574 (≠ I418), G575 (= G419)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
41% identity, 55% coverage: 214:475/477 of query aligns to 408:670/673 of 8hx8A
Sites not aligning to the query:
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
29% identity, 80% coverage: 90:472/477 of query aligns to 117:503/512 of 1i1qA
- active site: Q259 (= Q235), E305 (= E282), A323 (≠ K298), E357 (= E326), H394 (= H363), T421 (≠ S390), Y445 (= Y414), R465 (= R434), G481 (= G450), E494 (= E463), K498 (= K467)
- binding tryptophan: P287 (= P264), Y288 (≠ F265), M289 (≠ S266), G450 (= G419), C461 (≠ S430)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
30% identity, 73% coverage: 123:472/477 of query aligns to 147:506/519 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)
29% identity, 80% coverage: 90:472/477 of query aligns to 121:507/520 of P00898
- R128 (≠ S97) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ N150) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N261) mutation to D: Decrease in feedback control by tryptophan.
- P289 (≠ K262) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S266) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A267) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S278) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T367) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (≠ R425) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S430) 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
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
30% identity, 73% coverage: 123:472/477 of query aligns to 145:504/517 of 1i7qA
- active site: Q260 (= Q235), E306 (= E282), A324 (≠ K298), E358 (= E326), H395 (= H363), T422 (≠ S390), Y446 (= Y414), R466 (= R434), G482 (= G450), E495 (= E463), K499 (= K467)
- binding magnesium ion: E358 (= E326), E495 (= E463)
- binding pyruvic acid: Y446 (= Y414), I465 (= I433), R466 (= R434), A479 (= A447), G480 (= G448), K499 (= K467)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
30% identity, 73% coverage: 123:472/477 of query aligns to 139:498/511 of 1i7sA
- active site: Q254 (= Q235), E300 (= E282), A318 (≠ K298), E352 (= E326), H389 (= H363), T416 (≠ S390), Y440 (= Y414), R460 (= R434), G476 (= G450), E489 (= E463), K493 (= K467)
- binding tryptophan: P282 (= P264), Y283 (≠ F265), M284 (≠ S266), V444 (≠ I418), G445 (= G419), D454 (= D428), C456 (≠ S430)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
27% identity, 54% coverage: 217:475/477 of query aligns to 165:422/424 of 5jy9B
- active site: K183 (≠ Q235), E230 (= E282), A246 (≠ K298), E274 (= E326), H311 (= H363), T338 (≠ S390), Y362 (= Y414), R381 (= R434), G397 (= G450), E410 (= E463), K414 (= K467)
- binding fe (ii) ion: E274 (= E326), E410 (= E463)
Query Sequence
>5209432 FitnessBrowser__PV4:5209432
MDFSSTQGVALQKLDWQLSTIEVFDCFAHLPWAILLDSAGADHIDARYDIISFDPLATIT
SQDGVTHTRHLRPTAASATEENQSKDGVEISQDDPLSILQAAIADYFPTQHACELPFSGG
ALGTFSYDLGRRIEKLPTIAAQDIELPEMNIGLYDWALLFCYQSQTWSLVHYRGETALKE
RLADLEARLSSPSNEKANGEKFALSRDWQPQITKGEYRDKFDRVQDYLHSGDCYQINLTQ
RFEAEYRGDEWQAYLKLRASNKAPFSAFIRLDMHAILSISPERFIKLKGDAIETKPIKGT
MARSSDATADKAAAEALAASEKDRAENLMIVDLLRNDIGKVASPGSVRVPHLFAIESFPA
VHHLVSTVTANLAAPNSPCDLLRAAFPGGSITGAPKIRAMEIIEELEPSRRSLYCGSIGY
ISQDRQMDTSITIRTLVAEPPRLYCWAGGGIVADSQVDAEYQESYDKVSKILPVLSN
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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