SitesBLAST
Comparing CCNA_01972 FitnessBrowser__Caulo:CCNA_01972 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)
44% identity, 93% coverage: 25:502/513 of query aligns to 47:511/524 of A0QX93
- K355 (≠ A329) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 93% coverage: 25:502/513 of query aligns to 27:486/499 of 7bvdA
- active site: Q248 (= Q249), E301 (= E296), A317 (= A312), E341 (= E340), H378 (= H393), T405 (= T420), Y429 (= Y445), R449 (= R465), G465 (= G481), E478 (= E494), K482 (= K498)
- binding pyruvic acid: S93 (≠ Q96), G94 (≠ P97), A100 (≠ S103)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
43% identity, 93% coverage: 25:502/513 of query aligns to 27:490/505 of 5cwaA
- active site: Q248 (= Q249), E301 (= E296), A317 (= A312), E345 (= E340), H382 (= H393), T409 (= T420), Y433 (= Y445), R453 (= R465), G469 (= G481), E482 (= E494), K486 (= K498)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y445), I452 (≠ L464), A466 (= A478), G467 (= G479), K486 (= K498)
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, 94% coverage: 29:512/513 of query aligns to 31:480/489 of O94582
- S390 (= S422) modified: Phosphoserine
- S392 (≠ A424) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
7pi1DDD Aminodeoxychorismate synthase component 1
36% identity, 92% coverage: 34:507/513 of query aligns to 17:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G481), E438 (= E491)
- binding tryptophan: L33 (≠ F50), E34 (= E51), S35 (= S52), G39 (= G56), Y41 (= Y62), P242 (= P278), Y243 (≠ F279), M244 (≠ L280), Q406 (≠ D459), N408 (≠ C461)
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)
36% identity, 92% coverage: 34:507/513 of query aligns to 19:461/470 of P28820
- A283 (= A312) 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)
37% identity, 95% coverage: 22:509/513 of query aligns to 82:588/595 of P32068
- D341 (≠ P263) 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)
37% identity, 94% coverage: 26:509/513 of query aligns to 70:570/577 of Q94GF1
- D323 (≠ P263) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
36% identity, 93% coverage: 31:509/513 of query aligns to 15:509/512 of 1i1qA
- active site: Q259 (= Q249), E305 (= E296), A323 (= A312), E357 (= E340), H394 (= H393), T421 (= T420), Y445 (= Y445), R465 (= R465), G481 (= G481), E494 (= E494), K498 (= K498)
- binding tryptophan: L34 (≠ F50), E35 (= E51), S36 (= S52), K46 (≠ Y62), P287 (= P278), Y288 (≠ F279), M289 (≠ L280), G450 (= G450), C461 (= C461)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
36% identity, 93% coverage: 31:509/513 of query aligns to 19:513/520 of P00898
- E39 (= E51) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S52) binding ; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (≠ V53) mutation to V: Decrease in feedback control by tryptophan.
- K50 (≠ Y62) binding
- R128 (vs. gap) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ I155) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N275) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P276) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L280) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F281) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G292) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N397) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G456) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C461) 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.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
35% identity, 92% coverage: 33:505/513 of query aligns to 18:506/517 of 1i7qA
- active site: Q260 (= Q249), E306 (= E296), A324 (= A312), E358 (= E340), H395 (= H393), T422 (= T420), Y446 (= Y445), R466 (= R465), G482 (= G481), E495 (= E494), K499 (= K498)
- binding magnesium ion: E358 (= E340), E495 (= E494)
- binding pyruvic acid: Y446 (= Y445), I465 (≠ L464), R466 (= R465), A479 (= A478), G480 (= G479), K499 (= K498)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
35% identity, 92% coverage: 33:505/513 of query aligns to 20:508/519 of P00897
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
39% identity, 74% coverage: 128:505/513 of query aligns to 139:500/511 of 1i7sA
- active site: Q254 (= Q249), E300 (= E296), A318 (= A312), E352 (= E340), H389 (= H393), T416 (= T420), Y440 (= Y445), R460 (= R465), G476 (= G481), E489 (= E494), K493 (= K498)
- binding tryptophan: P282 (= P278), Y283 (≠ F279), M284 (≠ L280), V444 (= V449), G445 (= G450), D454 (= D459), C456 (= C461)
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)
31% identity, 90% coverage: 45:504/513 of query aligns to 29:450/453 of P05041
- S36 (= S52) binding
- E258 (= E296) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A312) 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 (= G313) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R349) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R354) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ N376) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H393) 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)
30% identity, 90% coverage: 45:504/513 of query aligns to 27:434/437 of 1k0eA
- active site: E256 (= E296), K272 (≠ A312), E286 (= E340), H323 (= H393), S350 (≠ T420), W374 (≠ Y445), R394 (= R465), G410 (= G481), E423 (= E494), K427 (= K498)
- binding tryptophan: L32 (≠ F50), H33 (≠ E51), S34 (= S52), Y41 (≠ R59), F44 (≠ Y62), P238 (= P278), F239 (= F279), S240 (≠ L280)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 90% coverage: 45:504/513 of query aligns to 29:417/420 of 1k0gA
- active site: E258 (= E296), K274 (= K336), E278 (= E340), S333 (≠ T420), W357 (≠ Y445), R377 (= R465), G393 (= G481), E406 (= E494), K410 (= K498)
- binding phosphate ion: D113 (= D133), R116 (= R136), D347 (= D434), R353 (≠ K440)
- binding tryptophan: L34 (≠ F50), H35 (≠ E51), S36 (= S52), Y43 (≠ R59), S44 (≠ G60), F46 (≠ Y62), P240 (= P278), F241 (= F279), S242 (≠ L280)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 90% coverage: 45:504/513 of query aligns to 29:414/415 of 1k0gB
- active site: E258 (= E296), K274 (≠ A312), E277 (= E340), S330 (≠ T420), W354 (≠ Y445), R374 (= R465), G390 (= G481), E403 (= E494), K407 (= K498)
- binding phosphate ion: Y112 (= Y132), D113 (= D133), R116 (= R136), D344 (= D434), R350 (≠ K440)
- binding tryptophan: L34 (≠ F50), H35 (≠ E51), S36 (= S52), Y43 (≠ R59), S44 (≠ G60), R45 (= R61), F46 (≠ Y62), P240 (= P278), F241 (= F279)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
35% identity, 61% coverage: 191:505/513 of query aligns to 364:669/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 54% coverage: 231:505/513 of query aligns to 372:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I311), K454 (≠ A312), G455 (= G313), T456 (= T314), M547 (≠ L421), Y570 (= Y445), R590 (= R465), V603 (≠ A478), G604 (= G479), G605 (= G480), A606 (≠ G481), E619 (= E494), K623 (= K498)
- binding tryptophan: P419 (= P278), Y420 (≠ F279), G421 (≠ L280), L574 (≠ V449), G575 (= G450)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
30% identity, 55% coverage: 219:498/513 of query aligns to 153:414/424 of 5jy9B
- active site: K183 (≠ Q249), E230 (= E296), A246 (= A312), E274 (= E340), H311 (= H393), T338 (= T420), Y362 (= Y445), R381 (= R465), G397 (= G481), E410 (= E494), K414 (= K498)
- binding fe (ii) ion: E274 (= E340), E410 (= E494)
Query Sequence
>CCNA_01972 FitnessBrowser__Caulo:CCNA_01972
MSLEPAFDAFSEAYDSGRQQVVWTRLIDDLETPVSAYLKIAQARPYSFLFESVEGGAWRG
RYSIVTMNPDLVWRCRGDQAEIAEGDDIAAGRFTPQPGGALDSLRDLVARSRMDLPKGLP
PMAAGVFGALGYDLVRLVERLPDVNPDALNLPDGIMTRPSIVAVFDAIAQEIILTTTVRP
QAGVSAKAAHDAARARIEAVMADLHRPLAHDAPRPPRGPMDFTTPVSRADYAEVVAKAKD
YIAAGDIFQVVASHRFRAPFDLPPFALYRSLRRTNPSPFLFFLNLDGFNLVGSSPEILVR
LRDGKITIRPIAGTRPRGATPEEDAALEAELLADPKERAEHLMLLDLGRNDVGRVAMLNH
HGRNAPPEQARPKGPNVRVTESFTIERYSHVMHIVSNVEGTAPEGVDPVDVLMAALPAGT
LSGAPKVRAMEIIDELEVEKRGISYAGAVGYFGADGAVDTCIVLRTALVKDGMMYVQAGG
GIVADSDPDAEYDETLHKSRALKRAAEEAWRFS
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