SitesBLAST
Comparing NP_662334.1 NCBI__GCF_000006985.1:NP_662334.1 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)
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)
40% identity, 95% coverage: 22:501/504 of query aligns to 23:478/489 of O94582
- S390 (≠ T414) modified: Phosphoserine
- S392 (≠ A416) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
42% identity, 94% coverage: 20:495/504 of query aligns to 41:513/524 of A0QX93
- K355 (= K337) 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)
39% identity, 94% coverage: 27:498/504 of query aligns to 13:461/470 of P28820
- A283 (= A320) 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
40% identity, 94% coverage: 27:498/504 of query aligns to 11:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G472), E438 (= E482)
- binding tryptophan: L33 (= L49), E34 (= E50), S35 (= S51), G39 (≠ A59), Y41 (= Y61), P242 (= P281), Y243 (= Y282), M244 (≠ L283), Q406 (≠ N450), N408 (≠ A452)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
42% identity, 94% coverage: 20:495/504 of query aligns to 21:492/505 of 5cwaA
- active site: Q248 (= Q252), E301 (= E299), A317 (= A320), E345 (= E348), H382 (= H385), T409 (= T412), Y433 (= Y436), R453 (= R456), G469 (= G472), E482 (= E485), K486 (= K489)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y436), I452 (= I455), A466 (= A469), G467 (≠ A470), K486 (= K489)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
42% identity, 94% coverage: 20:495/504 of query aligns to 21:488/499 of 7bvdA
- active site: Q248 (= Q252), E301 (= E299), A317 (= A320), E341 (= E348), H378 (= H385), T405 (= T412), Y429 (= Y436), R449 (= R456), G465 (= G472), E478 (= E485), K482 (= K489)
- binding pyruvic acid: S93 (≠ D101), G94 (vs. gap), A100 (vs. gap)
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, 98% coverage: 2:494/504 of query aligns to 63:581/595 of P32068
- D341 (≠ R266) 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, 96% coverage: 20:504/504 of query aligns to 63:575/577 of Q94GF1
- D323 (≠ R266) mutation to N: Insensitive to feedback inhibition by tryptophan.
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
38% identity, 73% coverage: 135:503/504 of query aligns to 148:520/520 of P00898
- C174 (= C163) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N278) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P279) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L283) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y284) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G295) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N389) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G447) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A452) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (≠ E498) 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, 72% coverage: 135:499/504 of query aligns to 144:508/512 of 1i1qA
- active site: Q259 (= Q252), E305 (= E299), A323 (= A320), E357 (= E348), H394 (= H385), T421 (= T412), Y445 (= Y436), R465 (= R456), G481 (= G472), E494 (= E485), K498 (= K489)
- binding tryptophan: P287 (= P281), Y288 (= Y282), M289 (≠ L283), G450 (= G441), C461 (≠ A452)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 96% coverage: 15:499/504 of query aligns to 2:509/517 of 1i7qA
- active site: Q260 (= Q252), E306 (= E299), A324 (= A320), E358 (= E348), H395 (= H385), T422 (= T412), Y446 (= Y436), R466 (= R456), G482 (= G472), E495 (= E485), K499 (= K489)
- binding magnesium ion: E358 (= E348), E495 (= E485)
- binding pyruvic acid: Y446 (= Y436), I465 (= I455), R466 (= R456), A479 (= A469), G480 (≠ A470), K499 (= K489)
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, 90% coverage: 44:498/504 of query aligns to 29:452/453 of P05041
- S36 (= S51) binding
- E258 (= E299) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A320) 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 (= G321) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R357) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R362) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T368) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H385) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
32% identity, 96% coverage: 15:499/504 of query aligns to 4:511/519 of P00897
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
33% identity, 96% coverage: 15:499/504 of query aligns to 2:503/511 of 1i7sA
- active site: Q254 (= Q252), E300 (= E299), A318 (= A320), E352 (= E348), H389 (= H385), T416 (= T412), Y440 (= Y436), R460 (= R456), G476 (= G472), E489 (= E485), K493 (= K489)
- binding tryptophan: L35 (= L49), E36 (= E50), S37 (= S51), P282 (= P281), Y283 (= Y282), M284 (≠ L283), V444 (= V440), G445 (= G441), D454 (≠ N450), C456 (≠ A452)
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 90% coverage: 44:498/504 of query aligns to 27:436/437 of 1k0eA
- active site: E256 (= E299), K272 (≠ A320), E286 (= E348), H323 (= H385), S350 (≠ T412), W374 (≠ Y436), R394 (= R456), G410 (= G472), E423 (= E485), K427 (= K489)
- binding tryptophan: L32 (= L49), H33 (≠ E50), S34 (= S51), Y41 (≠ M58), F44 (≠ Y61), P238 (= P281), F239 (≠ Y282), S240 (≠ L283)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
34% identity, 73% coverage: 132:498/504 of query aligns to 266:632/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I319), K454 (≠ A320), G455 (= G321), T456 (= T322), M547 (≠ L413), Y570 (= Y436), R590 (= R456), V603 (≠ A469), G604 (≠ A470), G605 (= G471), A606 (≠ G472), E619 (= E485), K623 (= K489)
- binding tryptophan: P419 (= P281), Y420 (= Y282), G421 (≠ L283), L574 (≠ V440), G575 (= G441)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
33% identity, 73% coverage: 132:499/504 of query aligns to 308:672/673 of 8hx8A
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 90% coverage: 44:498/504 of query aligns to 29:419/420 of 1k0gA
- active site: E258 (= E299), K274 (= K344), E278 (= E348), S333 (≠ T412), W357 (≠ Y436), R377 (= R456), G393 (= G472), E406 (= E485), K410 (= K489)
- binding phosphate ion: D113 (= D140), R116 (≠ H143), D347 (≠ Y426), R353 (≠ K432)
- binding tryptophan: L34 (= L49), H35 (≠ E50), S36 (= S51), Y43 (≠ M58), S44 (≠ A59), F46 (≠ Y61), P240 (= P281), F241 (≠ Y282), S242 (≠ L283)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 90% coverage: 44:497/504 of query aligns to 29:415/415 of 1k0gB
- active site: E258 (= E299), K274 (≠ A320), E277 (= E348), S330 (≠ T412), W354 (≠ Y436), R374 (= R456), G390 (= G472), E403 (= E485), K407 (= K489)
- binding phosphate ion: Y112 (= Y139), D113 (= D140), R116 (≠ H143), D344 (≠ Y426), R350 (≠ K432)
- binding tryptophan: L34 (= L49), H35 (≠ E50), S36 (= S51), Y43 (≠ M58), S44 (≠ A59), R45 (= R60), F46 (≠ Y61), P240 (= P281), F241 (≠ Y282)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
30% identity, 61% coverage: 183:490/504 of query aligns to 132:415/424 of 5jy9B
- active site: K183 (≠ Q252), E230 (= E299), A246 (= A320), E274 (= E348), H311 (= H385), T338 (= T412), Y362 (= Y436), R381 (= R456), G397 (= G472), E410 (= E485), K414 (= K489)
- binding fe (ii) ion: E274 (= E348), E410 (= E485)
Query Sequence
>NP_662334.1 NCBI__GCF_000006985.1:NP_662334.1
MIRSFSDNTADPAKEPSFILTPLVRTFQADTETPVSVYLKLQRPYSCLLESVEGEERMAR
YSYIAVDPVAVLKGTVGGEILLDVRDERFRQLSAIVEQERDLRAVVDRCMAMFSSEKLPR
HKSGSQQMSTSGVFGYFGYDTMHLIEKIPAAEQPDPAGMPDLCLLFCDTLVIFDNVMRKL
FLVTNYLDAADRTRADRKIDELAALLQKPLVPALVPFQPEKPEPVISNTTRDEYYAKVLK
AKEYILSGDIFQVQISQRLKRKLHTRPFDVYRALRTINPSPYLYFFDFEDFHVVGSSPEL
LVKVERDHTGRRMVDTRPIAGTRRRGESFEEDERNAKELISDEKERAEHLMLIDLSRNDI
GRIAKIGTVETNEMMVIEKYSHVMHIVSNVRGELQDGLTAMDAFWSCFPAGTLTGAPKVR
AMEIIYELEKEKRGLYGGAVGYLDFRGQLNTAIAIRTMVIRDGVIYFQAAGGIVADSTPE
FEYEETMNKMRAGLTALESIETFV
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