SitesBLAST
Comparing WP_020175711.1 NCBI__GCF_000385335.1:WP_020175711.1 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)
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, 92% coverage: 24:486/505 of query aligns to 47:510/524 of A0QX93
- K355 (≠ A331) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 92% coverage: 24:486/505 of query aligns to 27:485/499 of 7bvdA
- active site: Q248 (= Q251), E301 (= E298), A317 (= A314), E341 (= E342), H378 (= H379), T405 (= T406), Y429 (= Y430), R449 (= R450), G465 (= G466), E478 (= E479), K482 (= K483)
- binding pyruvic acid: S93 (≠ C96), G94 (≠ D97), A100 (≠ S103)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
43% identity, 92% coverage: 21:486/505 of query aligns to 24:489/505 of 5cwaA
- active site: Q248 (= Q251), E301 (= E298), A317 (= A314), E345 (= E342), H382 (= H379), T409 (= T406), Y433 (= Y430), R453 (= R450), G469 (= G466), E482 (= E479), K486 (= K483)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y430), I452 (≠ L449), A466 (= A463), G467 (= G464), K486 (= K483)
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)
40% identity, 91% coverage: 33:492/505 of query aligns to 19:461/470 of P28820
- A283 (= A314) 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
39% identity, 91% coverage: 33:492/505 of query aligns to 17:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G466), E438 (= E476)
- binding tryptophan: L33 (= L50), E34 (= E51), S35 (= S52), G39 (= G56), Y41 (= Y62), P242 (= P280), Y243 (≠ F281), M244 (≠ L282), Q406 (≠ D444), N408 (≠ C446)
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, 93% coverage: 27:497/505 of query aligns to 30:480/489 of O94582
- S390 (= S408) modified: Phosphoserine
- S392 (≠ A410) 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)
39% identity, 93% coverage: 25:494/505 of query aligns to 70:570/577 of Q94GF1
- D323 (≠ L264) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
38% identity, 93% coverage: 25:494/505 of query aligns to 86:588/595 of P32068
- D341 (≠ L264) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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: 128:494/505 of query aligns to 148:513/520 of P00898
- C174 (≠ F155) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N277) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P278) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L282) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ C283) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ C294) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N383) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G441) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C446) 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 L-tryptophan; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding L-tryptophan
- 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)
38% identity, 73% coverage: 128:494/505 of query aligns to 144:509/512 of 1i1qA
- active site: Q259 (= Q251), E305 (= E298), A323 (= A314), E357 (= E342), H394 (= H379), T421 (= T406), Y445 (= Y430), R465 (= R450), G481 (= G466), E494 (= E479), K498 (= K483)
- binding tryptophan: P287 (= P280), Y288 (≠ F281), M289 (≠ L282), G450 (= G435), C461 (= C446)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
38% identity, 72% coverage: 128:490/505 of query aligns to 145:506/517 of 1i7qA
- active site: Q260 (= Q251), E306 (= E298), A324 (= A314), E358 (= E342), H395 (= H379), T422 (= T406), Y446 (= Y430), R466 (= R450), G482 (= G466), E495 (= E479), K499 (= K483)
- binding magnesium ion: E358 (= E342), E495 (= E479)
- binding pyruvic acid: Y446 (= Y430), I465 (≠ L449), R466 (= R450), A479 (= A463), G480 (= G464), K499 (= K483)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
38% identity, 72% coverage: 128:490/505 of query aligns to 139:500/511 of 1i7sA
- active site: Q254 (= Q251), E300 (= E298), A318 (= A314), E352 (= E342), H389 (= H379), T416 (= T406), Y440 (= Y430), R460 (= R450), G476 (= G466), E489 (= E479), K493 (= K483)
- binding tryptophan: P282 (= P280), Y283 (≠ F281), M284 (≠ L282), V444 (≠ I434), G445 (= G435), D454 (= D444), C456 (= C446)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
37% identity, 77% coverage: 101:490/505 of query aligns to 123:508/519 of P00897
- PYM 290:292 (≠ PFL 280:282) binding L-tryptophan
- E360 (= E342) binding Mg(2+)
- E497 (= E479) binding Mg(2+)
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)
33% identity, 78% coverage: 100:493/505 of query aligns to 79:453/453 of P05041
- E258 (= E298) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A314) 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 (= G315) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R351) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R356) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T362) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H379) 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:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 78% coverage: 100:493/505 of query aligns to 77:437/437 of 1k0eA
- active site: E256 (= E298), K272 (≠ A314), E286 (= E342), H323 (= H379), S350 (≠ T406), W374 (≠ Y430), R394 (= R450), G410 (= G466), E423 (= E479), K427 (= K483)
- binding tryptophan: P238 (= P280), F239 (= F281), S240 (≠ L282)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
39% identity, 53% coverage: 225:490/505 of query aligns to 403:669/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
39% identity, 53% coverage: 225:490/505 of query aligns to 364:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I313), K454 (≠ A314), G455 (= G315), T456 (= T316), M547 (≠ V407), Y570 (= Y430), R590 (= R450), V603 (≠ A463), G604 (= G464), G605 (≠ A465), A606 (≠ G466), E619 (= E479), K623 (= K483)
- binding tryptophan: P419 (= P280), Y420 (≠ F281), G421 (≠ L282), L574 (≠ I434), G575 (= G435)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 78% coverage: 100:493/505 of query aligns to 79:420/420 of 1k0gA
- active site: E258 (= E298), K274 (= K338), E278 (= E342), S333 (≠ T406), W357 (≠ Y430), R377 (= R450), G393 (= G466), E406 (= E479), K410 (= K483)
- binding phosphate ion: D113 (= D133), R116 (= R136), D347 (= D420), R353 (≠ K426)
- binding tryptophan: P240 (= P280), F241 (= F281), S242 (≠ L282)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 76% coverage: 100:485/505 of query aligns to 79:409/415 of 1k0gB
- active site: E258 (= E298), K274 (≠ A314), E277 (= E342), S330 (≠ T406), W354 (≠ Y430), R374 (= R450), G390 (= G466), E403 (= E479), K407 (= K483)
- binding phosphate ion: Y112 (= Y132), D113 (= D133), R116 (= R136), D344 (= D420), R350 (≠ K426)
- binding tryptophan: P240 (= P280), F241 (= F281)
Sites not aligning to the query:
8qc4A Salicylate synthase (see paper)
34% identity, 49% coverage: 224:468/505 of query aligns to 161:411/438 of 8qc4A
Sites not aligning to the query:
Query Sequence
>WP_020175711.1 NCBI__GCF_000385335.1:WP_020175711.1
MIDPPYDLFAKRYEAGTSCLVSTKLIADLETPISAFLKLSAGRQGLIFLLESIEGGVVRG
RYSMIGLDPDVLWRAQGDKAEINRQALKDRTDFKPCDAPPLESLRAFVAESRIDAGEELP
PMAAGVFGYLGYDMVRQMEHLAPAKPDPIGVPDAFMMRPTVMLVFDTVKDEMTLVTPVRP
ADGVSAKSAYEAAIERIDAIVLTLEGPLSHEGSAADPYLLTAPPQSNTDETRFYDMVERA
KAYIRAGDIFQVVLSQRFTTPFALPAFALYRALRRVNPAPFLCYLDFDAFQIVCSSPEIL
VRVRDGKVTIRPIAGTRWRGKTSAEDLALEAELLADEKECAEHLMLLDLGRNDVGRVAEI
GTVEVTDRFSIERYSHVMHIVSNVEGRLDASHDAIDALCAGFPAGTVSGAPKIRAMEIID
ELEVDKRGIYAGCIGYFGASGEMDTCIVLRTSVVKDGFMHVQAGAGIVYDSDPAYEQREC
VNKAKAQFRAAEEAVKFATRPKRGQ
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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