SitesBLAST
Comparing WP_006746915.1 NCBI__GCF_000227685.2:WP_006746915.1 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, 96% coverage: 4:478/493 of query aligns to 30:512/524 of A0QX93
- K355 (≠ A321) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 97% coverage: 5:482/493 of query aligns to 9:475/489 of O94582
- S390 (= S398) modified: Phosphoserine
- S392 (≠ A400) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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, 95% coverage: 15:484/493 of query aligns to 3:463/470 of P28820
- A283 (= A304) 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, 95% coverage: 15:484/493 of query aligns to 1:456/459 of 7pi1DDD
- binding magnesium ion: G428 (= G456), E438 (= E466)
- binding tryptophan: L33 (≠ F46), E34 (= E47), S35 (= S48), G39 (= G52), Y41 (= Y58), P242 (= P270), Y243 (= Y271), M244 (= M272), Q406 (≠ D434), N408 (≠ A436)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
43% identity, 96% coverage: 4:478/493 of query aligns to 10:491/505 of 5cwaA
- active site: Q248 (= Q241), E301 (= E288), A317 (= A304), E345 (= E332), H382 (= H369), T409 (= T396), Y433 (= Y420), R453 (= R440), G469 (= G456), E482 (= E469), K486 (= K473)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y420), I452 (= I439), A466 (= A453), G467 (= G454), K486 (= K473)
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)
39% identity, 96% coverage: 10:484/493 of query aligns to 73:588/595 of P32068
- D341 (≠ P255) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 97% coverage: 4:479/493 of query aligns to 10:488/499 of 7bvdA
- active site: Q248 (= Q241), E301 (= E288), A317 (= A304), E341 (= E332), H378 (= H369), T405 (= T396), Y429 (= Y420), R449 (= R440), G465 (= G456), E478 (= E469), K482 (= K473)
- binding pyruvic acid: S93 (≠ E89), G94 (≠ H90), A100 (≠ W96)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 97% coverage: 5:484/493 of query aligns to 52:570/577 of Q94GF1
- D323 (≠ P255) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
40% identity, 75% coverage: 115:484/493 of query aligns to 141:509/512 of 1i1qA
- active site: Q259 (= Q241), E305 (= E288), A323 (= A304), E357 (= E332), H394 (= H369), T421 (= T396), Y445 (= Y420), R465 (= R440), G481 (= G456), E494 (= E469), K498 (= K473)
- binding tryptophan: P287 (= P270), Y288 (= Y271), M289 (= M272), G450 (= G425), C461 (≠ A436)
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)
40% identity, 75% coverage: 115:484/493 of query aligns to 145:513/520 of P00898
- C174 (≠ L144) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N267) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P268) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M272) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F273) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G284) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N373) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G431) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A436) 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.
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, 94% coverage: 18:482/493 of query aligns to 6:452/453 of P05041
- S36 (= S48) binding L-tryptophan
- E258 (= E288) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A304) 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 (= G305) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R341) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R346) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T352) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H369) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
38% identity, 75% coverage: 117:484/493 of query aligns to 138:504/511 of 1i7sA
- active site: Q254 (= Q241), E300 (= E288), A318 (= A304), E352 (= E332), H389 (= H369), T416 (= T396), Y440 (= Y420), R460 (= R440), G476 (= G456), E489 (= E469), K493 (= K473)
- binding tryptophan: P282 (= P270), Y283 (= Y271), M284 (= M272), V444 (= V424), G445 (= G425), D454 (= D434), C456 (≠ A436)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
38% identity, 75% coverage: 117:484/493 of query aligns to 144:510/517 of 1i7qA
- active site: Q260 (= Q241), E306 (= E288), A324 (= A304), E358 (= E332), H395 (= H369), T422 (= T396), Y446 (= Y420), R466 (= R440), G482 (= G456), E495 (= E469), K499 (= K473)
- binding magnesium ion: E358 (= E332), E495 (= E469)
- binding pyruvic acid: Y446 (= Y420), I465 (= I439), R466 (= R440), A479 (= A453), G480 (= G454), K499 (= K473)
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 94% coverage: 18:482/493 of query aligns to 4:436/437 of 1k0eA
- active site: E256 (= E288), K272 (≠ A304), E286 (= E332), H323 (= H369), S350 (≠ T396), W374 (≠ Y420), R394 (= R440), G410 (= G456), E423 (= E469), K427 (= K473)
- binding tryptophan: L32 (≠ F46), H33 (≠ E47), S34 (= S48), Y41 (≠ W55), F44 (≠ Y58), P238 (= P270), F239 (≠ Y271), S240 (≠ M272)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
37% identity, 75% coverage: 117:484/493 of query aligns to 146:512/519 of P00897
- PYM 290:292 (= PYM 270:272) binding L-tryptophan
- E360 (= E332) binding Mg(2+)
- E497 (= E469) binding Mg(2+)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 78% coverage: 96:480/493 of query aligns to 243:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I303), K454 (≠ A304), G455 (= G305), T456 (= T306), M547 (≠ V397), Y570 (= Y420), R590 (= R440), V603 (≠ A453), G604 (= G454), G605 (≠ A455), A606 (≠ G456), E619 (= E469), K623 (= K473)
- binding tryptophan: P419 (= P270), Y420 (= Y271), G421 (≠ M272), L574 (≠ V424), G575 (= G425)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 78% coverage: 96:480/493 of query aligns to 285:669/673 of 8hx8A
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 94% coverage: 18:482/493 of query aligns to 6:419/420 of 1k0gA
- active site: E258 (= E288), K274 (= K328), E278 (= E332), S333 (≠ T396), W357 (≠ Y420), R377 (= R440), G393 (= G456), E406 (= E469), K410 (= K473)
- binding phosphate ion: D113 (≠ E126), R116 (≠ Q129), D347 (= D410), R353 (≠ K416)
- binding tryptophan: L34 (≠ F46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), F46 (≠ Y58), P240 (= P270), F241 (≠ Y271), S242 (≠ M272)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 94% coverage: 18:479/493 of query aligns to 6:413/415 of 1k0gB
- active site: E258 (= E288), K274 (≠ A304), E277 (= E332), S330 (≠ T396), W354 (≠ Y420), R374 (= R440), G390 (= G456), E403 (= E469), K407 (= K473)
- binding phosphate ion: Y112 (≠ F125), D113 (≠ E126), R116 (≠ Q129), D344 (= D410), R350 (≠ K416)
- binding tryptophan: L34 (≠ F46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), R45 (= R57), F46 (≠ Y58), P240 (= P270), F241 (≠ Y271)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
32% identity, 51% coverage: 221:473/493 of query aligns to 147:398/408 of 2fn1A
- active site: K167 (≠ Q241), E214 (= E288), A230 (= A304), E258 (= E332), H295 (= H369), T322 (= T396), Y346 (= Y420), R365 (= R440), G381 (= G456), E394 (= E469), K398 (= K473)
- binding magnesium ion: E258 (= E332), E394 (= E469)
- binding pyruvic acid: Y346 (= Y420), L364 (≠ I439), R365 (= R440), A378 (= A453), G379 (= G454), K398 (= K473)
Query Sequence
>WP_006746915.1 NCBI__GCF_000227685.2:WP_006746915.1
MTPDQFDRLADEGHNRIPLVREVLADLDTPLSVFLRLANQPYSYLFESVQGGEKWGRYSF
IGLPARTLVRIRGHAIEVERAGTVVESLEHDDPLAWIESFQARYRVPDLGGMPRFTGGLV
GYFGFETVQLIEPRLAGKDKPDALGLPDILLMVSDEVVVFDNLAGRLYLVVHADATRPDG
QAEASARLDRLETRLLEPLARAEPHMRPHAMPEYLAGWPADEFKAAVARAQRYIVDGDVM
QVVLAQRMSVPFSAPPLDLYRALRGLNPSPYMFYMDLGDHHVVGASPEILVRLEDDRVTV
RPIAGTRPRGRSEQEDQALEADLLADPKERAEHLMLIDLGRNDVGRVSRTGTVRVTDTMV
VERYSHVMHIVSNVEGELQPGLSAMDVLRAAFPAGTVSGAPKIRALEIIDELEPVKRGIY
AGAVGYLSWSGNMDTAIAIRTAVLHDGVLHIQAGAGVVHDSVPENEWQETLNKGRAVVRA
AEMAIGGLGPRRD
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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