SitesBLAST
Comparing WP_011606086.1 NCBI__GCF_000058485.1:WP_011606086.1 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)
56% identity, 96% coverage: 10:500/512 of query aligns to 29:513/524 of A0QX93
- K355 (≠ A342) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
55% identity, 96% coverage: 10:500/512 of query aligns to 9:492/505 of 5cwaA
- active site: Q248 (= Q262), E301 (= E309), A317 (= A325), E345 (= E353), H382 (= H390), T409 (= T417), Y433 (= Y441), R453 (= R461), G469 (= G477), E482 (= E490), K486 (= K494)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y441), I452 (= I460), A466 (= A474), G467 (= G475), K486 (= K494)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
55% identity, 96% coverage: 10:500/512 of query aligns to 9:488/499 of 7bvdA
- active site: Q248 (= Q262), E301 (= E309), A317 (= A325), E341 (= E353), H378 (= H390), T405 (= T417), Y429 (= Y441), R449 (= R461), G465 (= G477), E478 (= E490), K482 (= K494)
- binding pyruvic acid: S93 (≠ T94), G94 (≠ E95), A100 (≠ I101)
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)
41% identity, 89% coverage: 51:506/512 of query aligns to 34:464/470 of P28820
- A283 (= A325) 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
41% identity, 89% coverage: 51:506/512 of query aligns to 32:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G477), E438 (= E487)
- binding tryptophan: L33 (= L52), E34 (= E53), S35 (= S54), G39 (= G58), Y41 (= Y64), P242 (= P291), Y243 (= Y292), M244 (= M293), Q406 (≠ D455), N408 (≠ A457)
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, 98% coverage: 6:507/512 of query aligns to 63:590/595 of P32068
- D341 (= D276) 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)
39% identity, 98% coverage: 6:507/512 of query aligns to 46:572/577 of Q94GF1
- D323 (= D276) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
38% identity, 93% coverage: 31:508/512 of query aligns to 30:480/489 of O94582
- S390 (= S419) modified: Phosphoserine
- S392 (≠ A421) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
41% identity, 74% coverage: 126:506/512 of query aligns to 148:514/520 of P00898
- C174 (≠ R153) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N288) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P289) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M293) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y294) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G305) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T394) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G452) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A457) 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)
41% identity, 74% coverage: 126:506/512 of query aligns to 144:510/512 of 1i1qA
- active site: Q259 (= Q262), E305 (= E309), A323 (= A325), E357 (= E353), H394 (= H390), T421 (= T417), Y445 (= Y441), R465 (= R461), G481 (= G477), E494 (= E490), K498 (= K494)
- binding tryptophan: P287 (= P291), Y288 (= Y292), M289 (= M293), G450 (= G446), C461 (≠ A457)
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)
32% identity, 91% coverage: 40:503/512 of query aligns to 22:452/453 of P05041
- S36 (= S54) binding L-tryptophan
- E258 (= E309) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A325) 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 (= G326) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R362) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R367) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S373) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H390) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
34% identity, 92% coverage: 36:506/512 of query aligns to 18:511/517 of 1i7qA
- active site: Q260 (= Q262), E306 (= E309), A324 (= A325), E358 (= E353), H395 (= H390), T422 (= T417), Y446 (= Y441), R466 (= R461), G482 (= G477), E495 (= E490), K499 (= K494)
- binding magnesium ion: E358 (= E353), E495 (= E490)
- binding pyruvic acid: Y446 (= Y441), I465 (= I460), R466 (= R461), A479 (= A474), G480 (= G475), K499 (= K494)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
34% identity, 92% coverage: 36:506/512 of query aligns to 18:505/511 of 1i7sA
- active site: Q254 (= Q262), E300 (= E309), A318 (= A325), E352 (= E353), H389 (= H390), T416 (= T417), Y440 (= Y441), R460 (= R461), G476 (= G477), E489 (= E490), K493 (= K494)
- binding tryptophan: L35 (= L52), E36 (= E53), S37 (= S54), P282 (= P291), Y283 (= Y292), M284 (= M293), V444 (= V445), G445 (= G446), D454 (= D455), C456 (≠ A457)
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
31% identity, 91% coverage: 40:503/512 of query aligns to 20:436/437 of 1k0eA
- active site: E256 (= E309), K272 (≠ A325), E286 (= E353), H323 (= H390), S350 (≠ T417), W374 (≠ Y441), R394 (= R461), G410 (= G477), E423 (= E490), K427 (= K494)
- binding tryptophan: L32 (= L52), H33 (≠ E53), S34 (= S54), Y41 (≠ W61), F44 (≠ Y64), P238 (= P291), F239 (≠ Y292), S240 (≠ M293)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
34% identity, 92% coverage: 36:506/512 of query aligns to 20:513/519 of P00897
- S39 (= S54) binding L-tryptophan
- PYM 290:292 (= PYM 291:293) binding L-tryptophan
- E360 (= E353) binding Mg(2+)
- E497 (= E490) binding Mg(2+)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 40:503/512 of query aligns to 22:419/420 of 1k0gA
- active site: E258 (= E309), K274 (= K349), E278 (= E353), S333 (≠ T417), W357 (≠ Y441), R377 (= R461), G393 (= G477), E406 (= E490), K410 (= K494)
- binding phosphate ion: D113 (= D131), R116 (= R134), D347 (= D431), R353 (= R437)
- binding tryptophan: L34 (= L52), H35 (≠ E53), S36 (= S54), Y43 (≠ W61), S44 (= S62), F46 (≠ Y64), P240 (= P291), F241 (≠ Y292), S242 (≠ M293)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 90% coverage: 40:502/512 of query aligns to 22:415/415 of 1k0gB
- active site: E258 (= E309), K274 (≠ A325), E277 (= E353), S330 (≠ T417), W354 (≠ Y441), R374 (= R461), G390 (= G477), E403 (= E490), K407 (= K494)
- binding phosphate ion: Y112 (= Y130), D113 (= D131), R116 (= R134), D344 (= D431), R350 (= R437)
- binding tryptophan: L34 (= L52), H35 (≠ E53), S36 (= S54), Y43 (≠ W61), S44 (= S62), R45 (= R63), F46 (≠ Y64), P240 (= P291), F241 (≠ Y292)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
34% identity, 90% coverage: 43:503/512 of query aligns to 180:632/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I324), K454 (≠ A325), G455 (= G326), T456 (≠ S327), M547 (≠ L418), Y570 (= Y441), R590 (= R461), V603 (≠ A474), G604 (= G475), G605 (≠ A476), A606 (≠ G477), E619 (= E490), K623 (= K494)
- binding tryptophan: L189 (= L52), D190 (≠ E53), S191 (= S54), S199 (= S62), F201 (≠ Y64), P419 (= P291), Y420 (= Y292), G421 (≠ M293), L574 (≠ V445), G575 (= G446)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
34% identity, 90% coverage: 43:503/512 of query aligns to 222:671/673 of 8hx8A
- binding magnesium ion: E521 (= E353), E655 (= E487), E658 (= E490)
- binding tryptophan: L231 (= L52), D232 (≠ E53), S233 (= S54), S241 (= S62), F243 (≠ Y64), P458 (= P291), Y459 (= Y292), G460 (≠ M293), G614 (= G446)
Sites not aligning to the query:
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
35% identity, 50% coverage: 243:498/512 of query aligns to 148:402/408 of 2fn1A
- active site: K167 (≠ Q262), E214 (= E309), A230 (= A325), E258 (= E353), H295 (= H390), T322 (= T417), Y346 (= Y441), R365 (= R461), G381 (= G477), E394 (= E490), K398 (= K494)
- binding magnesium ion: E258 (= E353), E394 (= E490)
- binding pyruvic acid: Y346 (= Y441), L364 (≠ I460), R365 (= R461), A378 (= A474), G379 (= G475), K398 (= K494)
Query Sequence
>WP_011606086.1 NCBI__GCF_000058485.1:WP_011606086.1
MTTGRIRPDRAAFHAAAGSRPVVAVTRRLLADGETPVGIYRKLAGGPGTFLLESAEHGGV
WSRYSFVGVRAAATLTERDGQAVWVGTPPPGVPTEGDPLDILRAVERSLRAANDPDAPPL
MGGLVGYLGYDIVRRIERLPSHAVDDLGLPELRMLLTTDLAVLDHADGSCLLVANVFTGA
STEPGGDPAEAARPDLDALYDDAVARLDAMTSDLAKWTEPTVATTSGAASGVGDFVSATP
PGAFQAAVERAIEEIRAGECFQIVVSQRFERTTAADSLDVYRVLRTTNPSPYMYLLRFGD
HDVVGSSPEAHVKVTGRRALLHPIAGSRPRGATPERDAELAAQLLADPKERSEHVMLVDL
VRNDLGRVCVPGSVRVVEFAAVERFSHIMHIVSTVIGEVAPERSAVDVLTATFPAGTLSG
APKVRAMEVIDELEPTRRGLYGGVVGYLDFGGDLDTAIAIRTTVLRDGVAYVQAGAGIVA
DSDPDAEDLESRTKAAAVLRAIEVAESLRPPA
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