SitesBLAST
Comparing 8501009 FitnessBrowser__Miya:8501009 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)
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)
34% identity, 88% coverage: 57:514/520 of query aligns to 5:464/470 of P28820
- A283 (= A330) 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
35% identity, 88% coverage: 57:514/520 of query aligns to 3:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G485), E438 (= E495)
- binding tryptophan: L33 (= L86), E34 (= E87), S35 (= S88), G39 (= G96), Y41 (≠ F98), P242 (= P296), Y243 (= Y297), M244 (= M298), Q406 (≠ D463), N408 (≠ G465)
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)
36% identity, 94% coverage: 18:506/520 of query aligns to 5:511/524 of A0QX93
- K355 (≠ R347) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 91% coverage: 36:506/520 of query aligns to 3:486/499 of 7bvdA
- active site: Q248 (= Q267), E301 (= E314), A317 (= A330), E341 (= E358), H378 (= H395), T405 (= T422), Y429 (= Y446), R449 (= R469), G465 (= G485), E478 (= E498), K482 (= K502)
- binding pyruvic acid: S93 (≠ D132), G94 (= G133), A100 (≠ G139)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
38% identity, 86% coverage: 61:506/520 of query aligns to 26:490/505 of 5cwaA
- active site: Q248 (= Q267), E301 (= E314), A317 (= A330), E345 (= E358), H382 (= H395), T409 (= T422), Y433 (= Y446), R453 (= R469), G469 (= G485), E482 (= E498), K486 (= K502)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y446), I452 (= I468), A466 (= A482), G467 (= G483), K486 (= K502)
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)
34% identity, 87% coverage: 65:514/520 of query aligns to 30:475/489 of O94582
- S390 (= S424) modified: Phosphoserine
- S392 (≠ A426) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
42% identity, 52% coverage: 249:520/520 of query aligns to 309:595/595 of P32068
- D341 (= D281) 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)
44% identity, 52% coverage: 249:519/520 of query aligns to 291:576/577 of Q94GF1
- D323 (= D281) 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, 75% coverage: 122:512/520 of query aligns to 115:513/520 of P00898
- R128 (≠ G135) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (= C193) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N293) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P294) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M298) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F299) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G310) mutation to S: Decrease in feedback control by tryptophan.
- R402 (= R399) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (≠ R457) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ G465) 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 ; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding
- 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, 75% coverage: 122:512/520 of query aligns to 111:509/512 of 1i1qA
- active site: Q259 (= Q267), E305 (= E314), A323 (= A330), E357 (= E358), H394 (= H395), T421 (= T422), Y445 (= Y446), R465 (= R469), G481 (= G485), E494 (= E498), K498 (= K502)
- binding tryptophan: P287 (= P296), Y288 (= Y297), M289 (= M298), G450 (= G451), C461 (≠ G465)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
33% identity, 85% coverage: 70:512/520 of query aligns to 18:510/517 of 1i7qA
- active site: Q260 (= Q267), E306 (= E314), A324 (= A330), E358 (= E358), H395 (= H395), T422 (= T422), Y446 (= Y446), R466 (= R469), G482 (= G485), E495 (= E498), K499 (= K502)
- binding magnesium ion: E358 (= E358), E495 (= E498)
- binding pyruvic acid: Y446 (= Y446), I465 (= I468), R466 (= R469), A479 (= A482), G480 (= G483), K499 (= K502)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
45% identity, 51% coverage: 249:512/520 of query aligns to 236:504/511 of 1i7sA
- active site: Q254 (= Q267), E300 (= E314), A318 (= A330), E352 (= E358), H389 (= H395), T416 (= T422), Y440 (= Y446), R460 (= R469), G476 (= G485), E489 (= E498), K493 (= K502)
- binding tryptophan: P282 (= P296), Y283 (= Y297), M284 (= M298), V444 (≠ I450), G445 (= G451), D454 (= D463), C456 (≠ G465)
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)
36% identity, 67% coverage: 160:506/520 of query aligns to 101:447/453 of P05041
- E258 (= E314) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A330) 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 (= G331) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R367) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R372) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T378) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H395) 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:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
44% identity, 51% coverage: 249:512/520 of query aligns to 244:512/519 of P00897
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
35% identity, 65% coverage: 167:506/520 of query aligns to 106:431/437 of 1k0eA
- active site: E256 (= E314), K272 (≠ A330), E286 (= E358), H323 (= H395), S350 (≠ T422), W374 (≠ Y446), R394 (= R469), G410 (= G485), E423 (= E498), K427 (= K502)
- binding tryptophan: P238 (= P296), F239 (≠ Y297), S240 (≠ M298)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
33% identity, 65% coverage: 167:506/520 of query aligns to 108:414/420 of 1k0gA
- active site: E258 (= E314), K274 (= K354), E278 (= E358), S333 (≠ T422), W357 (≠ Y446), R377 (= R469), G393 (= G485), E406 (= E498), K410 (= K502)
- binding phosphate ion: D113 (≠ G172), R116 (≠ G175), D347 (≠ S436), R353 (≠ A442)
- binding tryptophan: P240 (= P296), F241 (≠ Y297), S242 (≠ M298)
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, 52% coverage: 245:512/520 of query aligns to 407:672/673 of 8hx8A
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 67% coverage: 160:506/520 of query aligns to 101:411/415 of 1k0gB
- active site: E258 (= E314), K274 (≠ A330), E277 (= E358), S330 (≠ T422), W354 (≠ Y446), R374 (= R469), G390 (= G485), E403 (= E498), K407 (= K502)
- binding phosphate ion: Y112 (= Y171), D113 (≠ G172), R116 (≠ G175), D344 (≠ S436), R350 (≠ A442)
- binding tryptophan: P240 (= P296), F241 (≠ Y297)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
37% identity, 53% coverage: 234:511/520 of query aligns to 343:629/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I329), K454 (≠ A330), G455 (= G331), T456 (= T332), M547 (≠ V423), Y570 (= Y446), R590 (= R469), V603 (≠ A482), G604 (= G483), G605 (≠ A484), A606 (≠ G485), E619 (= E498), K623 (= K502)
- binding tryptophan: P419 (= P296), Y420 (= Y297), G421 (≠ M298), L574 (≠ I450), G575 (= G451)
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)
37% identity, 50% coverage: 249:506/520 of query aligns to 149:402/408 of 2fn1A
- active site: K167 (≠ Q267), E214 (= E314), A230 (= A330), E258 (= E358), H295 (= H395), T322 (= T422), Y346 (= Y446), R365 (= R469), G381 (= G485), E394 (= E498), K398 (= K502)
- binding magnesium ion: E258 (= E358), E394 (= E498)
- binding pyruvic acid: Y346 (= Y446), L364 (≠ I468), R365 (= R469), A378 (= A482), G379 (= G483), K398 (= K502)
Query Sequence
>8501009 FitnessBrowser__Miya:8501009
MEMPEMPAQAEAPETAKAPQAPETAQAPANGNGCPCATTGSGDDIPALPEGGEIVLRQTG
RWLEADVDTPISVFLGMVGSGQGILLESAEVDGRWGRFSVIAFNFLLRLGCRDGKLEVAV
RDPRLAPLRRFDGMGFIEGTRAVMRALRIEPDAAFADQPPITRALYGYFGYGVSGLFEPK
LAKVLPTSSAEACLALPGTVVLFDHLYNRLCQLSLTDLPGGRVDRSQVDRTPEPPEVGPV
VNVPEQAVYTRAVARVKDMIRQGEAIQVVLSTRFQASFSGDPFTLYRRLRRINPSPYMFF
MRLPGVSLLGSSPEVMVRCRADKLQVSPIAGTRPRGTDDAHDAALARELLEDPKERAEHV
MLVDLGRNDLGRIAAPGTVQVERFMDVEKFSHVMHLTSRVTAQIEPGRDALDVLAATFPA
GTVSGAPKVRAMEIISEAEGLARGPYAGAIGWLGLDRDSVNLDTGITIRSLWVRDGQVHW
QAGAGIVFDSVPEMEWKECNNKAAVIRAAVTGGEYVPVNR
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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