SitesBLAST
Comparing 7024328 FitnessBrowser__ANA3:7024328 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)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
55% identity, 91% coverage: 30:541/563 of query aligns to 11:510/520 of P00898
- E39 (= E58) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S59) binding ; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (= A60) mutation to V: Decrease in feedback control by tryptophan.
- K50 (= K69) binding
- R128 (= R150) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ L198) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N319) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P320) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M324) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F325) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G336) mutation to S: Decrease in feedback control by tryptophan.
- R402 (= R433) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G491) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C496) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
Sites not aligning to the query:
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
54% identity, 91% coverage: 30:541/563 of query aligns to 7:506/512 of 1i1qA
- active site: Q259 (= Q294), E305 (= E340), A323 (= A358), E357 (= E392), H394 (= H429), T421 (= T456), Y445 (= Y480), R465 (= R500), G481 (= G516), E494 (= E529), K498 (= K533)
- binding tryptophan: L34 (= L57), E35 (= E58), S36 (= S59), K46 (= K69), P287 (= P322), Y288 (= Y323), M289 (= M324), G450 (= G485), C461 (= C496)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
52% identity, 91% coverage: 30:541/563 of query aligns to 8:507/517 of 1i7qA
- active site: Q260 (= Q294), E306 (= E340), A324 (= A358), E358 (= E392), H395 (= H429), T422 (= T456), Y446 (= Y480), R466 (= R500), G482 (= G516), E495 (= E529), K499 (= K533)
- binding magnesium ion: E358 (= E392), E495 (= E529)
- binding pyruvic acid: Y446 (= Y480), I465 (= I499), R466 (= R500), A479 (= A513), G480 (= G514), K499 (= K533)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
52% identity, 91% coverage: 30:541/563 of query aligns to 10:509/519 of P00897
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
52% identity, 91% coverage: 30:541/563 of query aligns to 8:501/511 of 1i7sA
- active site: Q254 (= Q294), E300 (= E340), A318 (= A358), E352 (= E392), H389 (= H429), T416 (= T456), Y440 (= Y480), R460 (= R500), G476 (= G516), E489 (= E529), K493 (= K533)
- binding tryptophan: L35 (= L57), E36 (= E58), S37 (= S59), P282 (= P322), Y283 (= Y323), M284 (= M324), V444 (= V484), G445 (= G485), D454 (= D494), C456 (= C496)
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)
35% identity, 91% coverage: 30:539/563 of query aligns to 45:513/524 of A0QX93
- K355 (≠ L381) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
40% identity, 70% coverage: 145:539/563 of query aligns to 97:488/499 of 7bvdA
- active site: Q248 (= Q294), E301 (= E340), A317 (= A358), E341 (= E392), H378 (= H429), T405 (= T456), Y429 (= Y480), R449 (= R500), G465 (= G516), E478 (= E529), K482 (= K533)
- binding pyruvic acid: A100 (≠ G148)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
34% identity, 90% coverage: 31:539/563 of query aligns to 26:492/505 of 5cwaA
- active site: Q248 (= Q294), E301 (= E340), A317 (= A358), E345 (= E392), H382 (= H429), T409 (= T456), Y433 (= Y480), R453 (= R500), G469 (= G516), E482 (= E529), K486 (= K533)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y480), I452 (= I499), A466 (= A513), G467 (= G514), K486 (= K533)
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, 71% coverage: 143:542/563 of query aligns to 95:475/489 of O94582
- S390 (≠ V458) modified: Phosphoserine
- S392 (≠ A460) 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)
36% identity, 67% coverage: 166:544/563 of query aligns to 187:588/595 of P32068
- D341 (= D307) 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, 67% coverage: 166:543/563 of query aligns to 169:569/577 of Q94GF1
- D323 (= D307) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
35% identity, 73% coverage: 131:543/563 of query aligns to 61:462/470 of P28820
- A283 (= A358) 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, 73% coverage: 131:543/563 of query aligns to 59:455/459 of 7pi1DDD
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)
28% identity, 84% coverage: 68:542/563 of query aligns to 1:452/453 of P05041
- S36 (vs. gap) binding
- E258 (= E340) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A358) 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 (= G359) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R401) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R406) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S412) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H429) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
29% identity, 74% coverage: 124:542/563 of query aligns to 55:436/437 of 1k0eA
- active site: E256 (= E340), K272 (≠ A358), E286 (= E392), H323 (= H429), S350 (≠ T456), W374 (≠ Y480), R394 (= R500), G410 (= G516), E423 (= E529), K427 (= K533)
- binding tryptophan: P238 (= P322), F239 (≠ Y323), S240 (≠ M324)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
31% identity, 66% coverage: 171:541/563 of query aligns to 311:670/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
31% identity, 66% coverage: 171:541/563 of query aligns to 269:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I357), K454 (≠ A358), G455 (= G359), T456 (= T360), M547 (≠ L457), Y570 (= Y480), R590 (= R500), V603 (≠ A513), G604 (= G514), G605 (≠ A515), A606 (≠ G516), E619 (= E529), K623 (= K533)
- binding tryptophan: P419 (= P322), Y420 (= Y323), G421 (≠ M324), L574 (≠ V484), G575 (= G485)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
26% identity, 84% coverage: 68:542/563 of query aligns to 1:419/420 of 1k0gA
- active site: E258 (= E340), K274 (= K388), E278 (= E392), S333 (≠ T456), W357 (≠ Y480), R377 (= R500), G393 (= G516), E406 (= E529), K410 (= K533)
- binding phosphate ion: D113 (= D176), R116 (≠ D179), D347 (≠ R470), R353 (= R476)
- binding tryptophan: L34 (≠ A101), H35 (vs. gap), S36 (vs. gap), Y43 (≠ I103), S44 (≠ E104), F46 (= F106), P240 (= P322), F241 (≠ Y323), S242 (≠ M324)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
26% identity, 84% coverage: 68:541/563 of query aligns to 1:415/415 of 1k0gB
- active site: E258 (= E340), K274 (≠ A358), E277 (= E392), S330 (≠ T456), W354 (≠ Y480), R374 (= R500), G390 (= G516), E403 (= E529), K407 (= K533)
- binding phosphate ion: Y112 (= Y175), D113 (= D176), R116 (≠ D179), D344 (≠ R470), R350 (= R476)
- binding tryptophan: L34 (≠ A101), H35 (vs. gap), S36 (vs. gap), Y43 (≠ I103), S44 (≠ E104), R45 (≠ Q105), F46 (= F106), P240 (= P322), F241 (≠ Y323)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
32% identity, 52% coverage: 247:537/563 of query aligns to 142:418/424 of 5jy9B
- active site: K183 (≠ Q294), E230 (= E340), A246 (= A358), E274 (= E392), H311 (= H429), T338 (= T456), Y362 (= Y480), R381 (= R500), G397 (= G516), E410 (= E529), K414 (= K533)
- binding fe (ii) ion: E274 (= E392), E410 (= E529)
Query Sequence
>7024328 FitnessBrowser__ANA3:7024328
MTLKTFNQVTQVDGAHFAPSQQTFARSHTLKATLAYHSDPLRLYQHITQDVPHTMLLESA
EIDSKENLKSMVMTHAALMIRCDGYRLRFSALSDNGVSLLAPIEQFFIARSSQTQCQRDG
HNLVVTLQKDTELKDEDARLKSTSPLDGLRLFVKHIDCGQTPAFEDLFLGGVLSYDLIDT
VEPLPEAPNGANDCPDYLFYLAETLILIDHKQKHAEIITHNFSEGTEQHLEVTQALAERA
ENISAQCEALAKSATPAPALVGITATEQVNVSDDDFKQTVIDLKEHIIAGDIFQVVPSRS
FSLPCPDTLGAYRALRLTNPSPYMFYFRGYDFTLFGASPESALKYEASNNQVEVYPIAGT
RKRGKTASGEIDFDLDSRIELELRLDKKELSEHLMLVDLARNDIARISQSGSRKVAELLK
VDRYSHVMHLVSRVTGQLRQDLDALHAYQACMNMGTLVGAPKVRASQLVRQAEKTRRGSY
GGAVGYLNALGDMDTCIVIRSAFVKNGVAHIQAGAGVVFDSDPQSEADETRQKAQAVISA
IKMGAGLDESQQATATTTTEQQR
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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