SitesBLAST
Comparing CA265_RS22890 FitnessBrowser__Pedo557:CA265_RS22890 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)
33% identity, 97% coverage: 3:456/466 of query aligns to 39:511/524 of A0QX93
- K355 (≠ R302) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
33% identity, 97% coverage: 3:456/466 of query aligns to 19:486/499 of 7bvdA
- active site: Q248 (= Q222), E301 (= E269), A317 (= A285), E341 (= E313), H378 (= H348), T405 (= T375), Y429 (= Y399), R449 (= R419), G465 (= G435), E478 (= E448), K482 (= K452)
- binding pyruvic acid: S93 (≠ E76), G94 (≠ I77), A100 (≠ L83)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
33% identity, 97% coverage: 3:456/466 of query aligns to 19:490/505 of 5cwaA
- active site: Q248 (= Q222), E301 (= E269), A317 (= A285), E345 (= E313), H382 (= H348), T409 (= T375), Y433 (= Y399), R453 (= R419), G469 (= G435), E482 (= E448), K486 (= K452)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y399), I452 (= I418), A466 (= A432), G467 (= G433), K486 (= K452)
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)
32% identity, 98% coverage: 9:464/466 of query aligns to 83:589/595 of P32068
- D341 (= D236) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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)
33% identity, 98% coverage: 9:466/466 of query aligns to 25:480/489 of O94582
- S390 (= S377) modified: Phosphoserine
- S392 (≠ A379) 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)
32% identity, 92% coverage: 34:464/466 of query aligns to 33:464/470 of P28820
- A283 (= A285) 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
33% identity, 92% coverage: 34:464/466 of query aligns to 31:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G435), E438 (= E445)
- binding tryptophan: L33 (= L36), E34 (= E37), S35 (= S38), G39 (≠ N46), Y41 (≠ M48), P242 (= P251), Y243 (= Y252), M244 (≠ L253), Q406 (≠ N413), N408 (≠ A415)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 98% coverage: 10:464/466 of query aligns to 68:571/577 of Q94GF1
- D323 (= D236) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
35% identity, 76% coverage: 111:463/466 of query aligns to 144:509/512 of 1i1qA
- active site: Q259 (= Q222), E305 (= E269), A323 (= A285), E357 (= E313), H394 (= H348), T421 (= T375), Y445 (= Y399), R465 (= R419), G481 (= G435), E494 (= E448), K498 (= K452)
- binding tryptophan: P287 (= P251), Y288 (= Y252), M289 (≠ L253), G450 (= G404), C461 (≠ A415)
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)
36% identity, 76% coverage: 111:463/466 of query aligns to 148:513/520 of P00898
- C174 (≠ Q140) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N248) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P249) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L253) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F254) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G265) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ K352) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (≠ E410) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A415) 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
- 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)
28% identity, 92% coverage: 31:461/466 of query aligns to 29:452/453 of P05041
- S36 (= S38) binding
- E258 (= E269) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A285) 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 (= G286) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R322) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R327) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ R331) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H348) 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)
28% identity, 99% coverage: 2:463/466 of query aligns to 7:510/517 of 1i7qA
- active site: Q260 (= Q222), E306 (= E269), A324 (= A285), E358 (= E313), H395 (= H348), T422 (= T375), Y446 (= Y399), R466 (= R419), G482 (= G435), E495 (= E448), K499 (= K452)
- binding magnesium ion: E358 (= E313), E495 (= E448)
- binding pyruvic acid: Y446 (= Y399), I465 (= I418), R466 (= R419), A479 (= A432), G480 (= G433), K499 (= K452)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
33% identity, 76% coverage: 109:463/466 of query aligns to 137:504/511 of 1i7sA
- active site: Q254 (= Q222), E300 (= E269), A318 (= A285), E352 (= E313), H389 (= H348), T416 (= T375), Y440 (= Y399), R460 (= R419), G476 (= G435), E489 (= E448), K493 (= K452)
- binding tryptophan: P282 (= P251), Y283 (= Y252), M284 (≠ L253), V444 (≠ I403), G445 (= G404), D454 (≠ N413), C456 (≠ A415)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
27% identity, 99% coverage: 2:463/466 of query aligns to 9:512/519 of P00897
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
26% identity, 92% coverage: 31:461/466 of query aligns to 27:436/437 of 1k0eA
- active site: E256 (= E269), K272 (≠ A285), E286 (= E313), H323 (= H348), S350 (≠ T375), W374 (≠ Y399), R394 (= R419), G410 (= G435), E423 (= E448), K427 (= K452)
- binding tryptophan: L32 (= L36), H33 (≠ E37), S34 (= S38), Y41 (≠ E45), F44 (≠ M48), P238 (= P251), F239 (≠ Y252), S240 (≠ L253)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
25% identity, 92% coverage: 31:461/466 of query aligns to 29:419/420 of 1k0gA
- active site: E258 (= E269), K274 (= K309), E278 (= E313), S333 (≠ T375), W357 (≠ Y399), R377 (= R419), G393 (= G435), E406 (= E448), K410 (= K452)
- binding phosphate ion: D113 (≠ N116), R116 (≠ Q119), D347 (= D389), R353 (≠ G395)
- binding tryptophan: L34 (= L36), H35 (≠ E37), S36 (= S38), Y43 (≠ E45), S44 (≠ N46), F46 (≠ M48), P240 (= P251), F241 (≠ Y252), S242 (≠ L253)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
25% identity, 92% coverage: 31:460/466 of query aligns to 29:415/415 of 1k0gB
- active site: E258 (= E269), K274 (≠ A285), E277 (= E313), S330 (≠ T375), W354 (≠ Y399), R374 (= R419), G390 (= G435), E403 (= E448), K407 (= K452)
- binding phosphate ion: Y112 (≠ W115), D113 (≠ N116), R116 (≠ Q119), D344 (= D389), R350 (≠ G395)
- binding tryptophan: L34 (= L36), H35 (≠ E37), S36 (= S38), Y43 (≠ E45), S44 (≠ N46), R45 (≠ S47), F46 (≠ M48), P240 (= P251), F241 (≠ Y252)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
30% identity, 55% coverage: 204:460/466 of query aligns to 372:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I284), K454 (≠ A285), G455 (= G286), T456 (= T287), M547 (≠ L376), Y570 (= Y399), R590 (= R419), V603 (≠ A432), G604 (= G433), G605 (≠ A434), A606 (≠ G435), E619 (= E448), K623 (= K452)
- binding tryptophan: P419 (= P251), Y420 (= Y252), G421 (≠ L253), L574 (≠ I403), G575 (= G404)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
30% identity, 55% coverage: 204:460/466 of query aligns to 411:670/673 of 8hx8A
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
27% identity, 81% coverage: 79:456/466 of query aligns to 65:418/424 of 5jy9B
- active site: K183 (≠ Q222), E230 (= E269), A246 (= A285), E274 (= E313), H311 (= H348), T338 (= T375), Y362 (= Y399), R381 (= R419), G397 (= G435), E410 (= E448), K414 (= K452)
- binding fe (ii) ion: E274 (= E313), E410 (= E448)
Query Sequence
>CA265_RS22890 FitnessBrowser__Pedo557:CA265_RS22890
MMYKINTTYKKMLADTTTPVSIYLRLRDVYPNSILLESSDYHSRENSMSFVCADPVAGII
LKGSRLETYFPDGAVEITESKNLIEEITDFKDKFSETELPEIKFISSGLFGYFTWNAVQH
FEDIKFTSETPEGEEIPEMQYHLYRYIIAIDHFKNEITLFKNTFEGEEEGGLEKMEYLIQ
NKNYPEYKFQLRGEESSNLTDQGFMDLVEKLQKHIYRGDVFQIVPSRAFKQAFSGDEFNV
YRCLRSINPSPYLFYFDYGNFKLFGSSPEAQITIKNNSANIFPIAGTFKRSGNDIEDAEQ
ARKLEQDPKESAEHVMLVDLARNDLSRHCNRVEVKSFKEVQYYSHLIHLVSKVSGHLQEN
VSAFKVVADTYPAGTLSGAPKYKAMQLIDENEKLGRNFYAGAIGFMGFNEDFNHAIMIRT
FMSKNNELHYRAGAGIVADSVPETEMQEVNNKIAALRKAVQMAEGI
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