SitesBLAST
Comparing WP_066328935.1 NCBI__GCF_900100165.1:WP_066328935.1 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)
35% identity, 96% coverage: 10:456/466 of query aligns to 45:511/524 of A0QX93
- K355 (= K302) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
35% identity, 96% coverage: 10:456/466 of query aligns to 25:486/499 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 (= S76), G94 (≠ E77), A100 (= A83)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
35% identity, 96% coverage: 11:456/466 of query aligns to 26:490/505 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)
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)
35% identity, 97% coverage: 13:466/466 of query aligns to 28:480/489 of O94582
- S390 (= S377) modified: Phosphoserine
- S392 (≠ A379) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
33% identity, 98% coverage: 11:465/466 of query aligns to 68:572/577 of Q94GF1
- D323 (= D236) mutation to N: Insensitive to feedback inhibition by tryptophan.
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: 10:465/466 of query aligns to 83:590/595 of P32068
- D341 (= D236) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7pi1DDD Aminodeoxychorismate synthase component 1
33% identity, 92% coverage: 35:464/466 of query aligns to 31:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G435), E438 (= E445)
- binding tryptophan: L33 (= L37), E34 (= E38), S35 (= S39), G39 (≠ N47), Y41 (≠ F49), P242 (= P251), Y243 (= Y252), M244 (≠ L253), Q406 (≠ N413), N408 (≠ A415)
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)
33% identity, 92% coverage: 35:464/466 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
32% identity, 95% coverage: 20:463/466 of query aligns to 17:509/512 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: L34 (= L37), E35 (= E38), S36 (= S39), K46 (≠ F49), P287 (= P251), Y288 (= Y252), M289 (≠ L253), G450 (= G404), C461 (≠ A415)
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)
30% identity, 92% coverage: 24:453/466 of query aligns to 21:444/453 of P05041
- S36 (= S39) binding L-tryptophan
- 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 (≠ N331) 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.
8rp0CCC Aminodeoxychorismate synthase component 1
30% identity, 92% coverage: 24:453/466 of query aligns to 22:445/454 of 8rp0CCC
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: N214 (≠ V224), I274 (= I284), K275 (≠ A285), G276 (= G286), T277 (= T287), E303 (= E313), H340 (= H348), W391 (≠ Y399), I410 (= I418), R411 (= R419), A424 (= A432), G425 (= G433), G426 (≠ A434), E440 (= E448), K444 (= K452)
- binding magnesium ion: E303 (= E313), E440 (= E448)
- binding tryptophan: L35 (= L37), H36 (≠ E38), S37 (= S39), Y44 (≠ D46), R46 (≠ S48), F47 (= F49), P241 (= P251), F242 (≠ Y252), S243 (≠ L253), D405 (≠ N413)
8rp0DDD Aminodeoxychorismate synthase component 1
30% identity, 92% coverage: 24:453/466 of query aligns to 23:446/455 of 8rp0DDD
- binding glutamic acid: G209 (= G218), Y212 (≠ F221)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: N215 (≠ V224), I275 (= I284), K276 (≠ A285), G277 (= G286), T278 (= T287), E304 (= E313), W392 (≠ Y399), I411 (= I418), R412 (= R419), A425 (= A432), G426 (= G433), G427 (≠ A434), E441 (= E448), K445 (= K452)
- binding magnesium ion: E304 (= E313), E441 (= E448)
- binding tryptophan: H37 (≠ E38), S38 (= S39), Y45 (≠ D46), R47 (≠ S48), F48 (= F49), P242 (= P251), F243 (≠ Y252), S244 (≠ L253), D406 (≠ N413)
8rp1CCC Aminodeoxychorismate synthase component 1
30% identity, 92% coverage: 24:453/466 of query aligns to 24:447/456 of 8rp1CCC
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
31% identity, 95% coverage: 20:463/466 of query aligns to 21:513/520 of P00898
- E39 (= E38) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S39) binding L-tryptophan; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (≠ S40) mutation to V: Decrease in feedback control by tryptophan.
- K50 (≠ F49) binding L-tryptophan
- R128 (vs. gap) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ F142) 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 (= G410) 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:
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
30% identity, 95% coverage: 20:463/466 of query aligns to 18:504/511 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: L35 (= L37), E36 (= E38), S37 (= S39), P282 (= P251), Y283 (= Y252), M284 (≠ L253), V444 (≠ I403), G445 (= G404), D454 (≠ N413), C456 (≠ A415)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
30% identity, 95% coverage: 20:463/466 of query aligns to 18:510/517 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)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
29% identity, 95% coverage: 20:463/466 of query aligns to 20:512/519 of P00897
- S39 (= S39) binding L-tryptophan
- PYM 290:292 (≠ PYL 251:253) binding L-tryptophan
- E360 (= E313) binding Mg(2+)
- E497 (= E448) binding Mg(2+)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
27% identity, 92% coverage: 24:453/466 of query aligns to 21:411/420 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 (= D119), R116 (= R122), D347 (≠ E389), R353 (≠ N395)
- binding tryptophan: L34 (= L37), H35 (≠ E38), S36 (= S39), Y43 (≠ D46), S44 (≠ N47), F46 (= F49), P240 (= P251), F241 (≠ Y252), S242 (≠ L253)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
29% identity, 77% coverage: 105:461/466 of query aligns to 261:632/632 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)
29% identity, 77% coverage: 105:461/466 of query aligns to 303:671/673 of 8hx8A
Sites not aligning to the query:
Query Sequence
>WP_066328935.1 NCBI__GCF_900100165.1:WP_066328935.1
MKQFKLNTKFKQILADTITPVSVYFKIRDKFPNSLLLESSDYHANDNSFSYICCNPIASI
KIENETIFKQFPDGSSETTTIDAKTNIPEVIQQFSGQFKSEKNNFKFINNGLFGYISYDA
VRYFEKVTIAKKENSNTIPDLFYAVYQNIIAINHFKNEAYIFCHSVDDKNNIAEIEQLMQ
SRNIPSYKFSKEGEGFSNLTDEEFKHNVALAKKHCFRGDVFQLVLSRRFTQGFKGDEFNV
YRALRSINPSPYLFFFDYGDFKIFGSSPEAQIIVKDRKAEIHPIAGTFRRTGDDEKDAVL
AKKLSEDKKENSEHVMLVDLARNDLSRHGHNVNVERYREVQFFSHVIHLVSKVTGHLHDD
ATTMQVVADTFPAGTLSGAPKHRAMQLIEDYEKTNRNFYGGAIGFMDFEGNFNHAIMIRT
FLSKNHQLHSQAGAGIVASSDEESEMQEVYNKLRALNAALDLAETI
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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