SitesBLAST
Comparing WP_019556655.1 NCBI__GCF_000381085.1:WP_019556655.1 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)
7pi1DDD Aminodeoxychorismate synthase component 1
44% identity, 78% coverage: 101:466/472 of query aligns to 92:453/459 of 7pi1DDD
Sites not aligning to the query:
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)
43% identity, 78% coverage: 101:466/472 of query aligns to 94:460/470 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.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
37% identity, 78% coverage: 95:464/472 of query aligns to 109:492/505 of 5cwaA
- active site: Q248 (= Q215), E301 (= E269), A317 (= A285), E345 (= E313), H382 (= H350), T409 (= T377), Y433 (= Y401), R453 (= R421), G469 (= G441), E482 (= E454), K486 (= K458)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y401), I452 (= I420), A466 (= A438), G467 (= G439), K486 (= K458)
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)
37% identity, 77% coverage: 103:464/472 of query aligns to 139:513/524 of A0QX93
- K355 (≠ T302) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 92% coverage: 31:466/472 of query aligns to 25:451/453 of P05041
- S36 (= S42) 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 (≠ T333) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H350) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
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, 91% coverage: 38:466/472 of query aligns to 111:585/595 of P32068
- D341 (= D231) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 77% coverage: 103:464/472 of query aligns to 118:488/499 of 7bvdA
- active site: Q248 (= Q215), E301 (= E269), A317 (= A285), E341 (= E313), H378 (= H350), T405 (= T377), Y429 (= Y401), R449 (= R421), G465 (= G441), E478 (= E454), K482 (= K458)
Sites not aligning to the query:
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 91% coverage: 38:466/472 of query aligns to 95:567/577 of Q94GF1
- D323 (= D231) 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)
34% identity, 92% coverage: 35:466/472 of query aligns to 47:474/489 of O94582
- S390 (≠ T379) modified: Phosphoserine
- S392 (≠ C381) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
31% identity, 92% coverage: 31:466/472 of query aligns to 23:435/437 of 1k0eA
- active site: E256 (= E269), K272 (≠ A285), E286 (= E313), H323 (= H350), S350 (≠ T377), W374 (≠ Y401), R394 (= R421), G410 (= G441), E423 (= E454), K427 (= K458)
- binding tryptophan: L32 (= L40), H33 (≠ E41), S34 (= S42), Y41 (≠ L48), F44 (= F51), P238 (= P246), F239 (= F247), S240 (≠ A248)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
33% identity, 78% coverage: 98:466/472 of query aligns to 297:670/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
33% identity, 78% coverage: 98:466/472 of query aligns to 255:631/632 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 (≠ I378), Y570 (= Y401), R590 (= R421), V603 (≠ A438), G604 (= G439), G605 (≠ A440), A606 (≠ G441), E619 (= E454), K623 (= K458)
- binding tryptophan: P419 (= P246), Y420 (≠ F247), G421 (≠ A248), L574 (≠ M405), G575 (= G406)
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)
33% identity, 80% coverage: 93:468/472 of query aligns to 134:512/520 of P00898
- C174 (≠ E130) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N243) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P244) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A248) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A249) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S265) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N354) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G412) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N417) 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)
33% identity, 80% coverage: 93:468/472 of query aligns to 130:508/512 of 1i1qA
- active site: Q259 (= Q215), E305 (= E269), A323 (= A285), E357 (= E313), H394 (= H350), T421 (= T377), Y445 (= Y401), R465 (= R421), G481 (= G441), E494 (= E454), K498 (= K458)
- binding tryptophan: P287 (= P246), Y288 (≠ F247), M289 (≠ A248), G450 (= G406), C461 (≠ N417)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 92% coverage: 31:466/472 of query aligns to 25:418/420 of 1k0gA
- active site: E258 (= E269), K274 (= K309), E278 (= E313), S333 (≠ T377), W357 (≠ Y401), R377 (= R421), G393 (= G441), E406 (= E454), K410 (= K458)
- binding phosphate ion: D113 (= D115), R116 (≠ Q118), D347 (≠ A391), R353 (≠ P397)
- binding tryptophan: L34 (= L40), H35 (≠ E41), S36 (= S42), Y43 (≠ L48), S44 (≠ G49), F46 (= F51), P240 (= P246), F241 (= F247), S242 (≠ A248)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 92% coverage: 31:466/472 of query aligns to 25:415/415 of 1k0gB
- active site: E258 (= E269), K274 (≠ A285), E277 (= E313), S330 (≠ T377), W354 (≠ Y401), R374 (= R421), G390 (= G441), E403 (= E454), K407 (= K458)
- binding phosphate ion: Y112 (= Y114), D113 (= D115), R116 (≠ Q118), D344 (≠ A391), R350 (≠ P397)
- binding tryptophan: L34 (= L40), H35 (≠ E41), S36 (= S42), Y43 (≠ L48), S44 (≠ G49), R45 (≠ Q50), F46 (= F51), P240 (= P246), F241 (= F247)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
36% identity, 59% coverage: 189:468/472 of query aligns to 236:511/519 of P00897
- PYM 290:292 (≠ PFA 246:248) binding L-tryptophan
- E360 (= E313) binding Mg(2+)
- E497 (= E454) binding Mg(2+)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
36% identity, 59% coverage: 189:468/472 of query aligns to 234:509/517 of 1i7qA
- active site: Q260 (= Q215), E306 (= E269), A324 (= A285), E358 (= E313), H395 (= H350), T422 (= T377), Y446 (= Y401), R466 (= R421), G482 (= G441), E495 (= E454), K499 (= K458)
- binding magnesium ion: E358 (= E313), E495 (= E454)
- binding pyruvic acid: Y446 (= Y401), I465 (= I420), R466 (= R421), A479 (= A438), G480 (= G439), K499 (= K458)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
36% identity, 59% coverage: 189:468/472 of query aligns to 228:503/511 of 1i7sA
- active site: Q254 (= Q215), E300 (= E269), A318 (= A285), E352 (= E313), H389 (= H350), T416 (= T377), Y440 (= Y401), R460 (= R421), G476 (= G441), E489 (= E454), K493 (= K458)
- binding tryptophan: P282 (= P246), Y283 (≠ F247), M284 (≠ A248), V444 (≠ M405), G445 (= G406), D454 (= D415), C456 (≠ N417)
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)
33% identity, 43% coverage: 256:458/472 of query aligns to 201:398/408 of 2fn1A
- active site: E214 (= E269), A230 (= A285), E258 (= E313), H295 (= H350), T322 (= T377), Y346 (= Y401), R365 (= R421), G381 (= G441), E394 (= E454), K398 (= K458)
- binding magnesium ion: E258 (= E313), E394 (= E454)
- binding pyruvic acid: Y346 (= Y401), L364 (≠ I420), R365 (= R421), A378 (= A438), G379 (= G439), K398 (= K458)
Sites not aligning to the query:
Query Sequence
>WP_019556655.1 NCBI__GCF_000381085.1:WP_019556655.1
MSNLTNDQTVVSLPVLLPDPSLLDLSKLHELNPLRYPFLLESVAQGGLGQFDILFAYPQE
TIQLNQLSEKDDFLKRATQAFTESSIATTNDSVHVSSVSPELPFKGGWFAYFSYDYAQVV
EPVLNLPKSEFPLAVLTRIPAAVVVNHKTQSVLLIAEPEYTYLFTQMEADLHQALRLPST
IHPIESVHATEEPEAKYLEGVKAIKEYILSGDVFQVNLSRQWQVTLDKQTDYLSVYRALR
RSNPAPFAALACFKDIKNQAWQVISSSPERLVKYQAPWVETRPIAGTRKRGPDLETDKAL
ITELISHPKERAEHIMLIDLERNDLGRICKPGTVEVNELMAIESYEHVHHIVSNVRGQLQ
EGMSPLDIIHALFPGGTITGCPKVRCMQIVAELEQMPREAYTGSMGYINRDGSLDLNILI
RTMLQFEKEGLPTVQFRAGAGIVADSEAKSELVETRHKAKGLVNALISRDSR
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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