SitesBLAST
Comparing WP_010961799.1 NCBI__GCF_000008325.1:WP_010961799.1 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)
45% identity, 96% coverage: 4:479/495 of query aligns to 30:512/524 of A0QX93
- K355 (≠ R322) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
41% identity, 95% coverage: 15:486/495 of query aligns to 3:464/470 of P28820
- A283 (= A305) 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
42% identity, 95% coverage: 15:486/495 of query aligns to 1:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G457), E438 (= E467)
- binding tryptophan: L33 (≠ F46), E34 (= E47), S35 (= S48), G39 (= G52), Y41 (= Y58), P242 (= P271), Y243 (= Y272), M244 (= M273), Q406 (≠ D435), N408 (≠ A437)
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)
39% identity, 97% coverage: 15:495/495 of query aligns to 20:487/489 of O94582
- S390 (= S399) modified: Phosphoserine
- S392 (≠ A401) 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)
41% identity, 98% coverage: 5:487/495 of query aligns to 52:572/577 of Q94GF1
- D323 (≠ S256) mutation to N: Insensitive to feedback inhibition by tryptophan.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
44% identity, 96% coverage: 4:479/495 of query aligns to 10:491/505 of 5cwaA
- active site: Q248 (= Q242), E301 (= E289), A317 (= A305), E345 (= E333), H382 (= H370), T409 (= T397), Y433 (= Y421), R453 (= R441), G469 (= G457), E482 (= E470), K486 (= K474)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y421), I452 (= I440), A466 (= A454), G467 (= G455), K486 (= K474)
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)
40% identity, 97% coverage: 8:488/495 of query aligns to 71:591/595 of P32068
- D341 (≠ S256) 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]
44% identity, 96% coverage: 4:479/495 of query aligns to 10:487/499 of 7bvdA
- active site: Q248 (= Q242), E301 (= E289), A317 (= A305), E341 (= E333), H378 (= H370), T405 (= T397), Y429 (= Y421), R449 (= R441), G465 (= G457), E478 (= E470), K482 (= K474)
- binding pyruvic acid: S93 (≠ T89), G94 (≠ V90), A100 (≠ W96)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
37% identity, 83% coverage: 78:490/495 of query aligns to 111:518/520 of P00898
- R128 (≠ A95) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ L149) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N268) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P269) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M273) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y274) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G285) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N374) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G432) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A437) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (≠ A487) mutation to Y: Almost no change in feedback control by tryptophan.
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
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
37% identity, 83% coverage: 78:486/495 of query aligns to 107:510/512 of 1i1qA
- active site: Q259 (= Q242), E305 (= E289), A323 (= A305), E357 (= E333), H394 (= H370), T421 (= T397), Y445 (= Y421), R465 (= R441), G481 (= G457), E494 (= E470), K498 (= K474)
- binding tryptophan: P287 (= P271), Y288 (= Y272), M289 (= M273), G450 (= G426), C461 (≠ A437)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
39% identity, 75% coverage: 119:490/495 of query aligns to 137:509/511 of 1i7sA
- active site: Q254 (= Q242), E300 (= E289), A318 (= A305), E352 (= E333), H389 (= H370), T416 (= T397), Y440 (= Y421), R460 (= R441), G476 (= G457), E489 (= E470), K493 (= K474)
- binding tryptophan: P282 (= P271), Y283 (= Y272), M284 (= M273), V444 (= V425), G445 (= G426), D454 (= D435), C456 (≠ A437)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
39% identity, 75% coverage: 119:490/495 of query aligns to 143:515/517 of 1i7qA
- active site: Q260 (= Q242), E306 (= E289), A324 (= A305), E358 (= E333), H395 (= H370), T422 (= T397), Y446 (= Y421), R466 (= R441), G482 (= G457), E495 (= E470), K499 (= K474)
- binding magnesium ion: E358 (= E333), E495 (= E470)
- binding pyruvic acid: Y446 (= Y421), I465 (= I440), R466 (= R441), A479 (= A454), G480 (= G455), K499 (= K474)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
39% identity, 75% coverage: 119:490/495 of query aligns to 145:517/519 of P00897
- PYM 290:292 (= PYM 271:273) binding L-tryptophan
- E360 (= E333) binding Mg(2+)
- E497 (= E470) binding Mg(2+)
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)
32% identity, 91% coverage: 34:482/495 of query aligns to 22:451/453 of P05041
- S36 (= S48) binding L-tryptophan
- E258 (= E289) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A305) 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 (= G306) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R342) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R347) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S353) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H370) 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)
32% identity, 91% coverage: 34:482/495 of query aligns to 20:435/437 of 1k0eA
- active site: E256 (= E289), K272 (≠ A305), E286 (= E333), H323 (= H370), S350 (≠ T397), W374 (≠ Y421), R394 (= R441), G410 (= G457), E423 (= E470), K427 (= K474)
- binding tryptophan: L32 (≠ F46), H33 (≠ E47), S34 (= S48), Y41 (≠ W55), F44 (≠ Y58), P238 (= P271), F239 (≠ Y272), S240 (≠ M273)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 34:482/495 of query aligns to 22:418/420 of 1k0gA
- active site: E258 (= E289), K274 (= K329), E278 (= E333), S333 (≠ T397), W357 (≠ Y421), R377 (= R441), G393 (= G457), E406 (= E470), K410 (= K474)
- binding phosphate ion: D113 (≠ E126), R116 (≠ Y130), D347 (≠ A411), R353 (≠ K417)
- binding tryptophan: L34 (≠ F46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), F46 (≠ Y58), P240 (= P271), F241 (≠ Y272), S242 (≠ M273)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 34:482/495 of query aligns to 22:415/415 of 1k0gB
- active site: E258 (= E289), K274 (≠ A305), E277 (= E333), S330 (≠ T397), W354 (≠ Y421), R374 (= R441), G390 (= G457), E403 (= E470), K407 (= K474)
- binding phosphate ion: Y112 (= Y125), D113 (≠ E126), R116 (≠ Y130), D344 (≠ A411), R350 (≠ K417)
- binding tryptophan: L34 (≠ F46), H35 (≠ E47), S36 (= S48), Y43 (≠ W55), S44 (≠ G56), R45 (= R57), F46 (≠ Y58), P240 (= P271), F241 (≠ Y272)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
32% identity, 89% coverage: 43:482/495 of query aligns to 228:670/673 of 8hx8A
- binding magnesium ion: E521 (= E333), E655 (= E467), E658 (= E470)
- binding tryptophan: L231 (≠ F46), D232 (≠ E47), S233 (= S48), S241 (≠ G56), F243 (≠ Y58), P458 (= P271), Y459 (= Y272), G460 (≠ M273), G614 (= G426)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 89% coverage: 43:482/495 of query aligns to 186:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I304), K454 (≠ A305), G455 (= G306), T456 (= T307), M547 (≠ V398), Y570 (= Y421), R590 (= R441), V603 (≠ A454), G604 (= G455), G605 (≠ A456), A606 (≠ G457), E619 (= E470), K623 (= K474)
- binding tryptophan: L189 (≠ F46), D190 (≠ E47), S191 (= S48), S199 (≠ G56), F201 (≠ Y58), P419 (= P271), Y420 (= Y272), G421 (≠ M273), L574 (≠ V425), G575 (= G426)
Sites not aligning to the query:
2g5fA The structure of mbti from mycobacterium tuberculosis, the first enzyme in the synthesis of mycobactin, reveals it to be a salicylate synthase (see paper)
30% identity, 84% coverage: 44:459/495 of query aligns to 31:409/435 of 2g5fA
- active site: K191 (≠ Q242), E238 (= E289), A255 (= A305), E283 (= E333), H320 (= H370), T347 (= T397), Y371 (= Y421), R391 (= R441), G407 (= G457)
- binding pyruvic acid: Y371 (= Y421), L390 (≠ I440), R391 (= R441), G405 (= G455)
Sites not aligning to the query:
Query Sequence
>WP_010961799.1 NCBI__GCF_000008325.1:WP_010961799.1
MTPERFQAFAAQGYNRVPLARRVLADLDTPLSAYLKLADGPYSYLFESVHGGEQWGRYSI
IGLPCRTCIEVRGHEVIVLRDGARAETLTVENPLAWIKAFGSRFKVPDLEGLPRFTGGLV
GYFGYETMGYIEPRLAKTKPDPIGSPDILLMVSEEVLVFDKLTGKLLVVVHADPNEAGAY
AKAQTRLDELVRELRSRQLPPAPPRSPRTVDEADFISGFTREGFEDAVRRVKEYIVEGDV
MQVVLSQRLSIPYAASPLDLYRALRCLNPSPYMYQLNLGDFHVVGSSPEILVRLEDGTVT
VRPIAGTRRRGRSPEEDQALERELLADPKELAEHLMLIDLGRNDTGRISETGSVRLTEKM
VVERYSHVMHIVSNVTGKLQAGKDAYDVLAATFPAGTVSGAPKIRAMEIIAELEPVKRGV
YSGAVGYIGWSGNMDTAIAIRTAVIKDGRLHIQAGAGVVYDSVPRSEWEETMNKARAIFR
AVAMAEAGVEGGENA
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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