SitesBLAST
Comparing WP_009544161.1 NCBI__GCF_000017845.1:WP_009544161.1 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)
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)
39% identity, 98% coverage: 5:503/507 of query aligns to 66:585/595 of P32068
- D341 (= D267) 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)
39% identity, 98% coverage: 8:503/507 of query aligns to 52:567/577 of Q94GF1
- D323 (= D267) 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)
40% identity, 99% coverage: 2:503/507 of query aligns to 3:474/489 of O94582
- S390 (= S415) modified: Phosphoserine
- S392 (≠ A417) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
41% identity, 97% coverage: 7:500/507 of query aligns to 30:512/524 of A0QX93
- K355 (≠ E338) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
41% identity, 97% coverage: 7:500/507 of query aligns to 10:491/505 of 5cwaA
- active site: Q248 (= Q253), E301 (= E300), A317 (= A321), E345 (= E349), H382 (= H386), T409 (= T413), Y433 (= Y437), R453 (= R457), G469 (= G478), E482 (= E491), K486 (= K495)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y437), I452 (= I456), A466 (= A475), G467 (= G476), K486 (= K495)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
40% identity, 97% coverage: 7:500/507 of query aligns to 10:487/499 of 7bvdA
- active site: Q248 (= Q253), E301 (= E300), A317 (= A321), E341 (= E349), H378 (= H386), T405 (= T413), Y429 (= Y437), R449 (= R457), G465 (= G478), E478 (= E491), K482 (= K495)
- binding pyruvic acid: S93 (≠ F91), G94 (≠ E92), A100 (≠ I98)
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)
39% identity, 92% coverage: 38:503/507 of query aligns to 24:460/470 of P28820
- A283 (= A321) 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
39% identity, 92% coverage: 38:503/507 of query aligns to 22:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G478), E438 (= E488)
- binding tryptophan: L33 (= L49), E34 (= E50), S35 (= S51), G39 (= G55), Y41 (= Y61), P242 (= P282), Y243 (= Y283), M244 (= M284), Q406 (≠ N451), N408 (≠ A453)
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)
33% identity, 91% coverage: 44:503/507 of query aligns to 29:451/453 of P05041
- S36 (= S51) binding L-tryptophan
- E258 (= E300) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A321) 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 (= G322) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R358) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R363) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S369) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H386) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
34% identity, 93% coverage: 30:503/507 of query aligns to 19:510/520 of P00898
- E39 (= E50) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S51) binding L-tryptophan; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (≠ V52) mutation to V: Decrease in feedback control by tryptophan.
- K50 (≠ Y61) binding L-tryptophan
- R128 (≠ Q113) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ V151) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N279) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P280) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M284) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A285) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G296) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N390) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G448) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A453) 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)
34% identity, 93% coverage: 30:503/507 of query aligns to 15:506/512 of 1i1qA
- active site: Q259 (= Q253), E305 (= E300), A323 (= A321), E357 (= E349), H394 (= H386), T421 (= T413), Y445 (= Y437), R465 (= R457), G481 (= G478), E494 (= E491), K498 (= K495)
- binding tryptophan: L34 (= L49), E35 (= E50), S36 (= S51), K46 (≠ Y61), P287 (= P282), Y288 (= Y283), M289 (= M284), G450 (= G442), C461 (≠ A453)
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 91% coverage: 44:503/507 of query aligns to 27:435/437 of 1k0eA
- active site: E256 (= E300), K272 (≠ A321), E286 (= E349), H323 (= H386), S350 (≠ T413), W374 (≠ Y437), R394 (= R457), G410 (= G478), E423 (= E491), K427 (= K495)
- binding tryptophan: L32 (= L49), H33 (≠ E50), S34 (= S51), Y41 (≠ L58), F44 (≠ Y61), P238 (= P282), F239 (≠ Y283), S240 (≠ M284)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 93% coverage: 32:503/507 of query aligns to 18:507/517 of 1i7qA
- active site: Q260 (= Q253), E306 (= E300), A324 (= A321), E358 (= E349), H395 (= H386), T422 (= T413), Y446 (= Y437), R466 (= R457), G482 (= G478), E495 (= E491), K499 (= K495)
- binding magnesium ion: E358 (= E349), E495 (= E491)
- binding pyruvic acid: Y446 (= Y437), I465 (= I456), R466 (= R457), A479 (= A475), G480 (= G476), K499 (= K495)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
33% identity, 93% coverage: 32:503/507 of query aligns to 18:501/511 of 1i7sA
- active site: Q254 (= Q253), E300 (= E300), A318 (= A321), E352 (= E349), H389 (= H386), T416 (= T413), Y440 (= Y437), R460 (= R457), G476 (= G478), E489 (= E491), K493 (= K495)
- binding tryptophan: L35 (= L49), E36 (= E50), S37 (= S51), P282 (= P282), Y283 (= Y283), M284 (= M284), V444 (≠ Y441), G445 (= G442), D454 (≠ N451), C456 (≠ A453)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
32% identity, 93% coverage: 32:503/507 of query aligns to 20:509/519 of P00897
- S39 (= S51) binding L-tryptophan
- PYM 290:292 (= PYM 282:284) binding L-tryptophan
- E360 (= E349) binding Mg(2+)
- E497 (= E491) binding Mg(2+)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 44:503/507 of query aligns to 29:418/420 of 1k0gA
- active site: E258 (= E300), K274 (= K345), E278 (= E349), S333 (≠ T413), W357 (≠ Y437), R377 (= R457), G393 (= G478), E406 (= E491), K410 (= K495)
- binding phosphate ion: D113 (≠ E128), R116 (≠ N131), D347 (≠ N427), R353 (= R433)
- binding tryptophan: L34 (= L49), H35 (≠ E50), S36 (= S51), Y43 (≠ L58), S44 (≠ G59), F46 (≠ Y61), P240 (= P282), F241 (≠ Y283), S242 (≠ M284)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 91% coverage: 44:503/507 of query aligns to 29:415/415 of 1k0gB
- active site: E258 (= E300), K274 (≠ A321), E277 (= E349), S330 (≠ T413), W354 (≠ Y437), R374 (= R457), G390 (= G478), E403 (= E491), K407 (= K495)
- binding phosphate ion: Y112 (= Y127), D113 (≠ E128), R116 (≠ N131), D344 (≠ N427), R350 (= R433)
- binding tryptophan: L34 (= L49), H35 (≠ E50), S36 (= S51), Y43 (≠ L58), S44 (≠ G59), R45 (= R60), F46 (≠ Y61), P240 (= P282), F241 (≠ Y283)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
31% identity, 90% coverage: 46:503/507 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 (= I320), K454 (≠ A321), G455 (= G322), T456 (= T323), M547 (≠ V414), Y570 (= Y437), R590 (= R457), V603 (= V473), G604 (= G476), G605 (≠ A477), A606 (≠ G478), E619 (= E491), K623 (= K495)
- binding tryptophan: L189 (= L49), D190 (≠ E50), S191 (= S51), S199 (≠ G59), F201 (≠ Y61), P419 (= P282), Y420 (= Y283), G421 (≠ M284), L574 (≠ Y441), G575 (= G442)
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, 90% coverage: 46:503/507 of query aligns to 228:670/673 of 8hx8A
- binding magnesium ion: E521 (= E349), E655 (= E488), E658 (= E491)
- binding tryptophan: L231 (= L49), D232 (≠ E50), S233 (= S51), S241 (≠ G59), F243 (≠ Y61), P458 (= P282), Y459 (= Y283), G460 (≠ M284), G614 (= G442)
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)
31% identity, 54% coverage: 223:495/507 of query aligns to 137:398/408 of 2fn1A
- active site: K167 (≠ Q253), E214 (= E300), A230 (= A321), E258 (= E349), H295 (= H386), T322 (= T413), Y346 (= Y437), R365 (= R457), G381 (= G478), E394 (= E491), K398 (= K495)
- binding magnesium ion: E258 (= E349), E394 (= E491)
- binding pyruvic acid: Y346 (= Y437), L364 (≠ I456), R365 (= R457), A378 (= A475), G379 (= G476), K398 (= K495)
Query Sequence
>WP_009544161.1 NCBI__GCF_000017845.1:WP_009544161.1
MMFPDFEQFSVLAQQGNFVPVYQEWVADLETPVSSWYKVCGDRPYSFLLESVEGGENLGR
YSFLGCDPVWILSARGNITTQTYRDGRVKTFEGNPFDILTDCLASIKPVTLPQLPSGIGG
LFGFWGYELINWIEPRVPIYPITDDDLPDGVWMQVDHLIIFDQVKRKIWAIAYADLRDKN
ISLEQAYQQACDRVTKLVLKLQLPLPIQGKTLELNPNSEETQPLNYTSNTERAQFCENVR
QAKEYIRAGDIFQVVLSQRLQAHYEDDPFNLYRSLRLINPSPYMAYYNFGDWQIIGSSPE
VMVKAERQEDESLTAILRPIAGTRKRGQTPTEDQALAEDLLQDPKEIAEHVMLVDLGRND
LGRACCEGSVTVNELMVIERYSHVMHIVSNVIGKLADNKTPWDLFKACFPAGTVSGAPKI
RAMEIINELEPERRGPYSGVYGYYDFEGQLNTAIAIRTMVVRPLGSGQHLVCVQAGAGLV
ADSDPETEYEETMNKARGLLEAIRSLS
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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