SitesBLAST
Comparing WP_010966440.1 NCBI__GCF_000008765.1:WP_010966440.1 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)
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)
43% identity, 93% coverage: 27:467/475 of query aligns to 30:466/489 of O94582
- S390 (= S392) modified: Phosphoserine
- S392 (≠ A394) 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)
40% identity, 91% coverage: 42:475/475 of query aligns to 30:460/470 of P28820
- A283 (= A298) 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
40% identity, 91% coverage: 42:475/475 of query aligns to 28:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G450), E438 (= E460)
- binding tryptophan: L33 (= L47), E34 (= E48), S35 (= S49), G39 (= G57), Y41 (= Y59), P242 (= P264), Y243 (= Y265), M244 (≠ L266), Q406 (≠ D428), N408 (≠ C430)
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)
39% identity, 99% coverage: 3:471/475 of query aligns to 26:511/524 of A0QX93
- K355 (≠ S315) 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)
38% identity, 99% coverage: 3:471/475 of query aligns to 6:490/505 of 5cwaA
- active site: Q248 (= Q235), E301 (= E282), A317 (= A298), E345 (= E326), H382 (= H363), T409 (= T390), Y433 (= Y414), R453 (= R434), G469 (= G450), E482 (= E463), K486 (= K467)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y414), I452 (= I433), A466 (= A447), G467 (= G448), K486 (= K467)
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)
37% identity, 98% coverage: 9:475/475 of query aligns to 87:585/595 of P32068
- D341 (≠ R249) 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)
37% identity, 98% coverage: 9:475/475 of query aligns to 71:567/577 of Q94GF1
- D323 (≠ R249) mutation to N: Insensitive to feedback inhibition by tryptophan.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
38% identity, 99% coverage: 3:471/475 of query aligns to 6:486/499 of 7bvdA
- active site: Q248 (= Q235), E301 (= E282), A317 (= A298), E341 (= E326), H378 (= H363), T405 (= T390), Y429 (= Y414), R449 (= R434), G465 (= G450), E478 (= E463), K482 (= K467)
- binding pyruvic acid: S93 (≠ E89), G94 (≠ D90), A100 (≠ V95)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
37% identity, 75% coverage: 118:475/475 of query aligns to 139:501/511 of 1i7sA
- active site: Q254 (= Q235), E300 (= E282), A318 (= A298), E352 (= E326), H389 (= H363), T416 (= T390), Y440 (= Y414), R460 (= R434), G476 (= G450), E489 (= E463), K493 (= K467)
- binding tryptophan: P282 (= P264), Y283 (= Y265), M284 (≠ L266), V444 (= V418), G445 (= G419), D454 (= D428), C456 (= C430)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
37% identity, 75% coverage: 118:475/475 of query aligns to 145:507/517 of 1i7qA
- active site: Q260 (= Q235), E306 (= E282), A324 (= A298), E358 (= E326), H395 (= H363), T422 (= T390), Y446 (= Y414), R466 (= R434), G482 (= G450), E495 (= E463), K499 (= K467)
- binding magnesium ion: E358 (= E326), E495 (= E463)
- binding pyruvic acid: Y446 (= Y414), I465 (= I433), R466 (= R434), A479 (= A447), G480 (= G448), K499 (= K467)
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, 75% coverage: 118:475/475 of query aligns to 148:510/520 of P00898
- C174 (≠ I145) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N261) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P262) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L266) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F267) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G278) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ K367) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G425) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C430) 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)
37% identity, 75% coverage: 118:475/475 of query aligns to 144:506/512 of 1i1qA
- active site: Q259 (= Q235), E305 (= E282), A323 (= A298), E357 (= E326), H394 (= H363), T421 (= T390), Y445 (= Y414), R465 (= R434), G481 (= G450), E494 (= E463), K498 (= K467)
- binding tryptophan: P287 (= P264), Y288 (= Y265), M289 (≠ L266), G450 (= G419), C461 (= C430)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
36% identity, 75% coverage: 118:475/475 of query aligns to 147:509/519 of P00897
- PYM 290:292 (≠ PYL 264:266) binding L-tryptophan
- E360 (= E326) binding Mg(2+)
- E497 (= E463) 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)
31% identity, 91% coverage: 45:474/475 of query aligns to 32:451/453 of P05041
- S36 (= S49) binding L-tryptophan
- E258 (= E282) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A298) 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 (= G299) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R335) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ K340) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T346) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H363) 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)
30% identity, 91% coverage: 45:474/475 of query aligns to 30:435/437 of 1k0eA
- active site: E256 (= E282), K272 (≠ A298), E286 (= E326), H323 (= H363), S350 (≠ T390), W374 (≠ Y414), R394 (= R434), G410 (= G450), E423 (= E463), K427 (= K467)
- binding tryptophan: L32 (= L47), H33 (≠ E48), S34 (= S49), Y41 (≠ K56), F44 (≠ Y59), P238 (= P264), F239 (≠ Y265), S240 (≠ L266)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
28% identity, 91% coverage: 45:474/475 of query aligns to 32:415/415 of 1k0gB
- active site: E258 (= E282), K274 (≠ A298), E277 (= E326), S330 (≠ T390), W354 (≠ Y414), R374 (= R434), G390 (= G450), E403 (= E463), K407 (= K467)
- binding phosphate ion: Y112 (= Y122), D113 (= D123), R116 (≠ K126), D344 (= D404), R350 (≠ K410)
- binding tryptophan: L34 (= L47), H35 (≠ E48), S36 (= S49), Y43 (≠ K56), S44 (≠ G57), R45 (= R58), F46 (≠ Y59), P240 (= P264), F241 (≠ Y265)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
28% identity, 91% coverage: 45:474/475 of query aligns to 32:418/420 of 1k0gA
- active site: E258 (= E282), K274 (= K322), E278 (= E326), S333 (≠ T390), W357 (≠ Y414), R377 (= R434), G393 (= G450), E406 (= E463), K410 (= K467)
- binding phosphate ion: D113 (= D123), R116 (≠ K126), D347 (= D404), R353 (≠ K410)
- binding tryptophan: L34 (= L47), H35 (≠ E48), S36 (= S49), Y43 (≠ K56), S44 (≠ G57), F46 (≠ Y59), P240 (= P264), F241 (≠ Y265), S242 (≠ L266)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
28% identity, 90% coverage: 43:471/475 of query aligns to 227:666/673 of 8hx8A
- binding magnesium ion: E521 (= E326), E655 (= E460), E658 (= E463)
- binding tryptophan: L231 (= L47), D232 (≠ E48), S233 (= S49), S241 (≠ G57), F243 (≠ Y59), P458 (= P264), Y459 (= Y265), G460 (≠ L266), G614 (= G419)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
29% identity, 90% coverage: 43:471/475 of query aligns to 185:627/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I297), K454 (≠ A298), G455 (= G299), T456 (= T300), M547 (≠ V391), Y570 (= Y414), R590 (= R434), V603 (≠ A447), G604 (= G448), G605 (= G449), A606 (≠ G450), E619 (= E463), K623 (= K467)
- binding tryptophan: L189 (= L47), D190 (≠ E48), S191 (= S49), S199 (≠ G57), F201 (≠ Y59), P419 (= P264), Y420 (= Y265), G421 (≠ L266), L574 (≠ V418), G575 (= G419)
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)
28% identity, 55% coverage: 205:467/475 of query aligns to 137:398/408 of 2fn1A
- active site: K167 (≠ Q235), E214 (= E282), A230 (= A298), E258 (= E326), H295 (= H363), T322 (= T390), Y346 (= Y414), R365 (= R434), G381 (= G450), E394 (= E463), K398 (= K467)
- binding magnesium ion: E258 (= E326), E394 (= E463)
- binding pyruvic acid: Y346 (= Y414), L364 (≠ I433), R365 (= R434), A378 (= A447), G379 (= G448), K398 (= K467)
Query Sequence
>WP_010966440.1 NCBI__GCF_000008765.1:WP_010966440.1
MYNISEEQFNDNKKLKKAFQVIYEENGDEITPISLFYNLEGKNKFLLESNLFSESKGRYS
FIGANPYAIIKGFSNNTEIIRNGYVKKVEDKFLKVARKLTEEGKIEKSKYPFCGGGVGYV
GYDIIKQYEKIPSLNEDDLKIPDAILMFYKKIICYDHVKNSIVYIYNVFREDDKSYKEIK
QELFELSEISKKTREMHKLPESHNPANISSNFTKDEFCKMVKKAQEYIVKGDIFQMVPSQ
RFVMDIDERPFNVYRRLRGKNPSPYLFYIDFNDFQVTGSSPESLVCVFKDRVITNPIAGT
RPRGKNEQEDIKLKSELINDEKEIAEHSMLLDLARNDIGKISEFGTVTVDKFMEVELYSH
VMHIVSKVSGRLKKEYDCFEALKSCLPAGTVSGAPKIRAMEIIDELENTKRGCYAGAVGY
FSYDGNMDTCIAIRTLVIKEGKAYAQAGGGVVYDSIPENEYEESMNKSQILKEVI
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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