SitesBLAST
Comparing WP_012542057.1 NCBI__GCF_000025465.1:WP_012542057.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
85% identity, 100% coverage: 1:520/520 of query aligns to 1:520/520 of P00898
- E39 (= E39) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S40) binding L-tryptophan; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (= A41) mutation to V: Decrease in feedback control by tryptophan.
- K50 (= K50) binding L-tryptophan
- R128 (= R128) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (= C174) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N288) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P289) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M293) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F294) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G305) mutation to S: Decrease in feedback control by tryptophan.
- R402 (= R402) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G460) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C465) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
- H515 (= H515) mutation to Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
85% identity, 98% coverage: 5:516/520 of query aligns to 1:512/512 of 1i1qA
- active site: Q259 (= Q263), E305 (= E309), A323 (= A327), E357 (= E361), H394 (= H398), T421 (= T425), Y445 (= Y449), R465 (= R469), G481 (= G485), E494 (= E498), K498 (= K502)
- binding tryptophan: L34 (= L38), E35 (= E39), S36 (= S40), K46 (= K50), P287 (= P291), Y288 (= Y292), M289 (= M293), G450 (= G454), C461 (= C465)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
75% identity, 99% coverage: 4:520/520 of query aligns to 1:517/517 of 1i7qA
- active site: Q260 (= Q263), E306 (= E309), A324 (= A327), E358 (= E361), H395 (= H398), T422 (= T425), Y446 (= Y449), R466 (= R469), G482 (= G485), E495 (= E498), K499 (= K502)
- binding magnesium ion: E358 (= E361), E495 (= E498)
- binding pyruvic acid: Y446 (= Y449), I465 (= I468), R466 (= R469), A479 (= A482), G480 (= G483), K499 (= K502)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
74% identity, 100% coverage: 3:520/520 of query aligns to 2:519/519 of P00897
- S39 (= S40) binding L-tryptophan
- PYM 290:292 (= PYM 291:293) binding L-tryptophan
- E360 (= E361) binding Mg(2+)
- E497 (= E498) binding Mg(2+)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
74% identity, 99% coverage: 4:520/520 of query aligns to 1:511/511 of 1i7sA
- active site: Q254 (= Q263), E300 (= E309), A318 (= A327), E352 (= E361), H389 (= H398), T416 (= T425), Y440 (= Y449), R460 (= R469), G476 (= G485), E489 (= E498), K493 (= K502)
- binding tryptophan: L35 (= L38), E36 (= E39), S37 (= S40), P282 (= P291), Y283 (= Y292), M284 (= M293), V444 (= V453), G445 (= G454), D454 (= D463), C456 (= C465)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
42% identity, 69% coverage: 148:507/520 of query aligns to 125:491/505 of 5cwaA
- active site: Q248 (= Q263), E301 (= E309), A317 (= A327), E345 (= E361), H382 (= H398), T409 (= T425), Y433 (= Y449), R453 (= R469), G469 (= G485), E482 (= E498), K486 (= K502)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y449), I452 (= I468), A466 (= A482), G467 (= G483), K486 (= K502)
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)
36% identity, 94% coverage: 19:507/520 of query aligns to 53:512/524 of A0QX93
- K355 (≠ L350) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 94% coverage: 19:507/520 of query aligns to 33:487/499 of 7bvdA
- active site: Q248 (= Q263), E301 (= E309), A317 (= A327), E341 (= E361), H378 (= H398), T405 (= T425), Y429 (= Y449), R449 (= R469), G465 (= G485), E478 (= E498), K482 (= K502)
- binding pyruvic acid: S93 (≠ N94), G94 (≠ Q95), A100 (= A126)
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)
36% identity, 74% coverage: 128:512/520 of query aligns to 88:476/489 of O94582
- S390 (= S427) modified: Phosphoserine
- S392 (≠ A429) 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)
37% identity, 70% coverage: 148:510/520 of query aligns to 177:567/577 of Q94GF1
- D323 (≠ S276) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
37% identity, 70% coverage: 148:510/520 of query aligns to 104:460/470 of P28820
- A283 (= A327) 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
36% identity, 70% coverage: 148:510/520 of query aligns to 102:453/459 of 7pi1DDD
Sites not aligning to the query:
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)
35% identity, 71% coverage: 146:516/520 of query aligns to 193:591/595 of P32068
- D341 (≠ S276) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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, 80% coverage: 97:512/520 of query aligns to 52:453/453 of P05041
- E258 (= E309) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A327) 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 (= G328) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R370) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R375) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S381) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H398) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
29% identity, 80% coverage: 97:512/520 of query aligns to 50:437/437 of 1k0eA
- active site: E256 (= E309), K272 (≠ A327), E286 (= E361), H323 (= H398), S350 (≠ T425), W374 (≠ Y449), R394 (= R469), G410 (= G485), E423 (= E498), K427 (= K502)
- binding tryptophan: P238 (= P291), F239 (≠ Y292), S240 (≠ M293)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
30% identity, 70% coverage: 148:510/520 of query aligns to 269:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I326), K454 (≠ A327), G455 (= G328), T456 (= T329), M547 (≠ L426), Y570 (= Y449), R590 (= R469), V603 (≠ A482), G604 (= G483), G605 (≠ A484), A606 (≠ G485), E619 (= E498), K623 (= K502)
- binding tryptophan: P419 (= P291), Y420 (= Y292), G421 (≠ M293), L574 (≠ V453), G575 (= G454)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
30% identity, 70% coverage: 148:510/520 of query aligns to 311:670/673 of 8hx8A
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
28% identity, 80% coverage: 97:512/520 of query aligns to 52:420/420 of 1k0gA
- active site: E258 (= E309), K274 (= K357), E278 (= E361), S333 (≠ T425), W357 (≠ Y449), R377 (= R469), G393 (= G485), E406 (= E498), K410 (= K502)
- binding phosphate ion: D113 (= D153), R116 (≠ A156), D347 (≠ A439), R353 (= R445)
- binding tryptophan: P240 (= P291), F241 (≠ Y292), S242 (≠ M293)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
27% identity, 80% coverage: 97:510/520 of query aligns to 52:415/415 of 1k0gB
- active site: E258 (= E309), K274 (≠ A327), E277 (= E361), S330 (≠ T425), W354 (≠ Y449), R374 (= R469), G390 (= G485), E403 (= E498), K407 (= K502)
- binding phosphate ion: Y112 (= Y152), D113 (= D153), R116 (≠ A156), D344 (≠ A439), R350 (= R445)
- binding tryptophan: P240 (= P291), F241 (≠ Y292)
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, 55% coverage: 216:502/520 of query aligns to 120:398/408 of 2fn1A
- active site: K167 (≠ Q263), E214 (= E309), A230 (= A327), E258 (= E361), H295 (= H398), T322 (= T425), Y346 (= Y449), R365 (= R469), G381 (= G485), E394 (= E498), K398 (= K502)
- binding magnesium ion: E258 (= E361), E394 (= E498)
- binding pyruvic acid: Y346 (= Y449), L364 (≠ I468), R365 (= R469), A378 (= A482), G379 (= G483), K398 (= K502)
Query Sequence
>WP_012542057.1 NCBI__GCF_000025465.1:WP_012542057.1
MQTSKPALELLTSDAIYRENPTALFHQLCGARPATLLLESADIDSKDDLKSLLLVDSALR
ITALGDTVTIQALSANGAALLELLDGALPSGIANQRQPNGRILTFPAVSTLLDEDARLCS
LSVFDAFRLLQELVTVPANEREAMFFGGLFAYDLVAGFEDLPPLQSDTACPDYCFYLAET
LLVIDHQTKHTRIQASLFTPLESEKQRLEQRLSQLRQQLNEPPAPLPVTTVAEMQCDVDQ
SDEEYGAVVRKMQRAIRAGEIFQVVPSRRFSLPCPSPLAAYDVLKKSNPSPYMFFMQDND
FTLFGASPESSLKYDAVSRQIEIYPIAGTRPRGRRADGSLDRDLDSRIELEMRTDHKELS
EHLMLVDLARNDLARICTPGSRYVADLTKVDRYSFVMHLVSRVVGELRQDLDVLHAYRAC
MNMGTLSGAPKVRAMQLIAAAEGKRRGSYGGAVGYFTAHGDLDTCIVIRSAYVQEGIATV
QAGAGIVLDSVPQSEADETRNKARAVLRAIAQAHHAKEIF
Or try a new SitesBLAST search
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