SitesBLAST
Comparing 6937996 FitnessBrowser__SB2B:6937996 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)
55% identity, 94% coverage: 26:521/527 of query aligns to 17:510/520 of P00898
- E39 (= E48) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S49) binding ; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (= A50) mutation to V: Decrease in feedback control by tryptophan.
- K50 (= K59) binding
- R128 (= R134) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ L182) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N299) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P300) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M304) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F305) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G316) mutation to S: Decrease in feedback control by tryptophan.
- R402 (= R413) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G471) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C476) 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)
55% identity, 94% coverage: 26:521/527 of query aligns to 13:506/512 of 1i1qA
- active site: Q259 (= Q274), E305 (= E320), A323 (= A338), E357 (= E372), H394 (= H409), T421 (= T436), Y445 (= Y460), R465 (= R480), G481 (= G496), E494 (= E509), K498 (= K513)
- binding tryptophan: L34 (= L47), E35 (= E48), S36 (= S49), K46 (= K59), P287 (= P302), Y288 (= Y303), M289 (= M304), G450 (= G465), C461 (= C476)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
54% identity, 94% coverage: 26:521/527 of query aligns to 14:507/517 of 1i7qA
- active site: Q260 (= Q274), E306 (= E320), A324 (= A338), E358 (= E372), H395 (= H409), T422 (= T436), Y446 (= Y460), R466 (= R480), G482 (= G496), E495 (= E509), K499 (= K513)
- binding magnesium ion: E358 (= E372), E495 (= E509)
- binding pyruvic acid: Y446 (= Y460), I465 (= I479), R466 (= R480), A479 (= A493), G480 (= G494), K499 (= K513)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
53% identity, 95% coverage: 19:521/527 of query aligns to 9:509/519 of P00897
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
53% identity, 94% coverage: 26:521/527 of query aligns to 14:501/511 of 1i7sA
- active site: Q254 (= Q274), E300 (= E320), A318 (= A338), E352 (= E372), H389 (= H409), T416 (= T436), Y440 (= Y460), R460 (= R480), G476 (= G496), E489 (= E509), K493 (= K513)
- binding tryptophan: L35 (= L47), E36 (= E48), S37 (= S49), P282 (= P302), Y283 (= Y303), M284 (= M304), V444 (= V464), G445 (= G465), D454 (= D474), C456 (= C476)
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, 74% coverage: 129:519/527 of query aligns to 118:513/524 of A0QX93
- K355 (≠ L361) 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, 69% coverage: 155:519/527 of query aligns to 125:492/505 of 5cwaA
- active site: Q248 (= Q274), E301 (= E320), A317 (= A338), E345 (= E372), H382 (= H409), T409 (= T436), Y433 (= Y460), R453 (= R480), G469 (= G496), E482 (= E509), K486 (= K513)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y460), I452 (= I479), A466 (= A493), G467 (= G494), K486 (= K513)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
39% identity, 74% coverage: 129:519/527 of query aligns to 97:488/499 of 7bvdA
- active site: Q248 (= Q274), E301 (= E320), A317 (= A338), E341 (= E372), H378 (= H409), T405 (= T436), Y429 (= Y460), R449 (= R480), G465 (= G496), E478 (= E509), K482 (= K513)
- binding pyruvic acid: A100 (≠ G132)
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)
37% identity, 71% coverage: 150:524/527 of query aligns to 187:588/595 of P32068
- D341 (≠ L283) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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, 75% coverage: 127:522/527 of query aligns to 80:475/489 of O94582
- S390 (≠ T438) modified: Phosphoserine
- S392 (≠ A440) 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)
35% identity, 76% coverage: 124:523/527 of query aligns to 71:462/470 of P28820
- A283 (= A338) 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, 76% coverage: 124:523/527 of query aligns to 69:455/459 of 7pi1DDD
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)
35% identity, 75% coverage: 129:523/527 of query aligns to 148:569/577 of Q94GF1
- D323 (≠ L283) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
29% identity, 81% coverage: 97:522/527 of query aligns to 46:452/453 of P05041
- E258 (= E320) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A338) 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 (= G339) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R381) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R386) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T392) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H409) 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)
28% identity, 81% coverage: 97:522/527 of query aligns to 44:436/437 of 1k0eA
- active site: E256 (= E320), K272 (≠ A338), E286 (= E372), H323 (= H409), S350 (≠ T436), W374 (≠ Y460), R394 (= R480), G410 (= G496), E423 (= E509), K427 (= K513)
- binding tryptophan: F44 (= F97), P238 (= P302), F239 (≠ Y303), S240 (≠ M304)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
31% identity, 73% coverage: 138:521/527 of query aligns to 251:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I337), K454 (≠ A338), G455 (= G339), T456 (= T340), M547 (≠ L437), Y570 (= Y460), R590 (= R480), V603 (≠ A493), G604 (= G494), G605 (≠ A495), A606 (≠ G496), E619 (= E509), K623 (= K513)
- binding tryptophan: P419 (= P302), Y420 (= Y303), G421 (≠ M304), L574 (≠ V464), G575 (= G465)
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, 73% coverage: 138:521/527 of query aligns to 293:670/673 of 8hx8A
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
27% identity, 81% coverage: 97:522/527 of query aligns to 46:419/420 of 1k0gA
- active site: E258 (= E320), K274 (= K368), E278 (= E372), S333 (≠ T436), W357 (≠ Y460), R377 (= R480), G393 (= G496), E406 (= E509), K410 (= K513)
- binding phosphate ion: D113 (= D160), R116 (≠ D163), D347 (≠ R450), R353 (= R456)
- binding tryptophan: F46 (= F97), P240 (= P302), F241 (≠ Y303), S242 (≠ M304)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
27% identity, 81% coverage: 97:521/527 of query aligns to 46:415/415 of 1k0gB
- active site: E258 (= E320), K274 (≠ A338), E277 (= E372), S330 (≠ T436), W354 (≠ Y460), R374 (= R480), G390 (= G496), E403 (= E509), K407 (= K513)
- binding phosphate ion: Y112 (= Y159), D113 (= D160), R116 (≠ D163), D344 (≠ R450), R350 (= R456)
- binding tryptophan: F46 (= F97), P240 (= P302), F241 (≠ Y303)
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)
34% identity, 51% coverage: 250:517/527 of query aligns to 143:402/408 of 2fn1A
- active site: K167 (≠ Q274), E214 (= E320), A230 (= A338), E258 (= E372), H295 (= H409), T322 (= T436), Y346 (= Y460), R365 (= R480), G381 (= G496), E394 (= E509), K398 (= K513)
- binding magnesium ion: E258 (= E372), E394 (= E509)
- binding pyruvic acid: Y346 (= Y460), L364 (≠ I479), R365 (= R480), A378 (= A493), G379 (= G494), K398 (= K513)
Query Sequence
>6937996 FitnessBrowser__SB2B:6937996
MTQQAFDAKAEGKLATGKLTKQPLPYQDDPLALYESLTQDAHHTLLLESAEIDSKENLKS
IIMTHAALKIAAQGYRLEFTALDDNGRVLLPAIAGFFNCELTETNYLAVTLTRDTGLLDE
DARLKSTSPLDGLRALLKHIHVGEKVAFEDLFLGGVLAYDLIDTVEPLPKARDGANTCPD
YLFYLADTLVLVDHKAKQAELVLSTFSADGQISPFIEDELKRRAKVIEAIANRPRPVKAL
KPVNVEASVSISDEDFKDAVNALKEHIIAGDIFQVVPSRSFSLPCPNTLGAYRALRKTNP
SPYMFYFRSSDFTLFGASPESALKYDADSNQVEVYPIAGTRKRGKDASGNIDHDLDGRIE
LELRLDKKELSEHLMLVDLARNDIARISQSGTRKVAELLKVDRYSHVMHLVSRVTGQLRQ
DLDALHAYQACMNMGTLTGAPKVRASQLIRETEKTRRGSYGGAVGYLSATGDMDTCIVIR
SAFVKDGLAHIQAGAGVVYDSDPQAEADETRQKAQAVISAIKLGGGL
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