SitesBLAST
Comparing N515DRAFT_2134 FitnessBrowser__Dyella79:N515DRAFT_2134 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)
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)
44% identity, 91% coverage: 39:520/529 of query aligns to 26:513/524 of A0QX93
- K355 (≠ E362) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
41% identity, 91% coverage: 44:522/529 of query aligns to 52:567/577 of Q94GF1
- D323 (≠ R296) mutation to N: Insensitive to feedback inhibition by tryptophan.
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, 92% coverage: 38:522/529 of query aligns to 62:585/595 of P32068
- D341 (≠ R296) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
44% identity, 92% coverage: 35:520/529 of query aligns to 2:492/505 of 5cwaA
- active site: Q248 (= Q282), E301 (= E329), A317 (= A345), E345 (= E373), H382 (= H410), T409 (= T437), Y433 (= Y461), R453 (= R481), G469 (= G497), E482 (= E510), K486 (= K514)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y461), I452 (= I480), A466 (= A494), G467 (= G495), K486 (= K514)
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, 90% coverage: 54:527/529 of query aligns to 20:479/489 of O94582
- S390 (= S439) modified: Phosphoserine
- S392 (≠ A441) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 91% coverage: 39:520/529 of query aligns to 6:488/499 of 7bvdA
- active site: Q248 (= Q282), E301 (= E329), A317 (= A345), E341 (= E373), H378 (= H410), T405 (= T437), Y429 (= Y461), R449 (= R481), G465 (= G497), E478 (= E510), K482 (= K514)
- binding pyruvic acid: S93 (= S120), G94 (= G121), A100 (≠ E135)
7pi1DDD Aminodeoxychorismate synthase component 1
38% identity, 88% coverage: 55:522/529 of query aligns to 8:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G497), E438 (= E507)
- binding tryptophan: L33 (≠ F85), E34 (= E86), S35 (= S87), G39 (= G91), Y41 (= Y97), P242 (= P311), Y243 (= Y312), M244 (= M313), Q406 (≠ D475), N408 (≠ A477)
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)
38% identity, 88% coverage: 55:522/529 of query aligns to 10:460/470 of P28820
- A283 (= A345) 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.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
41% identity, 70% coverage: 156:525/529 of query aligns to 138:504/511 of 1i7sA
- active site: Q254 (= Q282), E300 (= E329), A318 (= A345), E352 (= E373), H389 (= H410), T416 (= T437), Y440 (= Y461), R460 (= R481), G476 (= G497), E489 (= E510), K493 (= K514)
- binding tryptophan: P282 (= P311), Y283 (= Y312), M284 (= M313), V444 (≠ I465), G445 (= G466), D454 (= D475), C456 (≠ A477)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
41% identity, 70% coverage: 156:525/529 of query aligns to 144:510/517 of 1i7qA
- active site: Q260 (= Q282), E306 (= E329), A324 (= A345), E358 (= E373), H395 (= H410), T422 (= T437), Y446 (= Y461), R466 (= R481), G482 (= G497), E495 (= E510), K499 (= K514)
- binding magnesium ion: E358 (= E373), E495 (= E510)
- binding pyruvic acid: Y446 (= Y461), I465 (= I480), R466 (= R481), A479 (= A494), G480 (= G495), K499 (= K514)
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, 72% coverage: 144:525/529 of query aligns to 135:513/520 of P00898
- C174 (≠ L189) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N308) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P309) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M313) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y314) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G325) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ Q414) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G472) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A477) 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 ; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding
- 128 R→H: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
40% identity, 70% coverage: 156:525/529 of query aligns to 146:512/519 of P00897
Sites not aligning to the query:
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
37% identity, 72% coverage: 144:525/529 of query aligns to 131:509/512 of 1i1qA
- active site: Q259 (= Q282), E305 (= E329), A323 (= A345), E357 (= E373), H394 (= H410), T421 (= T437), Y445 (= Y461), R465 (= R481), G481 (= G497), E494 (= E510), K498 (= K514)
- binding tryptophan: P287 (= P311), Y288 (= Y312), M289 (= M313), G450 (= G466), C461 (≠ A477)
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)
30% identity, 85% coverage: 73:522/529 of query aligns to 22:451/453 of P05041
- S36 (= S87) binding
- E258 (= E329) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A345) 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 (= G346) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R382) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R387) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S393) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H410) 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, 85% coverage: 73:522/529 of query aligns to 20:435/437 of 1k0eA
- active site: E256 (= E329), K272 (≠ A345), E286 (= E373), H323 (= H410), S350 (≠ T437), W374 (≠ Y461), R394 (= R481), G410 (= G497), E423 (= E510), K427 (= K514)
- binding tryptophan: L32 (≠ F85), H33 (≠ E86), S34 (= S87), Y41 (≠ W94), F44 (≠ Y97), P238 (= P311), F239 (≠ Y312), S240 (≠ M313)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
33% identity, 73% coverage: 137:522/529 of query aligns to 246:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (≠ L344), K454 (≠ A345), G455 (= G346), T456 (= T347), M547 (≠ L438), Y570 (= Y461), R590 (= R481), V603 (≠ A494), G604 (= G495), G605 (≠ A496), A606 (≠ G497), E619 (= E510), K623 (= K514)
- binding tryptophan: P419 (= P311), Y420 (= Y312), G421 (≠ M313), L574 (≠ I465), G575 (= G466)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
34% identity, 73% coverage: 137:522/529 of query aligns to 288:670/673 of 8hx8A
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
28% identity, 85% coverage: 73:522/529 of query aligns to 22:418/420 of 1k0gA
- active site: E258 (= E329), K274 (= K369), E278 (= E373), S333 (≠ T437), W357 (≠ Y461), R377 (= R481), G393 (= G497), E406 (= E510), K410 (= K514)
- binding phosphate ion: D113 (≠ E165), R116 (≠ G168), D347 (≠ Q451), R353 (≠ K457)
- binding tryptophan: L34 (≠ F85), H35 (≠ E86), S36 (= S87), Y43 (≠ W94), S44 (≠ G95), F46 (≠ Y97), P240 (= P311), F241 (≠ Y312), S242 (≠ M313)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
27% identity, 85% coverage: 73:522/529 of query aligns to 22:415/415 of 1k0gB
- active site: E258 (= E329), K274 (≠ A345), E277 (= E373), S330 (≠ T437), W354 (≠ Y461), R374 (= R481), G390 (= G497), E403 (= E510), K407 (= K514)
- binding phosphate ion: Y112 (≠ F164), D113 (≠ E165), R116 (≠ G168), D344 (≠ Q451), R350 (≠ K457)
- binding tryptophan: L34 (≠ F85), H35 (≠ E86), S36 (= S87), Y43 (≠ W94), S44 (≠ G95), R45 (= R96), F46 (≠ Y97), P240 (= P311), F241 (≠ Y312)
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)
32% identity, 49% coverage: 243:499/529 of query aligns to 157:409/435 of 2g5fA
- active site: K191 (≠ Q282), E238 (= E329), A255 (= A345), E283 (= E373), H320 (= H410), T347 (= T437), Y371 (= Y461), R391 (= R481), G407 (= G497)
- binding pyruvic acid: Y371 (= Y461), L390 (≠ I480), R391 (= R481), G405 (= G495)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_2134 FitnessBrowser__Dyella79:N515DRAFT_2134
MAREGHKHKLRGPFGSLHAYVYNGRLECLPHGFPDSPNVISREQFDALAAQGHTRIPLVR
EVFSDLDTPLSVYLKLADGPYTFLFESVEGGATWGRYSIIGLPARRVYRLRGHELEVEDS
GEVTERRHLDDPLGEIEKLRRQYDVPRLPQLPAFSGGLVGYFGFETIGYIEPRLARWDRA
DELGTPDVLLMLAEEVAVFDNLKGRLYLIVHADPARPHAYAEAQRRLDALVHRLRQGGAS
YPQLTQSVALDEGDFKSSFTKEEFEAMVERAKEYIRAGDIFQVVPSQRLSVGFNARPVDV
YRALRALNPSPYMYFVDLGDTQIVGSSPEILARLKDGKVVVRPLAGTRRRGATEAEDLAL
EEELLADPKERAEHVMLIDLGRNDIGRISETGSVEVSESFVVERYSHVMHIVSQVQGKVR
PEVGYMDVLKATFPAGTLSGAPKIRALEIIQELEPYKRNIYAGAIGWIGWWGDADTAIAI
RTAVIQDGRLHVQAGAGIVYDSDPTAEWEETMNKGRALFRAVAQAAKGL
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