SitesBLAST
Comparing CCNA_03048 FitnessBrowser__Caulo:CCNA_03048 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)
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)
38% identity, 84% coverage: 87:524/524 of query aligns to 7:453/453 of P05041
- S36 (≠ T114) binding
- E258 (= E325) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K342) 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 (= G343) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R379) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R384) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S390) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H407) 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)
37% identity, 84% coverage: 87:524/524 of query aligns to 5:437/437 of 1k0eA
- active site: E256 (= E325), K272 (= K342), E286 (= E370), H323 (= H407), S350 (= S434), W374 (≠ Y457), R394 (= R477), G410 (= G497), E423 (= E510), K427 (= K514)
- binding tryptophan: L32 (= L112), H33 (≠ V113), S34 (≠ T114), Y41 (vs. gap), F44 (≠ W120), P238 (= P307), F239 (= F308), S240 (= S309)
7pi1DDD Aminodeoxychorismate synthase component 1
34% identity, 75% coverage: 131:522/524 of query aligns to 67:453/459 of 7pi1DDD
Sites not aligning to the query:
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)
34% identity, 75% coverage: 131:522/524 of query aligns to 69:460/470 of P28820
- A283 (≠ K342) 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.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
40% identity, 71% coverage: 152:522/524 of query aligns to 294:670/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
40% identity, 71% coverage: 152:522/524 of query aligns to 252:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I341), K454 (= K342), G455 (= G343), T456 (= T344), M547 (≠ I435), Y570 (= Y457), R590 (= R477), V603 (≠ A494), G604 (= G495), G605 (≠ A496), A606 (≠ G497), E619 (= E510), K623 (= K514)
- binding tryptophan: P419 (= P307), Y420 (≠ F308), G421 (≠ S309), L574 (= L461), G575 (≠ F462)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
34% identity, 84% coverage: 87:524/524 of query aligns to 7:420/420 of 1k0gA
- active site: E258 (= E325), K274 (= K342), E278 (= E370), S333 (= S434), W357 (≠ Y457), R377 (= R477), G393 (= G497), E406 (= E510), K410 (= K514)
- binding phosphate ion: D113 (≠ E173), R116 (≠ D176), D347 (≠ A448), R353 (vs. gap)
- binding tryptophan: L34 (= L112), H35 (≠ V113), S36 (≠ T114), Y43 (vs. gap), S44 (≠ G118), F46 (≠ W120), P240 (= P307), F241 (= F308), S242 (= S309)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
34% identity, 83% coverage: 87:522/524 of query aligns to 7:415/415 of 1k0gB
- active site: E258 (= E325), K274 (= K342), E277 (= E370), S330 (= S434), W354 (≠ Y457), R374 (= R477), G390 (= G497), E403 (= E510), K407 (= K514)
- binding phosphate ion: Y112 (= Y172), D113 (≠ E173), R116 (≠ D176), D344 (≠ A448), R350 (vs. gap)
- binding tryptophan: L34 (= L112), H35 (≠ V113), S36 (≠ T114), Y43 (vs. gap), S44 (≠ G118), R45 (= R119), F46 (≠ W120), P240 (= P307), F241 (= F308)
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)
34% identity, 69% coverage: 162:522/524 of query aligns to 189:585/595 of P32068
- D341 (= D292) 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)
34% identity, 72% coverage: 140:518/524 of query aligns to 97:490/505 of 5cwaA
- active site: Q248 (= Q276), E301 (= E325), A317 (≠ K342), E345 (= E370), H382 (= H407), T409 (≠ S434), Y433 (= Y457), R453 (= R477), G469 (= G497), E482 (= E510), K486 (= K514)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y457), I452 (= I476), 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)
34% identity, 74% coverage: 139:524/524 of query aligns to 80:476/489 of O94582
- S390 (≠ T436) modified: Phosphoserine
- S392 (≠ A438) 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)
33% identity, 70% coverage: 154:522/524 of query aligns to 161:567/577 of Q94GF1
- D323 (= D292) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
33% identity, 76% coverage: 119:518/524 of query aligns to 83:511/524 of A0QX93
- K355 (≠ A359) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
34% identity, 69% coverage: 160:518/524 of query aligns to 117:486/499 of 7bvdA
- active site: Q248 (= Q276), E301 (= E325), A317 (≠ K342), E341 (= E370), H378 (= H407), T405 (≠ S434), Y429 (= Y457), R449 (= R477), G465 (= G497), E478 (= E510), K482 (= K514)
Sites not aligning to the query:
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
33% identity, 73% coverage: 140:522/524 of query aligns to 125:510/520 of P00898
- R128 (≠ A143) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ T192) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ S304) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P305) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S309) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A310) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S321) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T411) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G468) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S473) 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
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
33% identity, 73% coverage: 140:522/524 of query aligns to 121:506/512 of 1i1qA
- active site: Q259 (= Q276), E305 (= E325), A323 (≠ K342), E357 (= E370), H394 (= H407), T421 (≠ S434), Y445 (= Y457), R465 (= R477), G481 (= G497), E494 (= E510), K498 (= K514)
- binding tryptophan: P287 (= P307), Y288 (≠ F308), M289 (≠ S309), G450 (≠ F462), C461 (≠ S473)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
33% identity, 68% coverage: 168:522/524 of query aligns to 147:509/519 of P00897
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
33% identity, 68% coverage: 168:522/524 of query aligns to 145:507/517 of 1i7qA
- active site: Q260 (= Q276), E306 (= E325), A324 (≠ K342), E358 (= E370), H395 (= H407), T422 (≠ S434), Y446 (= Y457), R466 (= R477), G482 (= G497), E495 (= E510), K499 (= K514)
- binding magnesium ion: E358 (= E370), E495 (= E510)
- binding pyruvic acid: Y446 (= Y457), I465 (= I476), R466 (= R477), A479 (= A494), G480 (= G495), K499 (= K514)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
33% identity, 68% coverage: 168:522/524 of query aligns to 139:501/511 of 1i7sA
- active site: Q254 (= Q276), E300 (= E325), A318 (≠ K342), E352 (= E370), H389 (= H407), T416 (≠ S434), Y440 (= Y457), R460 (= R477), G476 (= G497), E489 (= E510), K493 (= K514)
- binding tryptophan: P282 (= P307), Y283 (≠ F308), M284 (≠ S309), V444 (≠ L461), G445 (≠ F462), D454 (= D471), C456 (≠ S473)
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)
33% identity, 52% coverage: 245:518/524 of query aligns to 137:402/408 of 2fn1A
- active site: K167 (≠ Q276), E214 (= E325), A230 (≠ K342), E258 (= E370), H295 (= H407), T322 (≠ S434), Y346 (= Y457), R365 (= R477), G381 (= G497), E394 (= E510), K398 (= K514)
- binding magnesium ion: E258 (= E370), E394 (= E510)
- binding pyruvic acid: Y346 (= Y457), L364 (≠ I476), R365 (= R477), A378 (= A494), G379 (= G495), K398 (= K514)
Query Sequence
>CCNA_03048 FitnessBrowser__Caulo:CCNA_03048
MVTRSAIGPPTIQPSFVIALSGGSVPTHPPTASRWAPPSLRERGVPCGVPSGSGTVSARH
PPPNRPRGLALVSVRRARYHHAMRHVALLTAPWREPVWALAPFRDEPYACALVTGGAGRW
SYLLRAPDATMSLSDKDPADPFAALAALVGPRLPSHPEGPPFQGGVVGLGAYELGDRVED
LGLSRTDWPDLTCARYPALLAFDHHARQVIAVGRGEAEAEANARAADALAWLEVAAPERA
EPAGPLCADLVASDPATYETAVAQVVARIVGGEIFQANIARAWTGRLAAGVDPFDLFVRL
RAQSPAPFSAYWRLPGRALVSNSPERFLKLDAAGAIQTQPIKGTRPRGRDPVEDRALAAE
LLASDKDRAENLMIVDLMRNDLARVSPAGSVRAPELFKVESFANVHHLVSTVTARLAPGR
GVADLLRASFPPGSITGAPKVQAMKVIAELEPPRGPYCGSLFWAGVDGAFDSSVLIRTVG
LVQDGAGWRLEARAGAGIVADSDPRGERLETEAKIAALKTALTQ
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