SitesBLAST
Comparing WP_005458381.1 NCBI__GCF_000244975.1:WP_005458381.1 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)
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)
69% identity, 93% coverage: 20:499/517 of query aligns to 28:513/524 of A0QX93
- K355 (= K341) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
69% identity, 93% coverage: 20:499/517 of query aligns to 8:488/499 of 7bvdA
- active site: Q248 (= Q261), E301 (= E308), A317 (= A324), E341 (= E352), H378 (= H389), T405 (= T416), Y429 (= Y440), R449 (= R460), G465 (= G476), E478 (= E489), K482 (= K493)
- binding pyruvic acid: S93 (≠ T106), G94 (≠ E107), A100 (≠ I113)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
67% identity, 93% coverage: 20:499/517 of query aligns to 8:492/505 of 5cwaA
- active site: Q248 (= Q261), E301 (= E308), A317 (= A324), E345 (= E352), H382 (= H389), T409 (= T416), Y433 (= Y440), R453 (= R460), G469 (= G476), E482 (= E489), K486 (= K493)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y440), I452 (= I459), A466 (= A473), G467 (= G474), K486 (= K493)
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)
41% identity, 95% coverage: 16:507/517 of query aligns to 2:480/489 of O94582
- S390 (= S418) modified: Phosphoserine
- S392 (≠ A420) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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, 93% coverage: 28:506/517 of query aligns to 74:590/595 of P32068
- D341 (= D275) 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)
41% identity, 92% coverage: 33:506/517 of query aligns to 63:572/577 of Q94GF1
- D323 (= D275) 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)
40% identity, 91% coverage: 35:505/517 of query aligns to 6:464/470 of P28820
- A283 (= A324) 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: 35:505/517 of query aligns to 4:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G476), E438 (= E486)
- binding tryptophan: L33 (= L64), E34 (= E65), S35 (= S66), G39 (= G70), Y41 (≠ W76), P242 (= P290), Y243 (= Y291), M244 (= M292), Q406 (≠ D454), N408 (≠ A456)
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
37% identity, 91% coverage: 35:504/517 of query aligns to 2:509/512 of 1i1qA
- active site: Q259 (= Q261), E305 (= E308), A323 (= A324), E357 (= E352), H394 (= H389), T421 (= T416), Y445 (= Y440), R465 (= R460), G481 (= G476), E494 (= E489), K498 (= K493)
- binding tryptophan: L34 (= L64), E35 (= E65), S36 (= S66), K46 (≠ W76), P287 (= P290), Y288 (= Y291), M289 (= M292), G450 (= G445), C461 (≠ A456)
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, 91% coverage: 35:504/517 of query aligns to 6:513/520 of P00898
- E39 (= E65) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S66) binding L-tryptophan; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (= A67) mutation to V: Decrease in feedback control by tryptophan.
- K50 (≠ W76) binding L-tryptophan
- R128 (vs. gap) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ T165) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N287) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P288) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M292) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y293) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G304) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T393) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G451) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A456) 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.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
36% identity, 89% coverage: 47:504/517 of query aligns to 18:510/517 of 1i7qA
- active site: Q260 (= Q261), E306 (= E308), A324 (= A324), E358 (= E352), H395 (= H389), T422 (= T416), Y446 (= Y440), R466 (= R460), G482 (= G476), E495 (= E489), K499 (= K493)
- binding magnesium ion: E358 (= E352), E495 (= E489)
- binding pyruvic acid: Y446 (= Y440), I465 (= I459), R466 (= R460), A479 (= A473), G480 (= G474), K499 (= K493)
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)
34% identity, 90% coverage: 35:501/517 of query aligns to 6:451/453 of P05041
- S36 (= S66) binding L-tryptophan
- E258 (= E308) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A324) 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 (= G325) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R361) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ K366) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T372) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H389) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
36% identity, 89% coverage: 47:504/517 of query aligns to 20:512/519 of P00897
- S39 (= S66) binding L-tryptophan
- PYM 290:292 (= PYM 290:292) binding L-tryptophan
- E360 (= E352) binding Mg(2+)
- E497 (= E489) binding Mg(2+)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
41% identity, 71% coverage: 136:504/517 of query aligns to 137:504/511 of 1i7sA
- active site: Q254 (= Q261), E300 (= E308), A318 (= A324), E352 (= E352), H389 (= H389), T416 (= T416), Y440 (= Y440), R460 (= R460), G476 (= G476), E489 (= E489), K493 (= K493)
- binding tryptophan: P282 (= P290), Y283 (= Y291), M284 (= M292), V444 (= V444), G445 (= G445), D454 (= D454), C456 (≠ A456)
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
33% identity, 90% coverage: 35:501/517 of query aligns to 4:435/437 of 1k0eA
- active site: E256 (= E308), K272 (≠ A324), E286 (= E352), H323 (= H389), S350 (≠ T416), W374 (≠ Y440), R394 (= R460), G410 (= G476), E423 (= E489), K427 (= K493)
- binding tryptophan: L32 (= L64), H33 (≠ E65), S34 (= S66), Y41 (≠ W73), F44 (≠ W76), P238 (= P290), F239 (≠ Y291), S240 (≠ M292)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 90% coverage: 35:501/517 of query aligns to 6:418/420 of 1k0gA
- active site: E258 (= E308), K274 (= K348), E278 (= E352), S333 (≠ T416), W357 (≠ Y440), R377 (= R460), G393 (= G476), E406 (= E489), K410 (= K493)
- binding phosphate ion: D113 (= D143), R116 (= R146), D347 (≠ E430), R353 (= R436)
- binding tryptophan: L34 (= L64), H35 (≠ E65), S36 (= S66), Y43 (≠ W73), S44 (= S74), F46 (≠ W76), P240 (= P290), F241 (≠ Y291), S242 (≠ M292)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
35% identity, 85% coverage: 61:501/517 of query aligns to 186:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I323), K454 (≠ A324), G455 (= G325), T456 (= T326), M547 (≠ L417), Y570 (= Y440), R590 (= R460), V603 (≠ A473), G604 (= G474), G605 (= G475), A606 (≠ G476), E619 (= E489), K623 (= K493)
- binding tryptophan: L189 (= L64), D190 (≠ E65), S191 (= S66), S199 (= S74), F201 (≠ W76), P419 (= P290), Y420 (= Y291), G421 (≠ M292), L574 (≠ V444), G575 (= G445)
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, 85% coverage: 61:501/517 of query aligns to 228:670/673 of 8hx8A
- binding magnesium ion: E521 (= E352), E655 (= E486), E658 (= E489)
- binding tryptophan: L231 (= L64), D232 (≠ E65), S233 (= S66), S241 (= S74), F243 (≠ W76), P458 (= P290), Y459 (= Y291), G460 (≠ M292), G614 (= G445)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 90% coverage: 35:501/517 of query aligns to 6:415/415 of 1k0gB
- active site: E258 (= E308), K274 (≠ A324), E277 (= E352), S330 (≠ T416), W354 (≠ Y440), R374 (= R460), G390 (= G476), E403 (= E489), K407 (= K493)
- binding phosphate ion: Y112 (= Y142), D113 (= D143), R116 (= R146), D344 (≠ E430), R350 (= R436)
- binding tryptophan: L34 (= L64), H35 (≠ E65), S36 (= S66), Y43 (≠ W73), S44 (= S74), R45 (= R75), F46 (≠ W76), P240 (= P290), F241 (≠ Y291)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
33% identity, 50% coverage: 241:497/517 of query aligns to 163:418/424 of 5jy9B
- active site: K183 (≠ Q261), E230 (= E308), A246 (= A324), E274 (= E352), H311 (= H389), T338 (= T416), Y362 (= Y440), R381 (= R460), G397 (= G476), E410 (= E489), K414 (= K493)
- binding fe (ii) ion: E274 (= E352), E410 (= E489)
Query Sequence
>WP_005458381.1 NCBI__GCF_000244975.1:WP_005458381.1
MVTAQNSHTAARGLGEVGPSRDDFRALARDRRVIPVVRRLLADADTPVALYRKLAGDRPG
TFLLESAENGQSWSRWSFVGVDSRAALTVRDGKAVWTGKPVAGLPTEGDPLTILRETLQK
LHTEPLPGMPPLTGGLVGYIGYDAVRWLERLPELAERDLDIPEVTMLLATDLAAFDHHEG
TVTLIANAVNWDDSPERVDAAYDDALRRLDVMTERLASPAPATNAVFERPAPEFTRKRTK
EDFHAAVHKAVEAIHAGEAFQIVPSQRFEMRTDADALDVYRVLRTSNPSPYMYLLRLEGF
DIVGSSPESLVTVRDGRASTHPIAGTRWRGADPEEDAQLAKDLLADEKERAEHLMLVDLG
RNDLGKVCRPGTVRVVDSFTIERYSHVMHIVSTVTGELADDATAFDAVLACFPAGTLSGA
PKVRAMELIEELEPTRRALYGGIVGYLDFAGDADTAIAIRTALMRDGVAYVQAGGGVVAD
SDADYEDNESLNKARTVLSAVAAADTMAPAKAADPGA
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