SitesBLAST
Comparing WP_245546805.1 NCBI__GCF_000384235.1:WP_245546805.1 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)
7pi1DDD Aminodeoxychorismate synthase component 1
43% identity, 72% coverage: 136:488/493 of query aligns to 96:453/459 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)
43% identity, 72% coverage: 136:488/493 of query aligns to 98:460/470 of P28820
- A283 (= A311) 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.
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)
37% identity, 71% coverage: 135:486/493 of query aligns to 139:513/524 of A0QX93
- K355 (≠ R328) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
33% identity, 72% coverage: 136:488/493 of query aligns to 189:585/595 of P32068
- D341 (≠ S262) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
37% identity, 71% coverage: 135:486/493 of query aligns to 118:488/499 of 7bvdA
- active site: Q248 (= Q247), E301 (= E295), A317 (= A311), E341 (= E339), H378 (= H376), T405 (= T403), Y429 (= Y427), R449 (= R447), G465 (= G463), E478 (= E476), K482 (= K480)
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)
34% identity, 84% coverage: 76:490/493 of query aligns to 44:453/453 of P05041
- E258 (= E295) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A311) 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 (= G312) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R348) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R353) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S359) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H376) 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:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
35% identity, 76% coverage: 112:486/493 of query aligns to 86:492/505 of 5cwaA
- active site: Q248 (= Q247), E301 (= E295), A317 (= A311), E345 (= E339), H382 (= H376), T409 (= T403), Y433 (= Y427), R453 (= R447), G469 (= G463), E482 (= E476), K486 (= K480)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y427), I452 (= I446), A466 (= A460), G467 (= G461), K486 (= K480)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
34% identity, 72% coverage: 136:488/493 of query aligns to 171:567/577 of Q94GF1
- D323 (≠ S262) mutation to N: Insensitive to feedback inhibition by tryptophan.
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
33% identity, 84% coverage: 76:490/493 of query aligns to 42:437/437 of 1k0eA
- active site: E256 (= E295), K272 (≠ A311), E286 (= E339), H323 (= H376), S350 (≠ T403), W374 (≠ Y427), R394 (= R447), G410 (= G463), E423 (= E476), K427 (= K480)
- binding tryptophan: F44 (= F78), P238 (= P277), F239 (= F278), S240 (≠ A279)
Sites not aligning to the query:
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)
29% identity, 97% coverage: 11:488/493 of query aligns to 14:474/489 of O94582
- S390 (≠ T405) modified: Phosphoserine
- S392 (≠ C407) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 72% coverage: 132:488/493 of query aligns to 259:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I310), K454 (≠ A311), G455 (= G312), T456 (= T313), M547 (≠ I404), Y570 (= Y427), R590 (= R447), V603 (≠ A460), G604 (= G461), G605 (≠ A462), A606 (≠ G463), E619 (= E476), K623 (= K480)
- binding tryptophan: P419 (= P277), Y420 (≠ F278), G421 (≠ A279), L574 (= L431), G575 (= G432)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 72% coverage: 132:488/493 of query aligns to 301:670/673 of 8hx8A
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, 72% coverage: 136:488/493 of query aligns to 145:510/520 of P00898
- C174 (≠ N162) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N274) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P275) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A279) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A280) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S291) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N380) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G438) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N443) 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 L-tryptophan; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding L-tryptophan
- 128 R→H: Almost no change in feedback control by tryptophan.
- 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, 72% coverage: 136:488/493 of query aligns to 141:506/512 of 1i1qA
- active site: Q259 (= Q247), E305 (= E295), A323 (= A311), E357 (= E339), H394 (= H376), T421 (= T403), Y445 (= Y427), R465 (= R447), G481 (= G463), E494 (= E476), K498 (= K480)
- binding tryptophan: P287 (= P277), Y288 (≠ F278), M289 (≠ A279), G450 (= G432), C461 (≠ N443)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
33% identity, 71% coverage: 138:488/493 of query aligns to 138:501/511 of 1i7sA
- active site: Q254 (= Q247), E300 (= E295), A318 (= A311), E352 (= E339), H389 (= H376), T416 (= T403), Y440 (= Y427), R460 (= R447), G476 (= G463), E489 (= E476), K493 (= K480)
- binding tryptophan: P282 (= P277), Y283 (≠ F278), M284 (≠ A279), V444 (≠ L431), G445 (= G432), D454 (= D441), C456 (≠ N443)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
33% identity, 71% coverage: 138:488/493 of query aligns to 144:507/517 of 1i7qA
- active site: Q260 (= Q247), E306 (= E295), A324 (= A311), E358 (= E339), H395 (= H376), T422 (= T403), Y446 (= Y427), R466 (= R447), G482 (= G463), E495 (= E476), K499 (= K480)
- binding magnesium ion: E358 (= E339), E495 (= E476)
- binding pyruvic acid: Y446 (= Y427), I465 (= I446), R466 (= R447), A479 (= A460), G480 (= G461), K499 (= K480)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 84% coverage: 76:490/493 of query aligns to 44:420/420 of 1k0gA
- active site: E258 (= E295), K274 (= K335), E278 (= E339), S333 (≠ T403), W357 (≠ Y427), R377 (= R447), G393 (= G463), E406 (= E476), K410 (= K480)
- binding phosphate ion: D113 (≠ E147), R116 (vs. gap), D347 (≠ A417), R353 (≠ P423)
- binding tryptophan: S44 (≠ G76), F46 (= F78), P240 (= P277), F241 (= F278), S242 (≠ A279)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 84% coverage: 77:488/493 of query aligns to 45:415/415 of 1k0gB
- active site: E258 (= E295), K274 (≠ A311), E277 (= E339), S330 (≠ T403), W354 (≠ Y427), R374 (= R447), G390 (= G463), E403 (= E476), K407 (= K480)
- binding phosphate ion: Y112 (= Y146), D113 (≠ E147), R116 (vs. gap), D344 (≠ A417), R350 (≠ P423)
- binding tryptophan: R45 (= R77), F46 (= F78), P240 (= P277), F241 (= F278)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
32% identity, 71% coverage: 138:488/493 of query aligns to 146:509/519 of P00897
- PYM 290:292 (≠ PFA 277:279) binding L-tryptophan
- E360 (= E339) binding Mg(2+)
- E497 (= E476) binding Mg(2+)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
38% identity, 39% coverage: 288:480/493 of query aligns to 223:414/424 of 5jy9B
- active site: E230 (= E295), A246 (= A311), E274 (= E339), H311 (= H376), T338 (= T403), Y362 (= Y427), R381 (= R447), G397 (= G463), E410 (= E476), K414 (= K480)
- binding fe (ii) ion: E274 (= E339), E410 (= E476)
Sites not aligning to the query:
Query Sequence
>WP_245546805.1 NCBI__GCF_000384235.1:WP_245546805.1
MTPHLPDAMPAPQWVAQPVPVWVSELPDVRDLNLLALCERWPERYPFLLESVASGQKQPG
VGLDGQPVGTTAESLGRFDILMAFPQTSDACLTPEAGQDFVRGFEQSLVENGLTPSDSAL
ADDTGVAETKTLSLPFTGGWFVYFGYEFAQVLEPSLSLPASNLPLAKWVRIPSAILIDHQ
TGHGYLVAEPGFEHRLHTLYQDLQQVGRVETSVPEIAVAEIHQDPPQRFTQGVDRIKDYI
LAGDVFQVNLSRQWEVDVKNASAPNVYRALRQANPAPFAAYADFGDWQVLSSSPERLVTS
DGEHVATRPIAGTRRRSSDTEKDLALIRELQAHPKEVAEHIMLIDLERNDLGRLSQPGSV
AVDELMAIETYQYVHHIVSNIQGRLQPGTSPLDIFAATFPGGTITGCPKIRCMEIIAELE
QTPREAYTGSLGYINRDGRLDSNILIRTFVQQGERLRFRAGAGIVADSDPEKELAETRHK
AKGLLKALRREMR
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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