SitesBLAST
Comparing WP_017597549.1 NCBI__GCF_000341125.1:WP_017597549.1 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)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
54% identity, 94% coverage: 20:440/447 of query aligns to 229:663/673 of 8hx8A
- binding magnesium ion: E521 (= E298), E655 (= E432), E658 (= E435)
- binding tryptophan: L231 (= L22), D232 (= D23), S233 (= S24), S241 (≠ A31), F243 (= F33), P458 (= P235), Y459 (= Y236), G460 (≠ A237), G614 (= G391)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
53% identity, 94% coverage: 20:440/447 of query aligns to 187:624/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I269), K454 (= K270), G455 (= G271), T456 (= T272), M547 (= M363), Y570 (= Y386), R590 (= R406), V603 (≠ A419), G604 (= G420), G605 (= G421), A606 (= A422), E619 (= E435), K623 (= K439)
- binding tryptophan: L189 (= L22), D190 (= D23), S191 (= S24), S199 (≠ A31), F201 (= F33), P419 (= P235), Y420 (= Y236), G421 (≠ A237), L574 (= L390), G575 (= G391)
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)
39% identity, 83% coverage: 71:440/447 of query aligns to 85:444/453 of P05041
- E258 (= E253) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K270) 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 (= G271) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R307) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R312) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S318) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (≠ Q335) 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)
38% identity, 83% coverage: 71:440/447 of query aligns to 83:428/437 of 1k0eA
- active site: E256 (= E253), K272 (= K270), E286 (= E298), H323 (≠ Q335), S350 (= S362), W374 (≠ Y386), R394 (= R406), G410 (≠ A422), E423 (= E435), K427 (= K439)
- binding tryptophan: P238 (= P235), F239 (≠ Y236), S240 (≠ A237)
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)
32% identity, 97% coverage: 7:439/447 of query aligns to 37:466/489 of O94582
- S390 (≠ T364) modified: Phosphoserine
- S392 (≠ A366) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
7pi1DDD Aminodeoxychorismate synthase component 1
32% identity, 84% coverage: 70:445/447 of query aligns to 82:451/459 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)
32% identity, 84% coverage: 70:445/447 of query aligns to 84:458/470 of P28820
- A283 (≠ K270) 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)
43% identity, 58% coverage: 180:440/447 of query aligns to 245:508/524 of A0QX93
- K355 (≠ E287) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 94% coverage: 20:440/447 of query aligns to 50:483/499 of 7bvdA
- active site: Q248 (≠ E204), E301 (= E253), A317 (≠ K270), E341 (= E298), H378 (≠ Q335), T405 (≠ S362), Y429 (= Y386), R449 (= R406), G465 (≠ A422), E478 (= E435), K482 (= K439)
- binding pyruvic acid: S93 (≠ E65), G94 (≠ P66), A100 (= A72)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
36% identity, 92% coverage: 31:440/447 of query aligns to 62:487/505 of 5cwaA
- active site: Q248 (≠ E204), E301 (= E253), A317 (≠ K270), E345 (= E298), H382 (≠ Q335), T409 (≠ S362), Y433 (= Y386), R453 (= R406), G469 (≠ A422), E482 (= E435), K486 (= K439)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y386), I452 (= I405), A466 (= A419), G467 (= G420), K486 (= K439)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 93% coverage: 32:445/447 of query aligns to 111:565/577 of Q94GF1
- D323 (= D220) mutation to N: Insensitive to feedback inhibition by tryptophan.
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
36% identity, 83% coverage: 71:440/447 of query aligns to 85:411/420 of 1k0gA
- active site: E258 (= E253), K274 (= K270), E278 (= E298), S333 (= S362), W357 (≠ Y386), R377 (= R406), G393 (≠ A422), E406 (= E435), K410 (= K439)
- binding phosphate ion: D113 (≠ E100), R116 (vs. gap), D347 (= D376), R353 (≠ A382)
- binding tryptophan: P240 (= P235), F241 (≠ Y236), S242 (≠ A237)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
36% identity, 83% coverage: 71:440/447 of query aligns to 85:408/415 of 1k0gB
- active site: E258 (= E253), K274 (= K270), E277 (= E298), S330 (= S362), W354 (≠ Y386), R374 (= R406), G390 (≠ A422), E403 (= E435), K407 (= K439)
- binding phosphate ion: Y112 (= Y99), D113 (≠ E100), R116 (vs. gap), D344 (= D376), R350 (≠ A382)
- binding tryptophan: P240 (= P235), F241 (≠ Y236)
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)
32% identity, 82% coverage: 79:445/447 of query aligns to 179:583/595 of P32068
- D341 (= D220) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
34% identity, 79% coverage: 89:440/447 of query aligns to 145:503/520 of P00898
- C174 (≠ V119) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (≠ S232) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P233) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A237) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A238) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S249) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T339) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G397) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S402) 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
34% identity, 79% coverage: 89:440/447 of query aligns to 141:499/512 of 1i1qA
- active site: Q259 (≠ E204), E305 (= E253), A323 (≠ K270), E357 (= E298), H394 (≠ Q335), T421 (≠ S362), Y445 (= Y386), R465 (= R406), G481 (≠ A422), E494 (= E435), K498 (= K439)
- binding tryptophan: P287 (= P235), Y288 (= Y236), M289 (≠ A237), G450 (= G391), C461 (≠ S402)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
34% identity, 77% coverage: 95:440/447 of query aligns to 145:500/517 of 1i7qA
- active site: Q260 (≠ E204), E306 (= E253), A324 (≠ K270), E358 (= E298), H395 (≠ Q335), T422 (≠ S362), Y446 (= Y386), R466 (= R406), G482 (≠ A422), E495 (= E435), K499 (= K439)
- binding magnesium ion: E358 (= E298), E495 (= E435)
- binding pyruvic acid: Y446 (= Y386), I465 (= I405), R466 (= R406), A479 (= A419), G480 (= G420), K499 (= K439)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
34% identity, 77% coverage: 95:440/447 of query aligns to 139:494/511 of 1i7sA
- active site: Q254 (≠ E204), E300 (= E253), A318 (≠ K270), E352 (= E298), H389 (≠ Q335), T416 (≠ S362), Y440 (= Y386), R460 (= R406), G476 (≠ A422), E489 (= E435), K493 (= K439)
- binding tryptophan: P282 (= P235), Y283 (= Y236), M284 (≠ A237), V444 (≠ L390), G445 (= G391), D454 (= D400), C456 (≠ S402)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
34% identity, 77% coverage: 95:440/447 of query aligns to 147:502/519 of P00897
Sites not aligning to the query:
8qc4A Salicylate synthase (see paper)
31% identity, 53% coverage: 190:424/447 of query aligns to 179:411/438 of 8qc4A
Sites not aligning to the query:
Query Sequence
>WP_017597549.1 NCBI__GCF_000341125.1:WP_017597549.1
HAVDTEAAFAHLYGAAEYAFWLDSSRPEGPARFSFLGAATGEILTYRVGDGEVRVRDVDG
AERREPGTIFDALDRRTRPTAPTGLPFDFTGGHVGYFGYELKADCGADNAHTSPTPDAVW
MRCDRFVAVDHAEGRAYVVHDDSDGARAWAGRTLDALSALPVPPPPAPPGPAVDLGAHLE
RPHGDYVTDVKECLGHLTEGESYEICLTNRVRLPDDTSDDDLDLYRRLRAASPAPYAALL
RLGPVSVLSASPERFLRVDGDRVAESRPIKGTAPRHADPDTDRRAAEELRTGAKTRAENL
MIVDLLRNDLGRVCEVGSVQVPAFMYTESYATVHQLVSTVRGRLRPDVTTLDAVRACFPG
GSMTGAPKLRTMEIIDRLESSARGVYSGALGYLSHAGTADLSIVIRTAVRSGGELTIGAG
GAIVLDSDPEDEYEEMLLKAAVPARVR
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