SitesBLAST
Comparing WP_002719157.1 NCBI__GCF_000015985.1:WP_002719157.1 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)
46% identity, 92% coverage: 22:486/503 of query aligns to 44:511/524 of A0QX93
- K355 (≠ A330) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
45% identity, 92% coverage: 22:486/503 of query aligns to 24:486/499 of 7bvdA
- active site: Q248 (= Q250), E301 (= E297), A317 (= A313), E341 (= E341), H378 (= H378), T405 (= T405), Y429 (= Y429), R449 (= R449), G465 (= G465), E478 (= E478), K482 (= K482)
- binding pyruvic acid: S93 (≠ L96), G94 (≠ E97), A100 (≠ T103)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
45% identity, 92% coverage: 22:486/503 of query aligns to 24:490/505 of 5cwaA
- active site: Q248 (= Q250), E301 (= E297), A317 (= A313), E345 (= E341), H382 (= H378), T409 (= T405), Y433 (= Y429), R453 (= R449), G469 (= G465), E482 (= E478), K486 (= K482)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y429), I452 (≠ L448), A466 (≠ S462), G467 (= G463), K486 (= K482)
7pi1DDD Aminodeoxychorismate synthase component 1
39% identity, 92% coverage: 31:491/503 of query aligns to 14:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G465), E438 (= E475)
- binding tryptophan: L33 (= L50), E34 (= E51), S35 (= S52), G39 (= G56), Y41 (= Y62), P242 (= P279), Y243 (≠ F280), M244 (= M281), Q406 (≠ D443), N408 (≠ C445)
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)
39% identity, 92% coverage: 31:491/503 of query aligns to 16:461/470 of P28820
- A283 (= A313) 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.
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, 96% coverage: 11:493/503 of query aligns to 12:477/489 of O94582
- S390 (= S407) modified: Phosphoserine
- S392 (≠ A409) 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)
37% identity, 97% coverage: 2:491/503 of query aligns to 62:586/595 of P32068
- D341 (≠ P264) 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)
38% identity, 96% coverage: 10:491/503 of query aligns to 53:568/577 of Q94GF1
- D323 (≠ P264) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
40% identity, 72% coverage: 128:489/503 of query aligns to 144:505/512 of 1i1qA
- active site: Q259 (= Q250), E305 (= E297), A323 (= A313), E357 (= E341), H394 (= H378), T421 (= T405), Y445 (= Y429), R465 (= R449), G481 (= G465), E494 (= E478), K498 (= K482)
- binding tryptophan: P287 (= P279), Y288 (≠ F280), M289 (= M281), G450 (= G434), C461 (= C445)
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)
41% identity, 72% coverage: 128:489/503 of query aligns to 148:509/520 of P00898
- C174 (≠ V155) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N276) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P277) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M281) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F282) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G293) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N382) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G440) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C445) 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.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
38% identity, 77% coverage: 101:489/503 of query aligns to 115:500/511 of 1i7sA
- active site: Q254 (= Q250), E300 (= E297), A318 (= A313), E352 (= E341), H389 (= H378), T416 (= T405), Y440 (= Y429), R460 (= R449), G476 (= G465), E489 (= E478), K493 (= K482)
- binding tryptophan: P282 (= P279), Y283 (≠ F280), M284 (= M281), V444 (= V433), G445 (= G434), D454 (= D443), C456 (= C445)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
38% identity, 77% coverage: 101:489/503 of query aligns to 121:506/517 of 1i7qA
- active site: Q260 (= Q250), E306 (= E297), A324 (= A313), E358 (= E341), H395 (= H378), T422 (= T405), Y446 (= Y429), R466 (= R449), G482 (= G465), E495 (= E478), K499 (= K482)
- binding magnesium ion: E358 (= E341), E495 (= E478)
- binding pyruvic acid: Y446 (= Y429), I465 (≠ L448), R466 (= R449), A479 (≠ S462), G480 (= G463), K499 (= K482)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
38% identity, 77% coverage: 101:489/503 of query aligns to 123:508/519 of P00897
- PYM 290:292 (≠ PFM 279:281) binding L-tryptophan
- E360 (= E341) binding Mg(2+)
- E497 (= E478) binding Mg(2+)
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)
33% identity, 78% coverage: 100:491/503 of query aligns to 79:452/453 of P05041
- E258 (= E297) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A313) 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 (= G314) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R350) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R355) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T361) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H378) 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)
32% identity, 78% coverage: 100:491/503 of query aligns to 77:436/437 of 1k0eA
- active site: E256 (= E297), K272 (≠ A313), E286 (= E341), H323 (= H378), S350 (≠ T405), W374 (≠ Y429), R394 (= R449), G410 (= G465), E423 (= E478), K427 (= K482)
- binding tryptophan: P238 (= P279), F239 (= F280), S240 (≠ M281)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 78% coverage: 100:491/503 of query aligns to 79:419/420 of 1k0gA
- active site: E258 (= E297), K274 (= K337), E278 (= E341), S333 (≠ T405), W357 (≠ Y429), R377 (= R449), G393 (= G465), E406 (= E478), K410 (= K482)
- binding phosphate ion: D113 (= D133), R116 (= R136), D347 (= D419), R353 (≠ K425)
- binding tryptophan: P240 (= P279), F241 (= F280), S242 (≠ M281)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
34% identity, 75% coverage: 112:486/503 of query aligns to 252:627/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I312), K454 (≠ A313), G455 (= G314), T456 (= T315), M547 (≠ V406), Y570 (= Y429), R590 (= R449), V603 (≠ S462), G604 (= G463), G605 (= G464), A606 (≠ G465), E619 (= E478), K623 (= K482)
- binding tryptophan: P419 (= P279), Y420 (≠ F280), G421 (≠ M281), L574 (≠ V433), G575 (= G434)
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, 75% coverage: 112:486/503 of query aligns to 294:666/673 of 8hx8A
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 76% coverage: 100:482/503 of query aligns to 79:407/415 of 1k0gB
- active site: E258 (= E297), K274 (≠ A313), E277 (= E341), S330 (≠ T405), W354 (≠ Y429), R374 (= R449), G390 (= G465), E403 (= E478), K407 (= K482)
- binding phosphate ion: Y112 (= Y132), D113 (= D133), R116 (= R136), D344 (= D419), R350 (≠ K425)
- binding tryptophan: P240 (= P279), F241 (= F280)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
32% identity, 50% coverage: 230:482/503 of query aligns to 163:414/424 of 5jy9B
- active site: K183 (≠ Q250), E230 (= E297), A246 (= A313), E274 (= E341), H311 (= H378), T338 (= T405), Y362 (= Y429), R381 (= R449), G397 (= G465), E410 (= E478), K414 (= K482)
- binding fe (ii) ion: E274 (= E341), E410 (= E478)
Query Sequence
>WP_002719157.1 NCBI__GCF_000015985.1:WP_002719157.1
MSLVTSFESFERGWKAGQNQIVYARLTADLDTPVSLMLKLAEARTDTFMLESVTGGEIRG
RYSVVGMKPDLIWQCHGQDSRINREARFDRQAFQPLEGHPLETLRALIAESRIEMPADLP
PIAAGLFGYLGYDMIRLVEHLPGINPDPLGLPDAVLMRPSVVAVLDGVKGEVTVVAPAWV
SSGLSARAAYAQAAERVMDALRDLDRAPPAQRDFGEVAQVGEMRSNFTHEGYKAAVEKAK
DYIRAGDIFQVVPSQRWAQDFRLPPFALYRSLRKTNPSPFMFFFNFGGFQVVGASPEILV
RLRDREVTVRPIAGTRKRGATPEEDRALEADLLSDKKELAEHLMLLDLGRNDVGRVAKIG
TVRPTEKFIIERYSHVMHIVSNVVGEIAEGEDALSALLAGLPAGTVSGAPKVRAMEIIDE
LEPEKRGVYGGGVGYFAANGEMDFCIALRTAVLKDETLYIQSGGGVVYDSDPEAEYQETV
NKARALRRAAEDAGLFARRAGNG
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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