SitesBLAST
Comparing WP_013010466.1 NCBI__GCF_000025725.1:WP_013010466.1 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)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
36% identity, 95% coverage: 10:477/493 of query aligns to 8:492/505 of 5cwaA
- active site: Q248 (= Q242), E301 (= E289), A317 (= A305), E345 (= E330), H382 (= H367), T409 (= T394), Y433 (= Y418), R453 (= R438), G469 (= G454), E482 (= E467), K486 (= K471)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y418), I452 (= I437), A466 (≠ S451), G467 (= G452), K486 (= K471)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
35% identity, 95% coverage: 10:477/493 of query aligns to 8:488/499 of 7bvdA
- active site: Q248 (= Q242), E301 (= E289), A317 (= A305), E341 (= E330), H378 (= H367), T405 (= T394), Y429 (= Y418), R449 (= R438), G465 (= G454), E478 (= E467), K482 (= K471)
- binding pyruvic acid: S93 (≠ F94), G94 (≠ S95), A100 (≠ Y101)
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)
35% identity, 95% coverage: 10:477/493 of query aligns to 28:513/524 of A0QX93
- K355 (= K318) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
35% identity, 96% coverage: 6:478/493 of query aligns to 2:473/489 of O94582
- S390 (= S396) modified: Phosphoserine
- S392 (≠ A398) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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, 87% coverage: 52:478/493 of query aligns to 34:459/470 of P28820
- A283 (= A305) 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.
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)
31% identity, 92% coverage: 24:478/493 of query aligns to 80:584/595 of P32068
- D341 (≠ N256) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7pi1DDD Aminodeoxychorismate synthase component 1
32% identity, 87% coverage: 52:478/493 of query aligns to 32:452/459 of 7pi1DDD
- binding magnesium ion: G428 (= G454), E438 (= E464)
- binding tryptophan: L33 (= L53), E34 (= E54), S35 (= S55), G39 (≠ S63), Y41 (≠ F65), P242 (= P271), Y243 (= Y272), M244 (= M273), Q406 (≠ D432), N408 (≠ C434)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 91% coverage: 28:478/493 of query aligns to 68:566/577 of Q94GF1
- D323 (≠ N256) mutation to N: Insensitive to feedback inhibition by tryptophan.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
36% identity, 72% coverage: 124:478/493 of query aligns to 143:506/517 of 1i7qA
- active site: Q260 (= Q242), E306 (= E289), A324 (= A305), E358 (= E330), H395 (= H367), T422 (= T394), Y446 (= Y418), R466 (= R438), G482 (= G454), E495 (= E467), K499 (= K471)
- binding magnesium ion: E358 (= E330), E495 (= E467)
- binding pyruvic acid: Y446 (= Y418), I465 (= I437), R466 (= R438), A479 (≠ S451), G480 (= G452), K499 (= K471)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
36% identity, 72% coverage: 124:478/493 of query aligns to 137:500/511 of 1i7sA
- active site: Q254 (= Q242), E300 (= E289), A318 (= A305), E352 (= E330), H389 (= H367), T416 (= T394), Y440 (= Y418), R460 (= R438), G476 (= G454), E489 (= E467), K493 (= K471)
- binding tryptophan: P282 (= P271), Y283 (= Y272), M284 (= M273), V444 (= V422), G445 (= G423), D454 (= D432), C456 (= C434)
Sites not aligning to the query:
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
41% identity, 55% coverage: 210:478/493 of query aligns to 229:505/512 of 1i1qA
- active site: Q259 (= Q242), E305 (= E289), A323 (= A305), E357 (= E330), H394 (= H367), T421 (= T394), Y445 (= Y418), R465 (= R438), G481 (= G454), E494 (= E467), K498 (= K471)
- binding tryptophan: P287 (= P271), Y288 (= Y272), M289 (= M273), G450 (= G423), C461 (= C434)
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, 55% coverage: 210:478/493 of query aligns to 233:509/520 of P00898
- N288 (= N268) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P269) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M273) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F274) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G285) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ E371) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G429) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C434) 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.
- 174 C→Y: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
35% identity, 72% coverage: 124:478/493 of query aligns to 145:508/519 of P00897
- PYM 290:292 (= PYM 271:273) binding L-tryptophan
- E360 (= E330) binding Mg(2+)
- E497 (= E467) binding Mg(2+)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
29% identity, 88% coverage: 44:478/493 of query aligns to 180:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I304), K454 (≠ A305), G455 (= G306), T456 (= T307), M547 (≠ V395), Y570 (= Y418), R590 (= R438), V603 (≠ S451), G604 (= G452), G605 (= G453), A606 (≠ G454), E619 (= E467), K623 (= K471)
- binding tryptophan: L189 (= L53), D190 (≠ E54), S191 (= S55), S199 (= S63), F201 (= F65), P419 (= P271), Y420 (= Y272), G421 (≠ M273), L574 (≠ V422), G575 (= G423)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
29% identity, 88% coverage: 44:478/493 of query aligns to 222:669/673 of 8hx8A
- binding magnesium ion: E521 (= E330), E655 (= E464), E658 (= E467)
- binding tryptophan: L231 (= L53), D232 (≠ E54), S233 (= S55), S241 (= S63), F243 (= F65), P458 (= P271), Y459 (= Y272), G460 (≠ M273), G614 (= G423)
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)
28% identity, 86% coverage: 51:476/493 of query aligns to 32:448/453 of P05041
- S36 (= S55) binding L-tryptophan
- E258 (= E289) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A305) 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 (= G306) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R339) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ T344) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S350) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H367) 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)
27% identity, 86% coverage: 51:476/493 of query aligns to 30:432/437 of 1k0eA
- active site: E256 (= E289), K272 (≠ A305), E286 (= E330), H323 (= H367), S350 (≠ T394), W374 (≠ Y418), R394 (= R438), G410 (= G454), E423 (= E467), K427 (= K471)
- binding tryptophan: L32 (= L53), H33 (≠ E54), S34 (= S55), Y41 (≠ F62), F44 (= F65), P238 (= P271), F239 (≠ Y272), S240 (≠ M273)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
25% identity, 86% coverage: 51:476/493 of query aligns to 32:415/420 of 1k0gA
- active site: E258 (= E289), K274 (= K326), E278 (= E330), S333 (≠ T394), W357 (≠ Y418), R377 (= R438), G393 (= G454), E406 (= E467), K410 (= K471)
- binding phosphate ion: D113 (≠ E131), R116 (≠ N134), D347 (≠ E408), R353 (≠ E414)
- binding tryptophan: L34 (= L53), H35 (≠ E54), S36 (= S55), Y43 (≠ F62), S44 (= S63), F46 (= F65), P240 (= P271), F241 (≠ Y272), S242 (≠ M273)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
25% identity, 86% coverage: 51:476/493 of query aligns to 32:412/415 of 1k0gB
- active site: E258 (= E289), K274 (≠ A305), E277 (= E330), S330 (≠ T394), W354 (≠ Y418), R374 (= R438), G390 (= G454), E403 (= E467), K407 (= K471)
- binding phosphate ion: Y112 (= Y130), D113 (≠ E131), R116 (≠ N134), D344 (≠ E408), R350 (≠ E414)
- binding tryptophan: L34 (= L53), H35 (≠ E54), S36 (= S55), Y43 (≠ F62), S44 (= S63), R45 (= R64), F46 (= F65), P240 (= P271), F241 (≠ Y272)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
28% identity, 54% coverage: 209:475/493 of query aligns to 134:402/408 of 2fn1A
- active site: K167 (≠ Q242), E214 (= E289), A230 (= A305), E258 (= E330), H295 (= H367), T322 (= T394), Y346 (= Y418), R365 (= R438), G381 (= G454), E394 (= E467), K398 (= K471)
- binding magnesium ion: E258 (= E330), E394 (= E467)
- binding pyruvic acid: Y346 (= Y418), L364 (≠ I437), R365 (= R438), A378 (≠ S451), G379 (= G452), K398 (= K471)
Query Sequence
>WP_013010466.1 NCBI__GCF_000025725.1:WP_013010466.1
MNLTEQIHPSRERFTELAGEFDRVTVYREIIGDTFTPITLLRNFSNEENIFLLESANLDK
TFSRFSFFGNKPKRVITFQNGQVTVKKGSKKETFSMNPMDYMSQQLYAEKGYNDGTFGDF
SGGFAGFFAYEAVNYMDTLRKPLKVSPESKLIGFMEVDEFYVFDNHFSKMYAAVSVQTKG
GESAYDKALKRTQKMSSEVHRFNFDNYDSDLDCELVTDMTEEEYMATVDALKEEITNGEG
IQIVPSNAHRLKGKINPLSLYRALRNVNPSPYMFYLKFGSEVLLGASPEIHLKIREGYAT
LKPIAGTYPITDDIEASKQALLSDPKERSEHLMLLDLARNDLYTCCEPESVKVKEQFVPE
VYSHVIHIVSEVEGKIENGYNPLNLFMKSFPAGTVSGAPKVRAMELIEQYEKSERGFYAG
CVGYFGYSGNMDTCITIRSAYVTETETVFRSGGGVIYDSDPQTEYKETKNKLGALFSAYK
NIGVTEGRDVSNG
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