SitesBLAST
Comparing Ga0059261_0256 FitnessBrowser__Korea:Ga0059261_0256 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)
43% identity, 94% coverage: 16:491/508 of query aligns to 33:512/524 of A0QX93
- K355 (≠ T334) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
44% identity, 93% coverage: 20:491/508 of query aligns to 17:491/505 of 5cwaA
- active site: Q248 (= Q254), E301 (= E301), A317 (= A317), E345 (= E345), H382 (= H382), T409 (= T409), Y433 (= Y433), R453 (= R453), G469 (= G469), E482 (= E482), K486 (= K486)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y433), I452 (≠ L452), A466 (= A466), G467 (= G467), K486 (= K486)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 94% coverage: 16:490/508 of query aligns to 54:563/577 of Q94GF1
- D323 (≠ P268) mutation to N: Insensitive to feedback inhibition by tryptophan.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 94% coverage: 16:491/508 of query aligns to 13:487/499 of 7bvdA
- active site: Q248 (= Q254), E301 (= E301), A317 (= A317), E341 (= E345), H378 (= H382), T405 (= T409), Y429 (= Y433), R449 (= R453), G465 (= G469), E478 (= E482), K482 (= K486)
- binding pyruvic acid: S93 (≠ A101), G94 (≠ A102), A100 (= A108)
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, 92% coverage: 33:497/508 of query aligns to 30:477/489 of O94582
- S390 (= S411) modified: Phosphoserine
- S392 (≠ A413) 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)
36% identity, 93% coverage: 19:490/508 of query aligns to 1:456/470 of P28820
- A283 (= A317) 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)
37% identity, 91% coverage: 27:490/508 of query aligns to 82:581/595 of P32068
- D341 (≠ P268) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
7pi1DDD Aminodeoxychorismate synthase component 1
37% identity, 90% coverage: 36:490/508 of query aligns to 14:449/459 of 7pi1DDD
- binding magnesium ion: G428 (= G469), E438 (= E479)
- binding tryptophan: L33 (= L55), E34 (= E56), S35 (= S57), G39 (= G61), Y41 (≠ H67), P242 (= P283), Y243 (≠ F284), M244 (≠ L285), Q406 (≠ D447), N408 (≠ C449)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
39% identity, 71% coverage: 133:493/508 of query aligns to 148:509/520 of P00898
- C174 (≠ I160) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N280) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P281) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L285) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y286) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G297) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N386) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G444) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C449) 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)
39% identity, 71% coverage: 133:493/508 of query aligns to 144:505/512 of 1i1qA
- active site: Q259 (= Q254), E305 (= E301), A323 (= A317), E357 (= E345), H394 (= H382), T421 (= T409), Y445 (= Y433), R465 (= R453), G481 (= G469), E494 (= E482), K498 (= K486)
- binding tryptophan: P287 (= P283), Y288 (≠ F284), M289 (≠ L285), G450 (= G438), C461 (= C449)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
39% identity, 76% coverage: 106:493/508 of query aligns to 123:508/519 of P00897
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
39% identity, 76% coverage: 106:493/508 of query aligns to 121:506/517 of 1i7qA
- active site: Q260 (= Q254), E306 (= E301), A324 (= A317), E358 (= E345), H395 (= H382), T422 (= T409), Y446 (= Y433), R466 (= R453), G482 (= G469), E495 (= E482), K499 (= K486)
- binding magnesium ion: E358 (= E345), E495 (= E482)
- binding pyruvic acid: Y446 (= Y433), I465 (≠ L452), R466 (= R453), A479 (= A466), G480 (= G467), K499 (= K486)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
39% identity, 76% coverage: 106:493/508 of query aligns to 115:500/511 of 1i7sA
- active site: Q254 (= Q254), E300 (= E301), A318 (= A317), E352 (= E345), H389 (= H382), T416 (= T409), Y440 (= Y433), R460 (= R453), G476 (= G469), E489 (= E482), K493 (= K486)
- binding tryptophan: P282 (= P283), Y283 (≠ F284), M284 (≠ L285), V444 (= V437), G445 (= G438), D454 (= D447), C456 (= C449)
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)
35% identity, 71% coverage: 132:491/508 of query aligns to 107:448/453 of P05041
- E258 (= E301) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A317) 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 (= G318) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R354) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R359) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T365) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H382) 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)
34% identity, 71% coverage: 132:491/508 of query aligns to 105:432/437 of 1k0eA
- active site: E256 (= E301), K272 (≠ A317), E286 (= E345), H323 (= H382), S350 (≠ T409), W374 (≠ Y433), R394 (= R453), G410 (= G469), E423 (= E482), K427 (= K486)
- binding tryptophan: P238 (= P283), F239 (= F284), S240 (≠ L285)
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, 77% coverage: 103:493/508 of query aligns to 280:669/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
34% identity, 77% coverage: 103:493/508 of query aligns to 238:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I316), K454 (≠ A317), G455 (= G318), T456 (= T319), M547 (≠ V410), Y570 (= Y433), R590 (= R453), V603 (≠ A466), G604 (= G467), G605 (≠ A468), A606 (≠ G469), E619 (= E482), K623 (= K486)
- binding tryptophan: P419 (= P283), Y420 (≠ F284), G421 (≠ L285), L574 (≠ V437), G575 (= G438)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
32% identity, 71% coverage: 132:491/508 of query aligns to 107:415/420 of 1k0gA
- active site: E258 (= E301), K274 (= K341), E278 (= E345), S333 (≠ T409), W357 (≠ Y433), R377 (= R453), G393 (= G469), E406 (= E482), K410 (= K486)
- binding phosphate ion: D113 (≠ E138), R116 (≠ G141), D347 (≠ A423), R353 (≠ Q429)
- binding tryptophan: P240 (= P283), F241 (= F284), S242 (≠ L285)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 71% coverage: 132:491/508 of query aligns to 107:412/415 of 1k0gB
- active site: E258 (= E301), K274 (≠ A317), E277 (= E345), S330 (≠ T409), W354 (≠ Y433), R374 (= R453), G390 (= G469), E403 (= E482), K407 (= K486)
- binding phosphate ion: Y112 (= Y137), D113 (≠ E138), R116 (≠ G141), D344 (≠ A423), R350 (≠ Q429)
- binding tryptophan: P240 (= P283), F241 (= F284)
Sites not aligning to the query:
3vehB Structure of a m. Tuberculosis salicylate synthase, mbti, in complex with an inhibitor methylamt (see paper)
37% identity, 46% coverage: 240:471/508 of query aligns to 193:425/451 of 3vehB
- active site: K207 (≠ Q254), E254 (= E301), A271 (= A317), E299 (= E345), H336 (= H382), T363 (= T409), Y387 (= Y433), R407 (= R453), G423 (= G469)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: L270 (≠ I316), T273 (= T319), H336 (= H382), T363 (= T409), Y387 (= Y433), L406 (= L452), A420 (= A466), G421 (= G467)
Sites not aligning to the query:
Query Sequence
>Ga0059261_0256 FitnessBrowser__Korea:Ga0059261_0256
MTTGVEGGVEGLDAARAALAQGRPALVWRRQLADTDTPVSAALKLIEPGRGDFLLESVEG
GAVRGRHSLIGLAPDLVFRAHGQQAEINPFWLTDRDAFAPAAQPTLEALRTLVQSCRMDV
PAELPRALACLVGYFGYETIGLVETLPRADEDALGLPDMIFVRPTVILIFDRLADSLFLV
APVWPGSTRDPEARLADAAERIDATAARLATAPLPPKVAGDALEIAARPTLADGDYAAMV
ARAKEYITAGDIFQVVLAQRFTAPFALPPIELYRALRRVNPSPFLYFLDLPGFALTGSSP
EILVRVRDDEVTIRPIAGTRPRGKTAAEDEANRTSLLADPKERAEHLMLLDLGRNDTGRV
AQAGTVRVTDSYTVEFYSHVMHIVSNVVGKLRPDADALDALFAGFPAGTVSGAPKVRACE
IIAELEREQRGPYAGGVGYFSPDGSMDSCIVLRTAIVKDGTMHVTAGAGIVADSDAAYEQ
RECEAKAGALFAAAREAVARASEPGFGQ
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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