SitesBLAST
Comparing Ac3H11_767 FitnessBrowser__acidovorax_3H11:Ac3H11_767 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)
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)
40% identity, 96% coverage: 17:496/499 of query aligns to 10:465/470 of P28820
- A283 (= A314) 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.
7pi1DDD Aminodeoxychorismate synthase component 1
40% identity, 96% coverage: 17:496/499 of query aligns to 8:458/459 of 7pi1DDD
- binding magnesium ion: G428 (= G466), E438 (= E476)
- binding tryptophan: L33 (= L51), E34 (= E52), S35 (= S53), G39 (= G57), Y41 (= Y63), P242 (= P276), Y243 (= Y277), M244 (= M278), Q406 (≠ D444), N408 (≠ A446)
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, 97% coverage: 6:488/499 of query aligns to 31:512/524 of A0QX93
- K355 (≠ V331) 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)
43% identity, 97% coverage: 6:488/499 of query aligns to 11:491/505 of 5cwaA
- active site: Q248 (= Q247), E301 (= E294), A317 (= A314), E345 (= E342), H382 (= H379), T409 (= T406), Y433 (= Y430), R453 (= R450), G469 (= G466), E482 (= E479), K486 (= K483)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y430), I452 (= I449), A466 (= A463), G467 (≠ A464), K486 (= K483)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
40% identity, 99% coverage: 4:495/499 of query aligns to 50:571/577 of Q94GF1
- D323 (≠ S261) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
40% identity, 96% coverage: 16:496/499 of query aligns to 20:479/489 of O94582
- S390 (≠ T408) modified: Phosphoserine
- S392 (≠ A410) 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)
39% identity, 98% coverage: 11:498/499 of query aligns to 73:592/595 of P32068
- D341 (≠ S261) 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]
43% identity, 97% coverage: 6:488/499 of query aligns to 11:487/499 of 7bvdA
- active site: Q248 (= Q247), E301 (= E294), A317 (= A314), E341 (= E342), H378 (= H379), T405 (= T406), Y429 (= Y430), R449 (= R450), G465 (= G466), E478 (= E479), K482 (= K483)
- binding pyruvic acid: S93 (≠ A97), G94 (≠ Q98), A100 (≠ F104)
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
39% identity, 74% coverage: 123:490/499 of query aligns to 141:505/512 of 1i1qA
- active site: Q259 (= Q247), E305 (= E294), A323 (= A314), E357 (= E342), H394 (= H379), T421 (= T406), Y445 (= Y430), R465 (= R450), G481 (= G466), E494 (= E479), K498 (= K483)
- binding tryptophan: P287 (= P276), Y288 (= Y277), M289 (= M278), G450 (= G435), C461 (≠ A446)
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)
39% identity, 74% coverage: 123:490/499 of query aligns to 145:509/520 of P00898
- C174 (≠ L158) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N273) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P274) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M278) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y279) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G290) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N383) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G441) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A446) 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.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
38% identity, 73% coverage: 127:490/499 of query aligns to 137:500/511 of 1i7sA
- active site: Q254 (= Q247), E300 (= E294), A318 (= A314), E352 (= E342), H389 (= H379), T416 (= T406), Y440 (= Y430), R460 (= R450), G476 (= G466), E489 (= E479), K493 (= K483)
- binding tryptophan: P282 (= P276), Y283 (= Y277), M284 (= M278), V444 (≠ C434), G445 (= G435), D454 (= D444), C456 (≠ A446)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
38% identity, 73% coverage: 127:490/499 of query aligns to 143:506/517 of 1i7qA
- active site: Q260 (= Q247), E306 (= E294), A324 (= A314), E358 (= E342), H395 (= H379), T422 (= T406), Y446 (= Y430), R466 (= R450), G482 (= G466), E495 (= E479), K499 (= K483)
- binding magnesium ion: E358 (= E342), E495 (= E479)
- binding pyruvic acid: Y446 (= Y430), I465 (= I449), R466 (= R450), A479 (= A463), G480 (≠ A464), K499 (= K483)
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)
31% identity, 89% coverage: 48:492/499 of query aligns to 31:452/453 of P05041
- S36 (= S53) binding
- E258 (= E294) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A314) 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 (= G315) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R351) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R356) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T362) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H379) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
38% identity, 73% coverage: 127:490/499 of query aligns to 145:508/519 of P00897
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
31% identity, 89% coverage: 48:492/499 of query aligns to 29:436/437 of 1k0eA
- active site: E256 (= E294), K272 (≠ A314), E286 (= E342), H323 (= H379), S350 (≠ T406), W374 (≠ Y430), R394 (= R450), G410 (= G466), E423 (= E479), K427 (= K483)
- binding tryptophan: L32 (= L51), H33 (≠ E52), S34 (= S53), Y41 (≠ F60), F44 (≠ Y63), P238 (= P276), F239 (≠ Y277), S240 (≠ M278)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
32% identity, 89% coverage: 48:490/499 of query aligns to 228:669/673 of 8hx8A
- binding magnesium ion: E521 (= E342), E655 (= E476), E658 (= E479)
- binding tryptophan: L231 (= L51), D232 (≠ E52), S233 (= S53), S241 (≠ G61), F243 (≠ Y63), P458 (= P276), Y459 (= Y277), G460 (≠ M278), G614 (= G435)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 89% coverage: 48:490/499 of query aligns to 186:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (≠ L313), K454 (≠ A314), G455 (= G315), T456 (= T316), M547 (≠ L407), Y570 (= Y430), R590 (= R450), V603 (≠ A463), G604 (≠ A464), G605 (≠ A465), A606 (≠ G466), E619 (= E479), K623 (= K483)
- binding tryptophan: L189 (= L51), D190 (≠ E52), S191 (= S53), S199 (≠ G61), F201 (≠ Y63), P419 (= P276), Y420 (= Y277), G421 (≠ M278), L574 (≠ C434), G575 (= G435)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
29% identity, 89% coverage: 48:492/499 of query aligns to 31:419/420 of 1k0gA
- active site: E258 (= E294), K274 (= K338), E278 (= E342), S333 (≠ T406), W357 (≠ Y430), R377 (= R450), G393 (= G466), E406 (= E479), K410 (= K483)
- binding phosphate ion: D113 (= D134), R116 (= R137), D347 (= D420), R353 (≠ K426)
- binding tryptophan: L34 (= L51), H35 (≠ E52), S36 (= S53), Y43 (≠ F60), S44 (≠ G61), F46 (≠ Y63), P240 (= P276), F241 (≠ Y277), S242 (≠ M278)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
28% identity, 89% coverage: 48:489/499 of query aligns to 31:413/415 of 1k0gB
- active site: E258 (= E294), K274 (≠ A314), E277 (= E342), S330 (≠ T406), W354 (≠ Y430), R374 (= R450), G390 (= G466), E403 (= E479), K407 (= K483)
- binding phosphate ion: Y112 (= Y133), D113 (= D134), R116 (= R137), D344 (= D420), R350 (≠ K426)
- binding tryptophan: L34 (= L51), H35 (≠ E52), S36 (= S53), Y43 (≠ F60), S44 (≠ G61), R45 (= R62), F46 (≠ Y63), P240 (= P276), F241 (≠ Y277)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
33% identity, 51% coverage: 229:483/499 of query aligns to 165:414/424 of 5jy9B
- active site: K183 (≠ Q247), E230 (= E294), A246 (= A314), E274 (= E342), H311 (= H379), T338 (= T406), Y362 (= Y430), R381 (= R450), G397 (= G466), E410 (= E479), K414 (= K483)
- binding fe (ii) ion: E274 (= E342), E410 (= E479)
Query Sequence
>Ac3H11_767 FitnessBrowser__acidovorax_3H11:Ac3H11_767
VITELEFKSLASEGYNRIPLMAEAFADLETPLSLYLKLAHTKDGGKHSFLLESVVGGERF
GRYSFIGLPARTLLRASGFGADARTEVVTDGQVVETAQGNPLDFIADYQKRFKVALRPGL
PRFCGGLAGYFGYDAVRYIEKKLETTCPPDTLGCPDILLLQCEELAVIDNLSGKLYLIVY
ADPAQPEAYTRAKKRLRELKEQLKYSVSAPVVKATESHPAQRDFAKADYLAAVHRAKELI
AAGDFMQVQVGQRIHKRYTESPLSLYRALRSLNPSPYMYFYDFGDFHVVGASPEILVRQE
KTEEGTKVTIRPLAGTRPRGATPEKDKATEVELINDPKERAEHVMLIDLARNDIGRIAKT
GTVKVTEAFAVERYSHVMHIVSNVEGILNDGMTSMDVLKATFPAGTLTGAPKVHAMELID
QLEPTKRGLYGGACGYLSYAGDMDVAIAIRTGIIKNGTLYVQAAAGVVADSVPELEWKET
EHKARALLRAAELVEEGLE
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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