SitesBLAST
Comparing WP_011841694.1 NCBI__GCF_000015985.1:WP_011841694.1 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)
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)
45% identity, 70% coverage: 104:370/381 of query aligns to 182:445/453 of P05041
- E258 (= E181) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K198) 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 (= G199) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R235) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R240) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S246) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (≠ Q263) 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:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
44% identity, 68% coverage: 111:370/381 of query aligns to 365:625/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (≠ M197), K454 (= K198), G455 (= G199), T456 (= T200), M547 (≠ V291), Y570 (= Y314), R590 (= R334), V603 (= V348), G604 (= G349), G605 (= G350), A606 (≠ G351), E619 (= E364), K623 (= K368)
- binding tryptophan: P419 (≠ G163), Y420 (≠ Q164), G421 (= G165), L574 (≠ M318), G575 (= G319)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
44% identity, 68% coverage: 111:370/381 of query aligns to 404:664/673 of 8hx8A
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
41% identity, 70% coverage: 104:370/381 of query aligns to 180:429/437 of 1k0eA
- active site: E256 (= E181), K272 (= K198), E286 (= E226), H323 (≠ Q263), S350 (= S290), W374 (≠ Y314), R394 (= R334), G410 (= G351), E423 (= E364), K427 (= K368)
- binding tryptophan: P238 (≠ G163), F239 (≠ Q164), S240 (≠ G165)
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)
40% identity, 67% coverage: 115:368/381 of query aligns to 202:452/470 of P28820
- A283 (≠ K198) 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, 67% coverage: 115:368/381 of query aligns to 195:445/459 of 7pi1DDD
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
39% identity, 70% coverage: 104:370/381 of query aligns to 182:412/420 of 1k0gA
- active site: E258 (= E181), K274 (= K198), E278 (= E226), S333 (= S290), W357 (≠ Y314), R377 (= R334), G393 (= G351), E406 (= E364), K410 (= K368)
- binding phosphate ion: D347 (≠ G304), R353 (≠ P310)
- binding tryptophan: P240 (= P161), F241 (≠ V162), S242 (≠ G163)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
39% identity, 70% coverage: 104:370/381 of query aligns to 182:409/415 of 1k0gB
- active site: E258 (= E181), K274 (= K198), E277 (= E226), S330 (= S290), W354 (≠ Y314), R374 (= R334), G390 (= G351), E403 (= E364), K407 (= K368)
- binding phosphate ion: D344 (≠ G304), R350 (≠ P310)
- binding tryptophan: P240 (= P161), F241 (≠ V162)
Sites not aligning to the query:
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)
38% identity, 70% coverage: 106:370/381 of query aligns to 242:509/524 of A0QX93
- K355 (= K215) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
38% identity, 70% coverage: 106:370/381 of query aligns to 221:484/499 of 7bvdA
- active site: Q248 (= Q133), E301 (= E181), A317 (≠ K198), E341 (= E226), H378 (≠ Q263), T405 (≠ S290), Y429 (= Y314), R449 (= R334), G465 (= G351), E478 (= E364), K482 (= K368)
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)
35% identity, 69% coverage: 107:370/381 of query aligns to 207:468/489 of O94582
- S390 (≠ T292) modified: Phosphoserine
- S392 (≠ A294) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
38% identity, 67% coverage: 114:370/381 of query aligns to 229:488/505 of 5cwaA
- active site: Q248 (= Q133), E301 (= E181), A317 (≠ K198), E345 (= E226), H382 (≠ Q263), T409 (≠ S290), Y433 (= Y314), R453 (= R334), G469 (= G351), E482 (= E364), K486 (= K368)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y314), I452 (= I333), A466 (≠ V348), G467 (= G349), K486 (= K368)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
34% identity, 69% coverage: 107:368/381 of query aligns to 283:559/577 of Q94GF1
- D323 (≠ S148) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
36% identity, 60% coverage: 114:340/381 of query aligns to 308:531/595 of P32068
- D341 (≠ S148) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
33% identity, 67% coverage: 116:370/381 of query aligns to 238:500/512 of 1i1qA
- active site: Q259 (= Q133), E305 (= E181), A323 (≠ K198), E357 (= E226), H394 (≠ Q263), T421 (≠ S290), Y445 (= Y314), R465 (= R334), G481 (= G351), E494 (= E364), K498 (= K368)
- binding tryptophan: P287 (≠ G163), Y288 (≠ Q164), M289 (≠ G165), G450 (= G319), C461 (≠ N330)
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)
33% identity, 67% coverage: 116:370/381 of query aligns to 242:504/520 of P00898
- N288 (≠ Q160) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P161) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ G165) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A166) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S177) mutation to S: Decrease in feedback control by tryptophan.
- R402 (= R267) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G325) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N330) 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)
31% identity, 67% coverage: 114:370/381 of query aligns to 243:503/519 of P00897
- PYM 290:292 (≠ GQG 163:165) binding L-tryptophan
- E360 (= E226) binding Mg(2+)
- E497 (= E364) binding Mg(2+)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
31% identity, 67% coverage: 114:370/381 of query aligns to 235:495/511 of 1i7sA
- active site: Q254 (= Q133), E300 (= E181), A318 (≠ K198), E352 (= E226), H389 (≠ Q263), T416 (≠ S290), Y440 (= Y314), R460 (= R334), G476 (= G351), E489 (= E364), K493 (= K368)
- binding tryptophan: P282 (≠ G163), Y283 (≠ Q164), M284 (≠ G165), V444 (≠ M318), G445 (= G319), D454 (≠ A328), C456 (≠ N330)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
31% identity, 67% coverage: 114:370/381 of query aligns to 241:501/517 of 1i7qA
- active site: Q260 (= Q133), E306 (= E181), A324 (≠ K198), E358 (= E226), H395 (≠ Q263), T422 (≠ S290), Y446 (= Y314), R466 (= R334), G482 (= G351), E495 (= E364), K499 (= K368)
- binding magnesium ion: E358 (= E226), E495 (= E364)
- binding pyruvic acid: Y446 (= Y314), I465 (= I333), R466 (= R334), A479 (≠ V348), G480 (= G349), K499 (= K368)
5jxzA A low magnesium structure of the isochorismate synthase, entc (see paper)
31% identity, 67% coverage: 112:365/381 of query aligns to 109:360/373 of 5jxzA
- active site: K130 (≠ Q133), E180 (= E181), A196 (≠ K198), E224 (= E226), H259 (≠ Q263), A286 (≠ S290), F310 (≠ Y314), R330 (= R334), G346 (= G351), E359 (= E364)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: L195 (≠ M197), G197 (= G199), S198 (≠ T200), E224 (= E226), A286 (≠ S290), I329 (= I333), R330 (= R334), A343 (≠ V348), G344 (= G349), E359 (= E364)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E180 (= E181), L195 (≠ M197), A196 (≠ K198), G197 (= G199), E224 (= E226), A286 (≠ S290), I329 (= I333), R330 (= R334), G344 (= G349), A345 (≠ G350), E359 (= E364)
- binding magnesium ion: E224 (= E226), E359 (= E364)
Sites not aligning to the query:
Query Sequence
>WP_011841694.1 NCBI__GCF_000015985.1:WP_011841694.1
MFLCENGPRSGPALFREPVETVIVEEPAALAPALARLDALRAEGFWIAGTVAYEAGLVFE
PRLARLMPPQRSEPLLAFGAFRAPLPAGDLLAQAAAEAGEVRLAPFRPRIARADYDAAFG
RLMAYIAAGDCYQVNLTFPLDGRLEAGSALGLYGALRARQPVGQGAFCDLGGPVAISASP
ELFFDCDAEGRISTRPMKGTAPRDPDPARDAELAKILGSSEKGRAENLMIVDLLRNDIGR
IAELGSVRVPELFAIESYATVHQMVSRVTGRLIGWPGLSGLLPALFPCGSVTGAPKIRAM
EIIGELEPFPRGLYCGAMGWMAPDGRAAFNVAIRTLRLFPGGELRLDVGGGIVQDSTAPG
EWEEALWKTRFAELPTTPTCG
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