SitesBLAST
Comparing BPHYT_RS17390 FitnessBrowser__BFirm:BPHYT_RS17390 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)
42% identity, 92% coverage: 31:487/497 of query aligns to 19:461/470 of P28820
- A283 (= A309) 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.
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
40% identity, 98% coverage: 3:487/497 of query aligns to 50:568/577 of Q94GF1
- D323 (≠ N256) 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)
41% identity, 96% coverage: 10:487/497 of query aligns to 73:586/595 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
41% identity, 92% coverage: 31:487/497 of query aligns to 17:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G461), E438 (= E471)
- binding tryptophan: L33 (= L50), E34 (= E51), S35 (= S52), G39 (= G56), Y41 (= Y62), P242 (= P271), Y243 (= Y272), M244 (= M273), Q406 (≠ D439), N408 (≠ A441)
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: 15:490/497 of query aligns to 20:478/489 of O94582
- S390 (= S403) modified: Phosphoserine
- S392 (≠ A405) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
42% identity, 96% coverage: 5:483/497 of query aligns to 31:512/524 of A0QX93
- K355 (≠ T326) 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)
45% identity, 96% coverage: 5:483/497 of query aligns to 11:491/505 of 5cwaA
- active site: Q248 (= Q242), E301 (= E289), A317 (= A309), E345 (= E337), H382 (= H374), T409 (= T401), Y433 (= Y425), R453 (= R445), G469 (= G461), E482 (= E474), K486 (= K478)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y425), I452 (= I444), A466 (= A458), G467 (≠ A459), K486 (= K478)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
41% identity, 96% coverage: 5:483/497 of query aligns to 11:487/499 of 7bvdA
- active site: Q248 (= Q242), E301 (= E289), A317 (= A309), E341 (= E337), H378 (= H374), T405 (= T401), Y429 (= Y425), R449 (= R445), G465 (= G461), E478 (= E474), K482 (= K478)
- binding pyruvic acid: S93 (≠ H92), G94 (≠ E93), A100 (≠ F99)
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
41% identity, 76% coverage: 109:485/497 of query aligns to 129:505/512 of 1i1qA
- active site: Q259 (= Q242), E305 (= E289), A323 (= A309), E357 (= E337), H394 (= H374), T421 (= T401), Y445 (= Y425), R465 (= R445), G481 (= G461), E494 (= E474), K498 (= K478)
- binding tryptophan: P287 (= P271), Y288 (= Y272), M289 (= M273), G450 (= G430), C461 (≠ A441)
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, 76% coverage: 109:485/497 of query aligns to 133:509/520 of P00898
- C174 (≠ Q153) mutation to Y: Almost no change in feedback control by tryptophan.
- 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 (≠ Y274) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G285) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ S378) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G436) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A441) 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.
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, 89% coverage: 47:488/497 of query aligns to 31:453/453 of P05041
- S36 (= S52) binding
- E258 (= E289) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A309) 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 (= G310) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R346) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R351) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S357) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H374) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
40% identity, 75% coverage: 113:485/497 of query aligns to 134:506/517 of 1i7qA
- active site: Q260 (= Q242), E306 (= E289), A324 (= A309), E358 (= E337), H395 (= H374), T422 (= T401), Y446 (= Y425), R466 (= R445), G482 (= G461), E495 (= E474), K499 (= K478)
- binding magnesium ion: E358 (= E337), E495 (= E474)
- binding pyruvic acid: Y446 (= Y425), I465 (= I444), R466 (= R445), A479 (= A458), G480 (≠ A459), K499 (= K478)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
40% identity, 75% coverage: 113:485/497 of query aligns to 128:500/511 of 1i7sA
- active site: Q254 (= Q242), E300 (= E289), A318 (= A309), E352 (= E337), H389 (= H374), T416 (= T401), Y440 (= Y425), R460 (= R445), G476 (= G461), E489 (= E474), K493 (= K478)
- binding tryptophan: P282 (= P271), Y283 (= Y272), M284 (= M273), V444 (= V429), G445 (= G430), D454 (= D439), C456 (≠ A441)
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, 75% coverage: 113:485/497 of query aligns to 136:508/519 of P00897
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 89% coverage: 47:488/497 of query aligns to 29:437/437 of 1k0eA
- active site: E256 (= E289), K272 (≠ A309), E286 (= E337), H323 (= H374), S350 (≠ T401), W374 (≠ Y425), R394 (= R445), G410 (= G461), E423 (= E474), K427 (= K478)
- binding tryptophan: L32 (= L50), H33 (≠ E51), S34 (= S52), Y41 (≠ F59), F44 (≠ Y62), P238 (= P271), F239 (≠ Y272), S240 (≠ M273)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
34% identity, 89% coverage: 45:485/497 of query aligns to 226:669/673 of 8hx8A
- binding magnesium ion: E521 (= E337), E655 (= E471), E658 (= E474)
- binding tryptophan: L231 (= L50), D232 (≠ E51), S233 (= S52), S241 (≠ G60), F243 (≠ Y62), P458 (= P271), Y459 (= Y272), G460 (≠ M273), G614 (= G430)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
34% identity, 89% coverage: 45:485/497 of query aligns to 184:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (≠ L308), K454 (≠ A309), G455 (= G310), T456 (= T311), M547 (≠ L402), Y570 (= Y425), R590 (= R445), V603 (≠ A458), G604 (≠ A459), G605 (≠ A460), A606 (≠ G461), E619 (= E474), K623 (= K478)
- binding tryptophan: L189 (= L50), D190 (≠ E51), S191 (= S52), S199 (≠ G60), F201 (≠ Y62), P419 (= P271), Y420 (= Y272), G421 (≠ M273), L574 (≠ V429), G575 (= G430)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 89% coverage: 47:488/497 of query aligns to 31:420/420 of 1k0gA
- active site: E258 (= E289), K274 (= K333), E278 (= E337), S333 (≠ T401), W357 (≠ Y425), R377 (= R445), G393 (= G461), E406 (= E474), K410 (= K478)
- binding phosphate ion: D113 (= D129), R116 (= R132), D347 (= D415), R353 (≠ K421)
- binding tryptophan: L34 (= L50), H35 (≠ E51), S36 (= S52), Y43 (≠ F59), S44 (≠ G60), F46 (≠ Y62), P240 (= P271), F241 (≠ Y272), S242 (≠ M273)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 88% coverage: 47:484/497 of query aligns to 31:413/415 of 1k0gB
- active site: E258 (= E289), K274 (≠ A309), E277 (= E337), S330 (≠ T401), W354 (≠ Y425), R374 (= R445), G390 (= G461), E403 (= E474), K407 (= K478)
- binding phosphate ion: Y112 (= Y128), D113 (= D129), R116 (= R132), D344 (= D415), R350 (≠ K421)
- binding tryptophan: L34 (= L50), H35 (≠ E51), S36 (= S52), Y43 (≠ F59), S44 (≠ G60), R45 (= R61), F46 (≠ Y62), P240 (= P271), F241 (≠ Y272)
8qc4A Salicylate synthase (see paper)
34% identity, 47% coverage: 228:463/497 of query aligns to 179:411/438 of 8qc4A
Sites not aligning to the query:
Query Sequence
>BPHYT_RS17390 FitnessBrowser__BFirm:BPHYT_RS17390
MTELEFQSLANEGFNRIPLIAEALADLETPLSLYLKLAQSERNGANSFLLESVVGGERFG
RYSFIGLPARTLLRTRNGVSEVVRDGKVVETHEGDPLEFIQQFQGRFKVAQRPGLPRFAG
GLAGYFGYDAVRYIEKKLAHTAPKDDLNLPDIQLLLTEEVAVIDNLAGKLYLVVYSDPTQ
PEAYTKAKQRLRELRQRLRTTVQPPVTSASVRTETYREFAKDDYLAAVRKAKEYIAAGEL
MQVQVGQRLTKPYRDNPLSLYRALRSLNPSPYMYYYNFGDFHVVGASPEILVRQEKRGED
RIVTIRPLAGTRPRGNTPERDAELATELLNDPKEIAEHVMLIDLARNDVGRIAQIGSVVV
TDKMVIEKYSHVQHIVSSVEGKLKPGTTNFDVLRATFPAGTLSGAPKVRAMELIDELEPI
KRGLYGGAVGYLSFTGEMDLAITIRTGVIANGNLYVQAAAGVVADSVPESEWQETENKAR
AVLRAAEQVQDGLDSDF
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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