SitesBLAST
Comparing 203782 FitnessBrowser__MR1:203782 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)
3bznA Crystal structure of open form of menaquinone-specific isochorismate synthase, menf (see paper)
35% identity, 99% coverage: 4:449/452 of query aligns to 2:428/430 of 3bznA
- active site: K190 (= K209), E240 (= E259), A256 (= A275), E284 (= E303), H318 (= H338), A344 (= A365), Y368 (= Y389), R387 (= R408), G403 (= G424), E416 (= E437), K420 (= K441)
- binding magnesium ion: E284 (= E303), E416 (= E437)
P38051 Isochorismate synthase MenF; Isochorismate hydroxymutase; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 99% coverage: 4:449/452 of query aligns to 2:428/431 of P38051
- K190 (= K209) active site, Proton acceptor; mutation to A: Lack of activity.
- E240 (= E259) active site, Proton donor; mutation to Q: Lack of activity.
- L255 (= L274) mutation to A: Decrease in activity.
- E284 (= E303) binding Mg(2+)
- A344 (= A365) mutation to T: Lack of activity.
- R387 (= R408) mutation to A: Lack of activity.
- E416 (= E437) binding Mg(2+)
8w71A Structural basis of chorismate isomerization by arabidopsis isochorismate synthase ics1 (see paper)
33% identity, 90% coverage: 39:443/452 of query aligns to 63:487/494 of 8w71A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: R252 (≠ K209), E302 (= E259), A319 (≠ G276), T320 (= T277), H381 (= H338), A408 (= A365), Y432 (= Y389), I450 (= I407), R451 (= R408), A465 (= A421), G466 (= G422), K485 (= K441)
- binding magnesium ion: G468 (= G424), E478 (= E434)
8w6vA Structural basis of chorismate isomerization by arabidopsis isochorismate synthase ics1 (see paper)
33% identity, 90% coverage: 39:443/452 of query aligns to 63:487/494 of 8w6vA
3hwoA Crystal structure of escherichia coli enterobactin-specific isochorismate synthase entc in complex with isochorismate (see paper)
28% identity, 62% coverage: 168:449/452 of query aligns to 94:376/379 of 3hwoA
- active site: K135 (= K209), E185 (= E259), A201 (= A275), E229 (= E303), H264 (= H338), A291 (= A365), F315 (≠ Y389), R335 (= R408), G351 (= G424), E364 (= E437), K368 (= K441)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: G202 (= G276), S203 (≠ T277), E229 (= E303), H264 (= H338), I334 (= I407), R335 (= R408), A348 (= A421), G349 (= G422), E364 (= E437), K368 (= K441)
- binding magnesium ion: T128 (≠ K202), T130 (≠ N204), V133 (≠ T207), D134 (≠ P208), E229 (= E303), E364 (= E437)
P45744 Isochorismate synthase DhbC; Isochorismate mutase; EC 5.4.4.2 from Bacillus subtilis (strain 168) (see paper)
32% identity, 59% coverage: 185:449/452 of query aligns to 121:393/398 of P45744
- S271 (≠ T329) modified: Phosphoserine
P0AEJ2 Isochorismate synthase EntC; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see paper)
28% identity, 62% coverage: 168:449/452 of query aligns to 106:388/391 of P0AEJ2
- T140 (≠ K202) binding Mg(2+)
- T142 (≠ N204) binding Mg(2+)
- V145 (≠ T207) binding Mg(2+)
- D146 (≠ P208) binding Mg(2+)
- G214 (= G276) binding isochorismate
- S215 (≠ T277) binding isochorismate
- E241 (= E303) binding isochorismate; binding Mg(2+)
- A303 (= A365) binding isochorismate; mutation to T: Loss of mutase activity.
- L304 (≠ V366) mutation to A: Loss of mutase activity.
- F327 (≠ Y389) mutation to Y: Loss of mutase activity.
- I346 (= I407) mutation to L: Loss of mutase activity.
- R347 (= R408) binding isochorismate
- F359 (= F420) mutation to Q: Loss of mutase activity.
- G361 (= G422) binding isochorismate
- E376 (= E437) binding Mg(2+)
- K380 (= K441) binding isochorismate
5jxzA A low magnesium structure of the isochorismate synthase, entc (see paper)
28% identity, 60% coverage: 177:449/452 of query aligns to 98:371/373 of 5jxzA
- active site: K130 (= K209), E180 (= E259), A196 (= A275), E224 (= E303), H259 (= H338), A286 (= A365), F310 (≠ Y389), R330 (= R408), G346 (= G424), E359 (= E437), K363 (= K441)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: L195 (= L274), G197 (= G276), S198 (≠ T277), E224 (= E303), A286 (= A365), I329 (= I407), R330 (= R408), A343 (= A421), G344 (= G422), E359 (= E437), K363 (= K441)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E180 (= E259), L195 (= L274), A196 (= A275), G197 (= G276), E224 (= E303), A286 (= A365), I329 (= I407), R330 (= R408), G344 (= G422), A345 (= A423), E359 (= E437), K363 (= K441)
- binding magnesium ion: E224 (= E303), E359 (= E437)
5jy8A An iron-bound structure of the isochorismate synthase entc (see paper)
28% identity, 60% coverage: 177:449/452 of query aligns to 93:366/368 of 5jy8A
- active site: K125 (= K209), E175 (= E259), A191 (= A275), E219 (= E303), H254 (= H338), A281 (= A365), F305 (≠ Y389), R325 (= R408), G341 (= G424), E354 (= E437), K358 (= K441)
- binding fe (iii) ion: E219 (= E303), E237 (≠ Y321), H239 (≠ G323), E354 (= E437)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E175 (= E259), L190 (= L274), A191 (= A275), G192 (= G276), E219 (= E303), L282 (≠ V366), I324 (= I407), F337 (= F420), A338 (= A421), G339 (= G422), E354 (= E437), K358 (= K441)
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)
29% identity, 58% coverage: 191:451/452 of query aligns to 215:476/489 of O94582
- S390 (≠ G367) modified: Phosphoserine
- S392 (≠ L369) 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)
27% identity, 68% coverage: 142:447/452 of query aligns to 176:492/505 of 5cwaA
- active site: Q248 (≠ K209), E301 (= E259), A317 (= A275), E345 (= E303), H382 (= H338), T409 (≠ A365), Y433 (= Y389), R453 (= R408), G469 (= G424), E482 (= E437), K486 (= K441)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y389), I452 (= I407), A466 (= A421), G467 (= G422), K486 (= K441)
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)
29% identity, 47% coverage: 224:437/452 of query aligns to 233:448/470 of P28820
- A283 (= A275) 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
29% identity, 47% coverage: 224:437/452 of query aligns to 226:441/459 of 7pi1DDD
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)
28% identity, 51% coverage: 218:447/452 of query aligns to 276:513/524 of A0QX93
- K355 (≠ N292) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
29% identity, 59% coverage: 180:445/452 of query aligns to 286:563/577 of Q94GF1
- D323 (= D225) 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)
26% identity, 66% coverage: 147:445/452 of query aligns to 260:581/595 of P32068
- D341 (= D225) 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]
28% identity, 51% coverage: 218:447/452 of query aligns to 255:488/499 of 7bvdA
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)
28% identity, 53% coverage: 209:446/452 of query aligns to 263:507/520 of P00898
- N288 (= N237) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P238) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ Q242) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F243) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S255) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ A342) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (≠ D399) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S404) 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
28% identity, 53% coverage: 209:446/452 of query aligns to 259:503/512 of 1i1qA
- active site: Q259 (≠ K209), E305 (= E259), A323 (= A275), E357 (= E303), H394 (= H338), T421 (≠ A365), Y445 (= Y389), R465 (= R408), G481 (= G424), E494 (= E437), K498 (= K441)
- binding tryptophan: P287 (≠ S240), Y288 (≠ F241), M289 (≠ Q242), G450 (= G394), C461 (≠ S404)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
29% identity, 54% coverage: 209:450/452 of query aligns to 183:423/424 of 5jy9B
- active site: K183 (= K209), E230 (= E259), A246 (= A275), E274 (= E303), H311 (= H338), T338 (≠ A365), Y362 (= Y389), R381 (= R408), G397 (= G424), E410 (= E437), K414 (= K441)
- binding fe (ii) ion: E274 (= E303), E410 (= E437)
Query Sequence
>203782 FitnessBrowser__MR1:203782
MPAHALSEDLKSLIDKLIQMKQVPATEPIVQLSLKTVSIPLISWLASQTLYPRIYWHGRD
KVEEVAAIGACKDFKFETGVDDKALASVYEQQRMLSSNPDIRYYGGVAFDRSIESWPEFG
NTRFVLPRIEFRRSANQFSLRVNLNFADNNPIDEIDLAIAAIEAVMPARPLAPPNKLTLV
SRQDIPDFPHWKTLVEQVIEPKFNQDTPKVVLSRLTELEVNEQVDPWMVLACWQGRNPNS
FQFGFQFSPDRTYISCSPERLFRRSQQELFTEALAGTTVRGLNQEEDVALANALLEDNKN
SVENQLVRRHIVSMLTPLSQYVGAEEEATIFKLNHIQHLHRAIRAELKPGVSDFQLLQAL
HPTPAVGGLPRESAMTFIRQREGYMRGWYAGACGYFNKDESEFSVAIRSALIEPGKINLF
AGAGIIAGSDPEAEWQELENKLATIMSILIEL
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