SitesBLAST
Comparing 5211261 FitnessBrowser__PV4:5211261 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, 97% coverage: 10:449/452 of query aligns to 1:428/430 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, 97% coverage: 10:449/452 of query aligns to 1:428/431 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
- A344 (= A365) mutation to T: Lack of activity.
- R387 (= R408) mutation to A: Lack of activity.
- E416 (= E437) binding
P45744 Isochorismate synthase DhbC; Isochorismate mutase; EC 5.4.4.2 from Bacillus subtilis (strain 168) (see paper)
32% identity, 53% coverage: 209:449/452 of query aligns to 145:393/398 of P45744
- S271 (≠ K329) modified: Phosphoserine
5jy8A An iron-bound structure of the isochorismate synthase entc (see paper)
26% 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)
5jxzA A low magnesium structure of the isochorismate synthase, entc (see paper)
26% 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)
3hwoA Crystal structure of escherichia coli enterobactin-specific isochorismate synthase entc in complex with isochorismate (see paper)
26% identity, 60% coverage: 177:449/452 of query aligns to 103:376/379 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 (≠ R202), T130 (≠ I204), V133 (≠ T207), D134 (≠ P208), E229 (= E303), E364 (= E437)
P0AEJ2 Isochorismate synthase EntC; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see paper)
26% identity, 60% coverage: 177:449/452 of query aligns to 115:388/391 of P0AEJ2
- T140 (≠ R202) binding
- T142 (≠ I204) binding
- V145 (≠ T207) binding
- D146 (≠ P208) binding
- G214 (= G276) binding
- S215 (≠ T277) binding
- E241 (= E303) binding ; binding
- A303 (= A365) binding ; 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
- F359 (= F420) mutation to Q: Loss of mutase activity.
- G361 (= G422) binding
- E376 (= E437) binding
- K380 (= K441) binding
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
28% identity, 56% coverage: 194:447/452 of query aligns to 237:492/505 of 5cwaA
- active site: Q248 (= Q205), 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)
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)
27% identity, 57% coverage: 191:447/452 of query aligns to 251:513/524 of A0QX93
- K355 (≠ Q292) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
27% identity, 57% coverage: 194:451/452 of query aligns to 222:476/489 of O94582
- S390 (≠ G367) modified: Phosphoserine
- S392 (≠ L369) 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)
27% 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
27% identity, 47% coverage: 224:437/452 of query aligns to 226:441/459 of 7pi1DDD
Sites not aligning to the query:
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
29% identity, 63% coverage: 160:446/452 of query aligns to 213:503/512 of 1i1qA
- active site: Q259 (≠ N196), E305 (= E250), A323 (= A275), E357 (= E303), H394 (= H338), T421 (≠ A365), Y445 (= Y389), R465 (= R408), G481 (= G424), E494 (= E437), K498 (= K441)
- binding tryptophan: P287 (≠ M228), Y288 (≠ L229), M289 (≠ L230), G450 (= G394), C461 (≠ A404)
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)
29% identity, 63% coverage: 160:446/452 of query aligns to 217:507/520 of P00898
- N288 (≠ D225) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P226) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L230) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A231) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ Q246) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ A342) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (vs. gap) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A404) 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.
- 174 C→Y: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
28% identity, 58% coverage: 180:441/452 of query aligns to 286:559/577 of Q94GF1
- D323 (= D225) mutation to N: Insensitive to feedback inhibition by tryptophan.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
26% identity, 57% coverage: 191:447/452 of query aligns to 230:488/499 of 7bvdA
- active site: Q248 (≠ K209), E301 (= E259), A317 (= A275), E341 (= E303), H378 (= H338), T405 (≠ A365), Y429 (= Y389), R449 (= R408), G465 (= G424), E478 (= E437), K482 (= K441)
Sites not aligning to the query:
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)
25% identity, 56% coverage: 191:441/452 of query aligns to 309:577/595 of P32068
- D341 (= D225) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
30% identity, 53% coverage: 209:449/452 of query aligns to 183:422/424 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)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
30% identity, 53% coverage: 209:449/452 of query aligns to 167:406/408 of 2fn1A
- active site: K167 (= K209), E214 (= E259), A230 (= A275), E258 (= E303), H295 (= H338), T322 (≠ A365), Y346 (= Y389), R365 (= R408), G381 (= G424), E394 (= E437), K398 (= K441)
- binding magnesium ion: E258 (= E303), E394 (= E437)
- binding pyruvic acid: Y346 (= Y389), L364 (≠ I407), R365 (= R408), A378 (= A421), G379 (= G422), K398 (= K441)
2fn0A Crystal structure of yersinia enterocolitica salicylate synthase (irp9) (see paper)
30% identity, 53% coverage: 209:449/452 of query aligns to 167:406/408 of 2fn0A
- active site: K167 (= K209), E214 (= E259), A230 (= A275), E258 (= E303), H295 (= H338), T322 (≠ A365), Y346 (= Y389), R365 (= R408), G381 (= G424), E394 (= E437), K398 (= K441)
- binding acetate ion: Y346 (= Y389), L364 (≠ I407), R365 (= R408), A378 (= A421), G379 (= G422)
- binding magnesium ion: E258 (= E303), E394 (= E437)
- binding phosphate ion: A230 (= A275), G231 (= G276), T232 (= T277), E258 (= E303), G381 (= G424), E394 (= E437), K398 (= K441)
Query Sequence
>5211261 FitnessBrowser__PV4:5211261
MSVSSLPQAIQSLSRKLEKLDIHPQGEPIIQLSVTACVMPMIAWIASQPCYPRIYWHGRD
TQEEVAALGCCKDFIFEDAVDDNQLSQAYQTQRSLSTNQEIRYYGGVAFDRHTECWPEYG
RAHFILPRVELRRSGDEYKLLVNLNVESGDIEQERNLALQALAALVPPKPLAPPNKIQLL
SRSDRPNKLRWHELVNQVTHDRFIQDTPKVVLSRLTQLEVNEKVDPWMLLASWQGRNQNS
FQFGFQFSPESAFISCTPERLYRRRQREVFTEALAGTTTRGLNEAEDAMLAQQLLDDTKN
SHENQLVREHIVDALTPLSNYVGADELAKVFKLSHIQHLHRAIRAELKPGVNDFQILQAL
HPTPAVGGLPKASAINFIRQREGYTRGWYAGACGYFNKYESEFAVAIRSALIEPGRINLF
AGAGIVSGSEAEAEWNELENKLKTIMSILTEV
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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