SitesBLAST
Comparing AZOBR_RS29550 FitnessBrowser__azobra:AZOBR_RS29550 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)
P45744 Isochorismate synthase DhbC; Isochorismate mutase; EC 5.4.4.2 from Bacillus subtilis (strain 168) (see paper)
45% identity, 91% coverage: 21:385/401 of query aligns to 24:395/398 of P45744
- S271 (= S261) modified: Phosphoserine
5jxzA A low magnesium structure of the isochorismate synthase, entc (see paper)
42% identity, 91% coverage: 21:385/401 of query aligns to 7:373/373 of 5jxzA
- active site: K130 (= K141), E180 (= E191), A196 (= A207), E224 (= E235), H259 (= H270), A286 (= A298), F310 (≠ Y322), R330 (= R342), G346 (= G358), E359 (= E371), K363 (= K375)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: L195 (= L206), G197 (= G208), S198 (= S209), E224 (= E235), A286 (= A298), I329 (= I341), R330 (= R342), A343 (= A355), G344 (= G356), E359 (= E371), K363 (= K375)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E180 (= E191), L195 (= L206), A196 (= A207), G197 (= G208), E224 (= E235), A286 (= A298), I329 (= I341), R330 (= R342), G344 (= G356), A345 (= A357), E359 (= E371), K363 (= K375)
- binding magnesium ion: E224 (= E235), E359 (= E371)
5jy8A An iron-bound structure of the isochorismate synthase entc (see paper)
43% identity, 91% coverage: 21:385/401 of query aligns to 6:368/368 of 5jy8A
- active site: K125 (= K141), E175 (= E191), A191 (= A207), E219 (= E235), H254 (= H270), A281 (= A298), F305 (≠ Y322), R325 (= R342), G341 (= G358), E354 (= E371), K358 (= K375)
- binding fe (iii) ion: E219 (= E235), E237 (≠ P253), H239 (≠ A255), E354 (= E371)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E175 (= E191), L190 (= L206), A191 (= A207), G192 (= G208), E219 (= E235), L282 (≠ I299), I324 (= I341), F337 (≠ Y354), A338 (= A355), G339 (= G356), E354 (= E371), K358 (= K375)
P0AEJ2 Isochorismate synthase EntC; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see paper)
42% identity, 91% coverage: 21:385/401 of query aligns to 21:390/391 of P0AEJ2
- T140 (≠ F134) binding
- T142 (≠ D136) binding
- V145 (≠ L139) binding
- D146 (≠ R140) binding
- G214 (= G208) binding
- S215 (= S209) binding
- E241 (= E235) binding ; binding
- A303 (= A298) binding ; mutation to T: Loss of mutase activity.
- L304 (≠ I299) mutation to A: Loss of mutase activity.
- F327 (≠ Y322) mutation to Y: Loss of mutase activity.
- I346 (= I341) mutation to L: Loss of mutase activity.
- R347 (= R342) binding
- F359 (≠ Y354) mutation to Q: Loss of mutase activity.
- G361 (= G356) binding
- E376 (= E371) binding
- K380 (= K375) binding
3hwoA Crystal structure of escherichia coli enterobactin-specific isochorismate synthase entc in complex with isochorismate (see paper)
42% identity, 91% coverage: 21:385/401 of query aligns to 9:378/379 of 3hwoA
- active site: K135 (= K141), E185 (= E191), A201 (= A207), E229 (= E235), H264 (= H270), A291 (= A298), F315 (≠ Y322), R335 (= R342), G351 (= G358), E364 (= E371), K368 (= K375)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: G202 (= G208), S203 (= S209), E229 (= E235), H264 (= H270), I334 (= I341), R335 (= R342), A348 (= A355), G349 (= G356), E364 (= E371), K368 (= K375)
- binding magnesium ion: T128 (≠ F134), T130 (≠ D136), V133 (≠ L139), D134 (≠ R140), E229 (= E235), E364 (= E371)
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)
33% identity, 58% coverage: 149:381/401 of query aligns to 261:513/524 of A0QX93
- K355 (≠ A224) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
33% identity, 58% coverage: 149:381/401 of query aligns to 240:488/499 of 7bvdA
- active site: Q248 (≠ A157), E301 (= E191), A317 (= A207), E341 (= E235), H378 (= H270), T405 (≠ A298), Y429 (= Y322), R449 (= R342), G465 (= G358), E478 (= E371), K482 (= K375)
Sites not aligning to the query:
P38051 Isochorismate synthase MenF; Isochorismate hydroxymutase; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see 2 papers)
33% identity, 61% coverage: 139:382/401 of query aligns to 188:430/431 of P38051
- K190 (= K141) active site, Proton acceptor; mutation to A: Lack of activity.
- E240 (= E191) active site, Proton donor; mutation to Q: Lack of activity.
- L255 (= L206) mutation to A: Decrease in activity.
- E284 (= E235) binding
- A344 (= A298) mutation to T: Lack of activity.
- R387 (= R342) mutation to A: Lack of activity.
- E416 (= E371) binding
3bznA Crystal structure of open form of menaquinone-specific isochorismate synthase, menf (see paper)
33% identity, 61% coverage: 139:382/401 of query aligns to 188:430/430 of 3bznA
- active site: K190 (= K141), E240 (= E191), A256 (= A207), E284 (= E235), H318 (= H270), A344 (= A298), Y368 (= Y322), R387 (= R342), G403 (= G358), E416 (= E371), K420 (vs. gap)
- binding magnesium ion: E284 (= E235), E416 (= E371)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
32% identity, 56% coverage: 158:381/401 of query aligns to 263:492/505 of 5cwaA
- active site: E301 (= E191), A317 (= A207), E345 (= E235), H382 (= H270), T409 (≠ A298), Y433 (= Y322), R453 (= R342), G469 (= G358), E482 (= E371), K486 (= K375)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y322), I452 (= I341), A466 (= A355), G467 (= G356), K486 (= K375)
Sites not aligning to the query:
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 65% coverage: 115:375/401 of query aligns to 283:559/577 of Q94GF1
- D323 (vs. gap) 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)
29% identity, 65% coverage: 117:376/401 of query aligns to 209:467/489 of O94582
- S390 (≠ C300) modified: Phosphoserine
- S392 (≠ T302) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
7pi1DDD Aminodeoxychorismate synthase component 1
26% identity, 64% coverage: 124:379/401 of query aligns to 192:449/459 of 7pi1DDD
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)
26% identity, 64% coverage: 124:379/401 of query aligns to 199:456/470 of P28820
- A283 (= A207) 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.
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
28% identity, 77% coverage: 70:379/401 of query aligns to 112:418/424 of 5jy9B
- active site: K183 (= K141), E230 (= E191), A246 (= A207), E274 (= E235), H311 (= H270), T338 (≠ A298), Y362 (= Y322), R381 (= R342), G397 (= G358), E410 (= E371), K414 (= K375)
- binding fe (ii) ion: E274 (= E235), E410 (= E371)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
30% identity, 67% coverage: 113:379/401 of query aligns to 139:402/408 of 2fn1A
- active site: K167 (= K141), E214 (= E191), A230 (= A207), E258 (= E235), H295 (= H270), T322 (≠ A298), Y346 (= Y322), R365 (= R342), G381 (= G358), E394 (= E371), K398 (= K375)
- binding magnesium ion: E258 (= E235), E394 (= E371)
- binding pyruvic acid: Y346 (= Y322), L364 (≠ I341), R365 (= R342), A378 (= A355), G379 (= G356), K398 (= K375)
2fn0A Crystal structure of yersinia enterocolitica salicylate synthase (irp9) (see paper)
30% identity, 67% coverage: 113:379/401 of query aligns to 139:402/408 of 2fn0A
- active site: K167 (= K141), E214 (= E191), A230 (= A207), E258 (= E235), H295 (= H270), T322 (≠ A298), Y346 (= Y322), R365 (= R342), G381 (= G358), E394 (= E371), K398 (= K375)
- binding acetate ion: Y346 (= Y322), L364 (≠ I341), R365 (= R342), A378 (= A355), G379 (= G356)
- binding magnesium ion: E258 (= E235), E394 (= E371)
- binding phosphate ion: A230 (= A207), G231 (= G208), T232 (≠ S209), E258 (= E235), G381 (= G358), E394 (= E371), K398 (= K375)
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)
27% identity, 83% coverage: 44:375/401 of query aligns to 218:577/595 of P32068
- D341 (vs. gap) 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)
30% identity, 70% coverage: 108:386/401 of query aligns to 226:509/512 of 1i1qA
- active site: Q259 (≠ K141), E305 (= E191), A323 (= A207), E357 (= E235), H394 (= H270), T421 (≠ A298), Y445 (= Y322), R465 (= R342), G481 (= G358), E494 (= E371), K498 (= K375)
- binding tryptophan: P287 (≠ A172), Y288 (= Y173), M289 (≠ V174), G450 (= G327), C461 (≠ A338)
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)
30% identity, 70% coverage: 108:386/401 of query aligns to 230:513/520 of P00898
- N288 (= N169) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P170) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ V174) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F175) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G187) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ E274) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G333) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A338) 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.
Query Sequence
>AZOBR_RS29550 FitnessBrowser__azobra:AZOBR_RS29550
MDVLPLPAGERPLGGRSDPDFAFASRGRVLKAYGVDERLDVALDDRSFADGRWEEALDRA
FRRRKAQGVENPILVGAVPFDGRQHARLFIPEHCDYEDAGRMAADPDPVALNAVEETVGR
NAFEAAVAQAIDLFRDTALRKVVLSRPLDVEAREAFAPSRLLRALLRQNPGAYVFAAPVA
YGQTLVGASPELLIRKTGRTVISNPLAGSAPRSLSAEVERQRTAALLASTKDRTEHRYVV
DAVRAALAGHCSPLAVPDAPSVIRTPTMLHLSTELTGELADPMVSSLRLAHALHPTPAIC
GTPTDLARDAIDRLEGYARNWYGGMVGWMDSRGNGEWALSIRCGLVQGRHLRLYAGAGVV
ADSDPAAEWEETAAKLTTMLNLFGVASARPSNTDLPVELAS
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