SitesBLAST
Comparing AZOBR_RS07490 FitnessBrowser__azobra:AZOBR_RS07490 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)
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)
46% identity, 92% coverage: 26:490/503 of query aligns to 48:512/524 of A0QX93
- K355 (≠ E333) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
45% identity, 92% coverage: 26:490/503 of query aligns to 28:487/499 of 7bvdA
- active site: Q248 (= Q253), E301 (= E300), A317 (= A316), E341 (= E344), H378 (= H381), T405 (= T408), Y429 (= Y432), R449 (= R452), G465 (= G468), E478 (= E481), K482 (= K485)
- binding pyruvic acid: S93 (≠ I98), G94 (≠ D99), A100 (≠ S105)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
46% identity, 92% coverage: 26:490/503 of query aligns to 28:491/505 of 5cwaA
- active site: Q248 (= Q253), E301 (= E300), A317 (= A316), E345 (= E344), H382 (= H381), T409 (= T408), Y433 (= Y432), R453 (= R452), G469 (= G468), E482 (= E481), K486 (= K485)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y432), I452 (≠ L451), A466 (= A465), G467 (= G466), K486 (= K485)
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)
39% identity, 99% coverage: 1:496/503 of query aligns to 1:477/489 of O94582
- S390 (= S410) modified: Phosphoserine
- S392 (≠ A412) 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)
37% identity, 93% coverage: 34:500/503 of query aligns to 19:467/470 of P28820
- A283 (= A316) 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.
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)
39% identity, 94% coverage: 22:492/503 of query aligns to 82:584/595 of P32068
- D341 (≠ S267) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 93% coverage: 25:492/503 of query aligns to 69:566/577 of Q94GF1
- D323 (≠ S267) mutation to N: Insensitive to feedback inhibition by tryptophan.
7pi1DDD Aminodeoxychorismate synthase component 1
36% identity, 92% coverage: 34:494/503 of query aligns to 17:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G468), E438 (= E478)
- binding tryptophan: L33 (≠ F50), E34 (= E51), S35 (= S52), G39 (= G56), Y41 (= Y64), P242 (= P282), Y243 (≠ F283), M244 (≠ L284), Q406 (≠ D446), N408 (≠ C448)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
41% identity, 73% coverage: 124:492/503 of query aligns to 142:506/517 of 1i7qA
- active site: Q260 (= Q253), E306 (= E300), A324 (= A316), E358 (= E344), H395 (= H381), T422 (= T408), Y446 (= Y432), R466 (= R452), G482 (= G468), E495 (= E481), K499 (= K485)
- binding magnesium ion: E358 (= E344), E495 (= E481)
- binding pyruvic acid: Y446 (= Y432), I465 (≠ L451), R466 (= R452), A479 (= A465), G480 (= G466), K499 (= K485)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
40% identity, 73% coverage: 124:492/503 of query aligns to 136:500/511 of 1i7sA
- active site: Q254 (= Q253), E300 (= E300), A318 (= A316), E352 (= E344), H389 (= H381), T416 (= T408), Y440 (= Y432), R460 (= R452), G476 (= G468), E489 (= E481), K493 (= K485)
- binding tryptophan: P282 (= P282), Y283 (≠ F283), M284 (≠ L284), V444 (= V436), G445 (= G437), D454 (= D446), C456 (= C448)
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)
39% identity, 72% coverage: 130:492/503 of query aligns to 148:509/520 of P00898
- C174 (≠ I157) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N279) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P280) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L284) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F285) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G296) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N385) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G443) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C448) 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
39% identity, 72% coverage: 130:492/503 of query aligns to 144:505/512 of 1i1qA
- active site: Q259 (= Q253), E305 (= E300), A323 (= A316), E357 (= E344), H394 (= H381), T421 (= T408), Y445 (= Y432), R465 (= R452), G481 (= G468), E494 (= E481), K498 (= K485)
- binding tryptophan: P287 (= P282), Y288 (≠ F283), M289 (≠ L284), G450 (= G437), C461 (= C448)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
40% identity, 73% coverage: 124:492/503 of query aligns to 144:508/519 of P00897
Sites not aligning to the query:
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)
34% identity, 78% coverage: 102:495/503 of query aligns to 79:453/453 of P05041
- E258 (= E300) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A316) 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 (= G317) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R353) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R358) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T364) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H381) 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:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
33% identity, 78% coverage: 102:495/503 of query aligns to 77:437/437 of 1k0eA
- active site: E256 (= E300), K272 (≠ A316), E286 (= E344), H323 (= H381), S350 (≠ T408), W374 (≠ Y432), R394 (= R452), G410 (= G468), E423 (= E481), K427 (= K485)
- binding tryptophan: P238 (= P282), F239 (= F283), S240 (≠ L284)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
40% identity, 52% coverage: 232:492/503 of query aligns to 369:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I315), K454 (≠ A316), G455 (= G317), T456 (= T318), M547 (≠ V409), Y570 (= Y432), R590 (= R452), V603 (≠ A465), G604 (= G466), G605 (= G467), A606 (≠ G468), E619 (= E481), K623 (= K485)
- binding tryptophan: P419 (= P282), Y420 (≠ F283), G421 (≠ L284), L574 (≠ V436), G575 (= G437)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
40% identity, 52% coverage: 232:492/503 of query aligns to 408:669/673 of 8hx8A
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 78% coverage: 102:495/503 of query aligns to 79:420/420 of 1k0gA
- active site: E258 (= E300), K274 (= K340), E278 (= E344), S333 (≠ T408), W357 (≠ Y432), R377 (= R452), G393 (= G468), E406 (= E481), K410 (= K485)
- binding phosphate ion: D113 (= D135), R116 (= R138), D347 (= D422), R353 (= R428)
- binding tryptophan: P240 (= P282), F241 (= F283), S242 (≠ L284)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 78% coverage: 102:491/503 of query aligns to 79:413/415 of 1k0gB
- active site: E258 (= E300), K274 (≠ A316), E277 (= E344), S330 (≠ T408), W354 (≠ Y432), R374 (= R452), G390 (= G468), E403 (= E481), K407 (= K485)
- binding phosphate ion: Y112 (= Y131), D113 (= D135), R116 (= R138), D344 (= D422), R350 (= R428)
- binding tryptophan: P240 (= P282), F241 (= F283)
Sites not aligning to the query:
6za5B M. Tuberculosis salicylate synthase mbti in complex with salicylate and mg2+ (see paper)
35% identity, 49% coverage: 242:485/503 of query aligns to 185:429/440 of 6za5B
- active site: K196 (≠ Q253), E243 (= E300), A260 (= A316), E288 (= E344), H325 (= H381), T352 (= T408), Y376 (= Y432), R396 (= R452), G412 (= G468), E425 (= E481), K429 (= K485)
- binding magnesium ion: E288 (= E344), E425 (= E481)
Query Sequence
>AZOBR_RS07490 FitnessBrowser__azobra:AZOBR_RS07490
VKVQPEFAAFHTAYEAGKPQVVWTTLVSDLETPVSAYMKLADGRPFGFLFESAERGAGSR
RDRYSVIGFKPDLVWRCRRDRAEVNRNALHDRDAYEPIDAAPLESLRALINESRIDLPDA
LPPMAAGLFGYLTYDMVRLMERLPDDNPDELGIPDAILSRPSIVAIFDSHTDSVTLVTPV
WPKPGVDGAAAYGDARERLMDAVADLERPLPYRREPRTKDGLPLAWTSNTTREEYHAIVE
RAKEYIRAGDIFQVVPSQRIRFPFKPSPLALYRTLRRLNPSPFLFHCDFGELSVVGSSPE
ILVRVRDGNVTVRPIAGTRKRGATAAEDQALAEDLLSDPKELAEHLMLLDLGRNDVGRVA
RTGTVKVTQKMIVELYSHVMHIVSNVEGDLDPKHDALDALIAGFPAGTVSGAPKVRAMQI
IDELEKARRGVYAGCVGYFGASGAMDTCIALRTAVLKDGMMYVQAGGGVVADSDPEAEYQ
ETVNKSMALIRAAEETVRETSAQ
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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