SitesBLAST
Comparing WP_068461603.1 NCBI__GCF_001541235.1:WP_068461603.1 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)
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)
45% identity, 92% coverage: 25:489/503 of query aligns to 47:512/524 of A0QX93
- K355 (≠ D332) 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)
44% identity, 92% coverage: 25:489/503 of query aligns to 27:491/505 of 5cwaA
- active site: Q248 (= Q252), E301 (= E299), A317 (= A315), E345 (= E343), H382 (= H380), T409 (= T407), Y433 (= Y431), R453 (= R451), G469 (= G467), E482 (= E480), K486 (= K484)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y431), I452 (≠ L450), A466 (= A464), G467 (= G465), K486 (= K484)
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: 22:495/503 of query aligns to 82:588/595 of P32068
- D341 (≠ P266) 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)
41% identity, 93% coverage: 26:495/503 of query aligns to 70:570/577 of Q94GF1
- D323 (≠ P266) mutation to N: Insensitive to feedback inhibition by tryptophan.
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
44% identity, 92% coverage: 25:489/503 of query aligns to 27:487/499 of 7bvdA
- active site: Q248 (= Q252), E301 (= E299), A317 (= A315), E341 (= E343), H378 (= H380), T405 (= T407), Y429 (= Y431), R449 (= R451), G465 (= G467), E478 (= E480), K482 (= K484)
- binding pyruvic acid: S93 (≠ N91), G94 (≠ A92), A100 (≠ S103)
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, 95% coverage: 22:498/503 of query aligns to 24:480/489 of O94582
- S390 (= S409) modified: Phosphoserine
- S392 (≠ A411) 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, 91% coverage: 34:493/503 of query aligns to 19:461/470 of P28820
- A283 (= A315) 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
37% identity, 91% coverage: 34:493/503 of query aligns to 17:454/459 of 7pi1DDD
- binding magnesium ion: G428 (= G467), E438 (= E477)
- binding tryptophan: L33 (= L50), E34 (= E51), S35 (= S52), G39 (= G56), Y41 (= Y62), P242 (= P281), Y243 (≠ F282), M244 (≠ L283), Q406 (≠ D445), N408 (≠ C447)
1i7qA Anthranilate synthase from s. Marcescens (see paper)
35% identity, 91% coverage: 33:491/503 of query aligns to 18:506/517 of 1i7qA
- active site: Q260 (= Q252), E306 (= E299), A324 (= A315), E358 (= E343), H395 (= H380), T422 (= T407), Y446 (= Y431), R466 (= R451), G482 (= G467), E495 (= E480), K499 (= K484)
- binding magnesium ion: E358 (= E343), E495 (= E480)
- binding pyruvic acid: Y446 (= Y431), I465 (≠ L450), R466 (= R451), A479 (= A464), G480 (= G465), K499 (= K484)
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
34% identity, 92% coverage: 31:495/503 of query aligns to 15:509/512 of 1i1qA
- active site: Q259 (= Q252), E305 (= E299), A323 (= A315), E357 (= E343), H394 (= H380), T421 (= T407), Y445 (= Y431), R465 (= R451), G481 (= G467), E494 (= E480), K498 (= K484)
- binding tryptophan: L34 (= L50), E35 (= E51), S36 (= S52), K46 (≠ Y62), P287 (= P281), Y288 (≠ F282), M289 (≠ L283), G450 (= G436), C461 (= C447)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
34% identity, 92% coverage: 31:495/503 of query aligns to 19:513/520 of P00898
- E39 (= E51) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S52) binding L-tryptophan; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (≠ V53) mutation to V: Decrease in feedback control by tryptophan.
- K50 (≠ Y62) binding L-tryptophan
- R128 (vs. gap) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ I155) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N278) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P279) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L283) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F284) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G295) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N384) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G442) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (= C447) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
Sites not aligning to the query:
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
39% identity, 72% coverage: 128:491/503 of query aligns to 139:500/511 of 1i7sA
- active site: Q254 (= Q252), E300 (= E299), A318 (= A315), E352 (= E343), H389 (= H380), T416 (= T407), Y440 (= Y431), R460 (= R451), G476 (= G467), E489 (= E480), K493 (= K484)
- binding tryptophan: P282 (= P281), Y283 (≠ F282), M284 (≠ L283), V444 (= V435), G445 (= G436), D454 (= D445), C456 (= C447)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
34% identity, 91% coverage: 33:491/503 of query aligns to 20:508/519 of P00897
- S39 (= S52) binding L-tryptophan
- PYM 290:292 (≠ PFL 281:283) binding L-tryptophan
- E360 (= E343) binding Mg(2+)
- E497 (= E480) binding Mg(2+)
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)
31% identity, 95% coverage: 17:494/503 of query aligns to 7:453/453 of P05041
- S36 (= S52) binding L-tryptophan
- E258 (= E299) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A315) 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 (= G316) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R352) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R357) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S363) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H380) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
30% identity, 95% coverage: 18:494/503 of query aligns to 6:437/437 of 1k0eA
- active site: E256 (= E299), K272 (≠ A315), E286 (= E343), H323 (= H380), S350 (≠ T407), W374 (≠ Y431), R394 (= R451), G410 (= G467), E423 (= E480), K427 (= K484)
- binding tryptophan: L32 (= L50), H33 (≠ E51), S34 (= S52), Y41 (≠ R59), F44 (≠ Y62), P238 (= P281), F239 (= F282), S240 (≠ L283)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
28% identity, 95% coverage: 18:494/503 of query aligns to 8:420/420 of 1k0gA
- active site: E258 (= E299), K274 (= K339), E278 (= E343), S333 (≠ T407), W357 (≠ Y431), R377 (= R451), G393 (= G467), E406 (= E480), K410 (= K484)
- binding phosphate ion: D113 (= D133), R116 (= R136), D347 (= D421), R353 (≠ K427)
- binding tryptophan: L34 (= L50), H35 (≠ E51), S36 (= S52), Y43 (≠ R59), S44 (≠ G60), F46 (≠ Y62), P240 (= P281), F241 (= F282), S242 (≠ L283)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
31% identity, 78% coverage: 98:491/503 of query aligns to 238:630/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I314), K454 (≠ A315), G455 (= G316), T456 (= T317), M547 (≠ V408), Y570 (= Y431), R590 (= R451), V603 (≠ A464), G604 (= G465), G605 (≠ A466), A606 (≠ G467), E619 (= E480), K623 (= K484)
- binding tryptophan: P419 (= P281), Y420 (≠ F282), G421 (≠ L283), L574 (≠ V435), G575 (= G436)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
32% identity, 78% coverage: 98:491/503 of query aligns to 280:669/673 of 8hx8A
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
28% identity, 94% coverage: 18:490/503 of query aligns to 8:413/415 of 1k0gB
- active site: E258 (= E299), K274 (≠ A315), E277 (= E343), S330 (≠ T407), W354 (≠ Y431), R374 (= R451), G390 (= G467), E403 (= E480), K407 (= K484)
- binding phosphate ion: Y112 (= Y132), D113 (= D133), R116 (= R136), D344 (= D421), R350 (≠ K427)
- binding tryptophan: L34 (= L50), H35 (≠ E51), S36 (= S52), Y43 (≠ R59), S44 (≠ G60), R45 (= R61), F46 (≠ Y62), P240 (= P281), F241 (= F282)
8qc4A Salicylate synthase (see paper)
34% identity, 48% coverage: 231:469/503 of query aligns to 172:411/438 of 8qc4A
Sites not aligning to the query:
Query Sequence
>WP_068461603.1 NCBI__GCF_001541235.1:WP_068461603.1
MEATPTLADFAARYDGGVAQVLWTRLVADLETPVSAYMKLADEKPMSFLLESVEGGATRG
RYSVIGLEPDLIWRADGDRASINRNPAEKPNAFEPDTQPTLASLRALLAESQIDLPSELP
PMAAGIFGFMGYDTVRLMEKLPGEQADTLGVPDGILMRPTVMAIFDNVKDEITIVTPVRP
SKDLSAKKAHKAACKRLKRAVSALEERLPHTPAKARNKDLAAPTPVSNTTPAEYKTMVER
AKEYIVAGDIFQVVLSQRFSAPFSLPSFALYRALRRTNPSPFLFHLNFGAFALVGSSPEI
LVRVREGEVTIRPIAGTAPRGATEAEDQELADALLKDPKERAEHLMLLDLGRNDVGRVAE
VGSVTVTGRFFIERYSHVMHIVSNVIGKLDAKHDAVDALMAGFPAGTVSGAPKVRAMEVI
DELEKAKRGPYAGCVGYFSASGQMDSCIALRTAIIKDGVMHVQAGAGLVHDSVPEKEQQE
CINKARALFRAAEEAVRFATKTR
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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