SitesBLAST
Comparing WP_007513181.1 NCBI__GCF_021560695.1:WP_007513181.1 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)
7pi1DDD Aminodeoxychorismate synthase component 1
39% identity, 85% coverage: 63:444/449 of query aligns to 65:453/459 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)
39% identity, 86% coverage: 63:448/449 of query aligns to 67:464/470 of P28820
- A283 (= A268) 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.
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)
38% identity, 80% coverage: 86:444/449 of query aligns to 94:451/453 of P05041
- E258 (= E252) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A268) 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 (= G269) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R304) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R309) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T315) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H332) 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)
37% identity, 80% coverage: 86:444/449 of query aligns to 92:435/437 of 1k0eA
- active site: E256 (= E252), K272 (≠ A268), E286 (= E295), H323 (= H332), S350 (≠ T359), W374 (≠ Y383), R394 (= R403), G410 (= G419), E423 (= E432), K427 (= K436)
- binding tryptophan: P238 (= P234), F239 (= F235), S240 (≠ A236)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
46% identity, 55% coverage: 194:442/449 of query aligns to 239:492/505 of 5cwaA
- active site: Q248 (= Q203), E301 (= E252), A317 (= A268), E345 (= E295), H382 (= H332), T409 (= T359), Y433 (= Y383), R453 (= R403), G469 (= G419), E482 (= E432), K486 (= K436)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y383), I452 (= I402), A466 (= A416), G467 (= G417), K486 (= K436)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 83% coverage: 72:444/449 of query aligns to 240:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I267), K454 (≠ A268), G455 (= G269), T456 (= T270), M547 (≠ I360), Y570 (= Y383), R590 (= R403), V603 (≠ A416), G604 (= G417), G605 (≠ A418), A606 (≠ G419), E619 (= E432), K623 (= K436)
- binding tryptophan: P419 (= P234), Y420 (≠ F235), G421 (≠ A236), L574 (= L387), G575 (= G388)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 83% coverage: 72:444/449 of query aligns to 282:670/673 of 8hx8A
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)
35% identity, 95% coverage: 18:442/449 of query aligns to 63:513/524 of A0QX93
- K355 (≠ R284) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
43% identity, 58% coverage: 183:442/449 of query aligns to 228:488/499 of 7bvdA
- active site: Q248 (= Q203), E301 (= E252), A317 (= A268), E341 (= E295), H378 (= H332), T405 (= T359), Y429 (= Y383), R449 (= R403), G465 (= G419), E478 (= E432), K482 (= K436)
Sites not aligning to the query:
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)
33% identity, 96% coverage: 13:444/449 of query aligns to 31:474/489 of O94582
- S390 (≠ T361) modified: Phosphoserine
- S392 (≠ C363) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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, 83% coverage: 73:446/449 of query aligns to 124:512/520 of P00898
- R128 (≠ D77) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ L126) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N231) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P232) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A236) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ G237) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S248) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N336) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G394) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N399) 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
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
34% identity, 83% coverage: 73:446/449 of query aligns to 120:508/512 of 1i1qA
- active site: Q259 (= Q203), E305 (= E252), A323 (= A268), E357 (= E295), H394 (= H332), T421 (= T359), Y445 (= Y383), R465 (= R403), G481 (= G419), E494 (= E432), K498 (= K436)
- binding tryptophan: P287 (= P234), Y288 (≠ F235), M289 (≠ A236), G450 (= G388), C461 (≠ N399)
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)
34% identity, 79% coverage: 94:449/449 of query aligns to 189:590/595 of P32068
- D341 (≠ Q216) 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)
35% identity, 81% coverage: 86:449/449 of query aligns to 161:572/577 of Q94GF1
- D323 (≠ Q216) mutation to N: Insensitive to feedback inhibition by tryptophan.
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
34% identity, 80% coverage: 86:444/449 of query aligns to 94:418/420 of 1k0gA
- active site: E258 (= E252), K274 (= K291), E278 (= E295), S333 (≠ T359), W357 (≠ Y383), R377 (= R403), G393 (= G419), E406 (= E432), K410 (= K436)
- binding phosphate ion: D113 (≠ E105), R116 (≠ G108), D347 (≠ A373), R353 (≠ P379)
- binding tryptophan: P240 (= P234), F241 (= F235), S242 (≠ A236)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
33% identity, 88% coverage: 52:446/449 of query aligns to 94:503/511 of 1i7sA
- active site: Q254 (= Q203), E300 (= E252), A318 (= A268), E352 (= E295), H389 (= H332), T416 (= T359), Y440 (= Y383), R460 (= R403), G476 (= G419), E489 (= E432), K493 (= K436)
- binding tryptophan: P282 (= P234), Y283 (≠ F235), M284 (≠ A236), V444 (≠ L387), G445 (= G388), D454 (= D397), C456 (≠ N399)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
33% identity, 88% coverage: 52:446/449 of query aligns to 100:509/517 of 1i7qA
- active site: Q260 (= Q203), E306 (= E252), A324 (= A268), E358 (= E295), H395 (= H332), T422 (= T359), Y446 (= Y383), R466 (= R403), G482 (= G419), E495 (= E432), K499 (= K436)
- binding magnesium ion: E358 (= E295), E495 (= E432)
- binding pyruvic acid: Y446 (= Y383), I465 (= I402), R466 (= R403), A479 (= A416), G480 (= G417), K499 (= K436)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
33% identity, 88% coverage: 52:446/449 of query aligns to 102:511/519 of P00897
- PYM 290:292 (≠ PFA 234:236) binding L-tryptophan
- E360 (= E295) binding Mg(2+)
- E497 (= E432) binding Mg(2+)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
34% identity, 80% coverage: 86:444/449 of query aligns to 94:415/415 of 1k0gB
- active site: E258 (= E252), K274 (≠ A268), E277 (= E295), S330 (≠ T359), W354 (≠ Y383), R374 (= R403), G390 (= G419), E403 (= E432), K407 (= K436)
- binding phosphate ion: Y112 (= Y104), D113 (≠ E105), R116 (≠ G108), D344 (≠ A373), R350 (≠ P379)
- binding tryptophan: P240 (= P234), F241 (= F235)
Sites not aligning to the query:
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
31% identity, 57% coverage: 183:436/449 of query aligns to 163:414/424 of 5jy9B
- active site: K183 (≠ Q203), E230 (= E252), A246 (= A268), E274 (= E295), H311 (= H332), T338 (= T359), Y362 (= Y383), R381 (= R403), G397 (= G419), E410 (= E432), K414 (= K436)
- binding fe (ii) ion: E274 (= E295), E410 (= E432)
Query Sequence
>WP_007513181.1 NCBI__GCF_021560695.1:WP_007513181.1
MTCHRRILDGRRDLLAPAAACPGRYPCLLESVVHGTAQSRHDILFAFPRERMSLHADGGL
RDDAGVVREGRFLDALDAAWQAERLPPESDGLPFHGGWVLLLAYELAGEIEPTLKLRPPS
TLPLALAVRCPAAVIVDHVRNCTILVAEAGCEHLLDALEADLAAVPSMPPLPALRDWDED
ARQQFLDGVVRIHEHLHAGDIFQVNLSRAWRAHFAQPPVPASLYAVLRRANPAPFAGLLQ
QPGWAVASSSPERLVEVRGGVAQTRPIAGTRPRLPGDDDTARIRELSAHPKERAEHVMLI
DLERNDLGRVCVPGTVEVDELMAVESYAHVHHIVSNVRGRLRAGVTPGEVIAATFPGGTI
TGCPKVRCMEIIAALEDAPRGAYTGALGYLDRNGELDLNILIRTLTLAGDEVSLRAGAGI
VADSVATSELDETRAKARGLLRALGVPDS
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