SitesBLAST
Comparing WP_015933298.1 NCBI__GCF_000022085.1:WP_015933298.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
31% identity, 91% coverage: 1:426/470 of query aligns to 1:460/554 of P22106
- M1 (= M1) modified: Initiator methionine, Removed
- C2 (= C2) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
- H30 (= H24) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D28) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y74) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A99) mutation to H: Little effect on the kinetic properties.
- E349 (= E317) mutation E->A,Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity.; mutation to D: 5-fold increase in affinity for aspartate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry.
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
32% identity, 90% coverage: 3:426/470 of query aligns to 2:440/497 of 1ct9A
- active site: L50 (= L45), N74 (= N68), G75 (= G69), T305 (≠ A290), R308 (≠ E293), E332 (= E317), M366 (≠ R354)
- binding adenosine monophosphate: L232 (= L215), L233 (≠ I216), S234 (= S217), S239 (= S222), A255 (≠ T240), V256 (≠ A241), D263 (= D249), M316 (≠ L301), S330 (= S315), G331 (= G316), E332 (= E317)
- binding glutamine: R49 (= R44), L50 (= L45), I52 (≠ L47), V53 (= V48), N74 (= N68), G75 (= G69), E76 (= E70), D98 (= D93)
Sites not aligning to the query:
P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 91% coverage: 1:426/470 of query aligns to 1:475/557 of P78753
- S391 (≠ G355) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
28% identity, 90% coverage: 1:422/470 of query aligns to 1:473/561 of P08243
- C2 (= C2) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- A6 (vs. gap) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (vs. gap) to E: in dbSNP:rs1049674
- F362 (vs. gap) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
Sites not aligning to the query:
- 550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
28% identity, 84% coverage: 21:415/470 of query aligns to 22:453/509 of 6gq3A
- active site: L49 (= L45), N74 (= N68), G75 (= G69), T324 (≠ A290), R327 (≠ E293)
- binding 5-oxo-l-norleucine: R48 (= R44), V51 (≠ L47), V52 (= V48), Y73 (≠ F67), N74 (= N68), G75 (= G69), E76 (= E70), V95 (≠ G92), D96 (= D93)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 78% coverage: 69:435/470 of query aligns to 66:446/491 of 1mc1A
- active site: G66 (= G69), D306 (≠ E293), Y332 (≠ E317), E366 (≠ K362), K427 (= K416)
- binding adenosine monophosphate: V231 (≠ C214), S233 (= S217), S238 (= S222), S256 (≠ T240), M257 (≠ A241), G331 (= G316), K427 (= K416), V430 (≠ F419)
- binding magnesium ion: D237 (= D221), D335 (= D320)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ L297), Y332 (≠ E317), G333 (≠ A318), I336 (≠ E321), D357 (≠ A353), E366 (≠ K362), K427 (= K416)
- binding pyrophosphate 2-: S233 (= S217), G235 (= G219), D237 (= D221), S238 (= S222), D335 (= D320), K407 (= K396), K427 (= K416), L428 (≠ D417)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 78% coverage: 69:435/470 of query aligns to 70:451/496 of 1mbzA
- active site: G70 (= G69), D311 (≠ E293), Y337 (≠ E317), E371 (≠ K362), K432 (= K416)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ C214), L237 (= L215), S238 (= S217), S243 (= S222), S261 (≠ T240), M262 (≠ A241), Y315 (≠ L297), L319 (= L301), G336 (= G316), Y337 (≠ E317), G338 (≠ A318), D340 (= D320), I341 (≠ E321), D362 (≠ A353), E371 (≠ K362), K432 (= K416), G434 (≠ T418), V435 (≠ F419)
- binding magnesium ion: D242 (= D221), D340 (= D320)
- binding pyrophosphate 2-: S238 (= S217), G240 (= G219), D242 (= D221), S243 (= S222), D340 (= D320), K412 (= K396), K432 (= K416), L433 (≠ D417)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
25% identity, 74% coverage: 69:416/470 of query aligns to 74:440/500 of 1jgtB
- active site: G74 (= G69), D319 (≠ E293), Y345 (≠ E317), E379 (≠ K362), K440 (= K416)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ C214), L245 (= L215), S246 (= S217), G248 (= G219), I249 (≠ L220), D250 (= D221), S251 (= S222), S269 (≠ T240), M270 (≠ A241), L327 (= L301), G344 (= G316), Y345 (≠ E317), D348 (= D320), K420 (= K396), K440 (= K416)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ L297), Y345 (≠ E317), G346 (≠ A318), D348 (= D320), I349 (≠ E321), M354 (≠ Y326), D370 (≠ A353), E379 (≠ K362)
- binding magnesium ion: D250 (= D221), D348 (= D320)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 75% coverage: 69:420/470 of query aligns to 71:435/485 of 1mb9A
- active site: G71 (= G69), D310 (≠ E293), Y336 (≠ E317), E370 (≠ K362), K431 (= K416)
- binding adenosine monophosphate: V235 (≠ C214), L236 (= L215), S242 (= S222), S260 (≠ T240), M261 (≠ A241), Y314 (≠ L297), L318 (= L301), G335 (= G316), Y336 (≠ E317)
- binding adenosine-5'-triphosphate: V235 (≠ C214), L236 (= L215), S237 (= S217), G239 (= G219), D241 (= D221), S242 (= S222), S260 (≠ T240), M261 (≠ A241), L318 (= L301), G335 (= G316), D339 (= D320), K411 (= K396), K431 (= K416)
- binding magnesium ion: D241 (= D221), D339 (= D320)
- binding pyrophosphate 2-: S237 (= S217), G239 (= G219), D241 (= D221), S242 (= S222), D339 (= D320), K411 (= K396), K431 (= K416)
Sites not aligning to the query:
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
27% identity, 43% coverage: 2:203/470 of query aligns to 1:224/460 of 6lbpA
Sites not aligning to the query:
- active site: 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 43% coverage: 2:203/470 of query aligns to 87:310/561 of Q9STG9
- H187 (≠ F67) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ I136) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P137) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
Sites not aligning to the query:
- 371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
- 476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
- 494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
26% identity, 29% coverage: 19:152/470 of query aligns to 20:190/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
26% identity, 29% coverage: 19:152/470 of query aligns to 20:194/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
26% identity, 29% coverage: 19:152/470 of query aligns to 31:205/476 of P00497
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 247 binding
- 294 binding
- 356 binding
- 357 binding
- 393 binding
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding ; C→S: Loss of activity.
- 451 binding ; C→S: Loss of activity.
- 452 F→C: Lethal.
Query Sequence
>WP_015933298.1 NCBI__GCF_000022085.1:WP_015933298.1
MCGIIGSFNLPGFDVSSRLEQLAHRGPDGSGVLSAGPAVHGHVRLSLVDLTSASDQPFRY
GDAVLTFNGEIWNYQEVRAQLQAEGVRFRTAGDTEVLAAVLHRWGVHGLARLEGMFAFAW
SKGEMHILVRDRFGEIPLYVHRKGNGFAWSSERKGLGRDCPAAPLPPGCVLDLPNGEVRP
WYERPEHPGINDRLISLVRDGVERRLVADAPLCCLISGGLDSSLVLALAKARKPDVVAYT
AVLDGESADLRAARRLCDEFEVPLVEVPVPAPTGDALEAAARAIEIDSKAQVEIAALCIP
LAHAIASDGFKACLSGEAADELFGGYGNMCIKGASASDIGWREIRVAQLLKMARGNFVRC
NKAFMAAGVECRLPFIERRLVEAVIAMTKAECPPGKGALKQAAAGIVPGWVVKRPKDTFQ
GGAGMSDAAGRVLPDPAAFYRSVVQTAYGPAAIARPPAGRRTARASRRAA
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