SitesBLAST
Comparing WP_028321394.1 NCBI__GCF_000422285.1:WP_028321394.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
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)
40% identity, 87% coverage: 23:493/540 of query aligns to 28:523/557 of P78753
- S391 (≠ I367) modified: Phosphoserine
- S489 (= S459) modified: Phosphoserine
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 91% coverage: 1:492/540 of query aligns to 1:507/554 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 (= H25) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D29) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ F76) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H100) mutation to H: Little effect on the kinetic properties.
- E349 (= E333) 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)
39% identity, 88% coverage: 23:495/540 of query aligns to 27:490/497 of 1ct9A
- active site: L50 (= L46), N74 (= N70), G75 (= G71), T305 (≠ S307), R308 (= R310), E332 (= E333), M366 (≠ N366)
- binding adenosine monophosphate: L232 (≠ F227), L233 (≠ C228), S234 (= S229), S239 (= S234), A255 (≠ V252), V256 (= V253), D263 (= D265), M316 (≠ T318), S330 (≠ T331), G331 (= G332), E332 (= E333)
- binding glutamine: R49 (= R45), L50 (= L46), I52 (= I48), V53 (= V49), N74 (= N70), G75 (= G71), E76 (= E72), D98 (= D94)
Sites not aligning to the query:
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)
35% identity, 91% coverage: 1:492/540 of query aligns to 1:527/561 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 (≠ G6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ I189) to E: in dbSNP:rs1049674
- F362 (≠ L330) 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)
34% identity, 91% coverage: 2:492/540 of query aligns to 1:501/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L46), N74 (= N70), G75 (= G71), T324 (≠ S307), R327 (= R310)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R45), V51 (≠ I48), V52 (= V49), Y73 (vs. gap), N74 (= N70), G75 (= G71), E76 (= E72), V95 (≠ S93), D96 (= D94)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 72% coverage: 61:448/540 of query aligns to 56:438/491 of 1mc1A
- active site: A65 (≠ N70), G66 (= G71), D306 (≠ S307), Y332 (≠ E333), E366 (≠ N366), K427 (= K437)
- binding adenosine monophosphate: V231 (≠ F227), S233 (= S229), S238 (= S234), S256 (≠ V252), M257 (≠ V253), G331 (= G332), K427 (= K437), V430 (≠ Y440)
- binding magnesium ion: D237 (= D233), D335 (= D336)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ C311), Y332 (≠ E333), G333 (= G334), I336 (≠ E337), D357 (≠ A357), E366 (≠ N366), K427 (= K437)
- binding pyrophosphate 2-: S233 (= S229), G235 (= G231), D237 (= D233), S238 (= S234), D335 (= D336), K407 (= K415), K427 (= K437), L428 (≠ V438)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 72% coverage: 61:448/540 of query aligns to 60:443/496 of 1mbzA
- active site: A69 (≠ N70), G70 (= G71), D311 (≠ S307), Y337 (≠ E333), E371 (≠ N366), K432 (= K437)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F227), L237 (≠ C228), S238 (= S229), S243 (= S234), S261 (≠ V252), M262 (≠ V253), Y315 (≠ C311), L319 (≠ C315), G336 (= G332), Y337 (≠ E333), G338 (= G334), D340 (= D336), I341 (≠ E337), D362 (≠ A357), E371 (≠ N366), K432 (= K437), G434 (≠ Q439), V435 (≠ Y440)
- binding magnesium ion: D242 (= D233), D340 (= D336)
- binding pyrophosphate 2-: S238 (= S229), G240 (= G231), D242 (= D233), S243 (= S234), D340 (= D336), K412 (= K415), K432 (= K437), L433 (≠ V438)
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 71% coverage: 61:442/540 of query aligns to 61:436/485 of 1mb9A
- active site: A70 (≠ N70), G71 (= G71), D310 (≠ S307), Y336 (≠ E333), E370 (≠ N366), K431 (= K437)
- binding adenosine monophosphate: V235 (≠ F227), L236 (≠ C228), S242 (= S234), S260 (≠ V252), M261 (≠ V253), Y314 (≠ C311), L318 (≠ C315), G335 (= G332), Y336 (≠ E333)
- binding adenosine-5'-triphosphate: V235 (≠ F227), L236 (≠ C228), S237 (= S229), G239 (= G231), D241 (= D233), S242 (= S234), S260 (≠ V252), M261 (≠ V253), L318 (≠ C315), G335 (= G332), D339 (= D336), K411 (= K415), K431 (= K437)
- binding magnesium ion: D241 (= D233), D339 (= D336)
- binding pyrophosphate 2-: S237 (= S229), G239 (= G231), D241 (= D233), S242 (= S234), D339 (= D336), K411 (= K415), K431 (= K437)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
25% identity, 71% coverage: 61:441/540 of query aligns to 64:444/500 of 1jgtB
- active site: A73 (≠ N70), G74 (= G71), D319 (≠ S307), Y345 (≠ E333), E379 (≠ N366), K440 (= K437)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F227), L245 (≠ C228), S246 (= S229), G248 (= G231), I249 (≠ L232), D250 (= D233), S251 (= S234), S269 (≠ V252), M270 (≠ V253), L327 (≠ C315), G344 (= G332), Y345 (≠ E333), D348 (= D336), K420 (= K415), K440 (= K437)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ C311), Y345 (≠ E333), G346 (= G334), D348 (= D336), I349 (≠ E337), M354 (≠ Y342), D370 (≠ A357), E379 (≠ N366)
- binding magnesium ion: D250 (= D233), D348 (= D336)
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
29% identity, 29% coverage: 2:159/540 of query aligns to 1:201/460 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)
29% identity, 29% coverage: 2:159/540 of query aligns to 87:287/561 of Q9STG9