SitesBLAST
Comparing 5209024 FitnessBrowser__PV4:5209024 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 12 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)
70% identity, 100% coverage: 1:552/552 of query aligns to 1:553/554 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 (= H30) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A105) mutation to H: Little effect on the kinetic properties.
- E349 (= E347) 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)
69% identity, 93% coverage: 3:515/552 of query aligns to 2:497/497 of 1ct9A
- active site: L50 (= L51), N74 (= N75), G75 (= G76), T305 (= T320), R308 (= R323), E332 (= E347), M366 (≠ L381)
- binding adenosine monophosphate: L232 (= L231), L233 (= L232), S234 (= S233), S239 (= S238), A255 (= A270), V256 (= V271), D263 (= D278), M316 (= M331), S330 (= S345), G331 (= G346), E332 (= E347)
- binding glutamine: R49 (= R50), L50 (= L51), I52 (= I53), V53 (= V54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D99)
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)
52% identity, 98% coverage: 1:542/552 of query aligns to 1:547/557 of P78753
- S391 (≠ F382) modified: Phosphoserine
- S489 (≠ D472) 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)
42% identity, 91% coverage: 1:505/552 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 (= A6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ Q195) 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)
42% identity, 86% coverage: 30:505/552 of query aligns to 25:501/509 of 6gq3A
- active site: L49 (= L51), N74 (= N75), G75 (= G76), T324 (= T320), R327 (= R323)
- binding 5-oxo-l-norleucine: R48 (= R50), V51 (≠ I53), V52 (= V54), Y73 (≠ V74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S98), D96 (= D99)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 71% coverage: 60:452/552 of query aligns to 57:435/485 of 1mb9A
- active site: A70 (= A73), G71 (= G76), D310 (≠ T320), Y336 (≠ E347), E370 (≠ L381), K431 (= K448)
- binding adenosine monophosphate: V235 (≠ L231), L236 (= L232), S242 (= S238), S260 (≠ A270), M261 (≠ V271), Y314 (≠ A324), L318 (≠ M328), G335 (= G346), Y336 (≠ E347)
- binding adenosine-5'-triphosphate: V235 (≠ L231), L236 (= L232), S237 (= S233), G239 (= G235), D241 (= D237), S242 (= S238), S260 (≠ A270), M261 (≠ V271), L318 (≠ M328), G335 (= G346), D339 (= D350), K411 (= K428), K431 (= K448)
- binding magnesium ion: D241 (= D237), D339 (= D350)
- binding pyrophosphate 2-: S237 (= S233), G239 (= G235), D241 (= D237), S242 (= S238), D339 (= D350), K411 (= K428), K431 (= K448)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 72% coverage: 60:458/552 of query aligns to 52:437/491 of 1mc1A
- active site: A65 (= A73), G66 (= G76), D306 (≠ T320), Y332 (≠ E347), E366 (≠ L381), K427 (= K448)
- binding adenosine monophosphate: V231 (≠ L231), S233 (= S233), S238 (= S238), S256 (≠ A270), M257 (≠ V271), G331 (= G346), K427 (= K448), V430 (≠ F451)
- binding magnesium ion: D237 (= D237), D335 (= D350)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A324), Y332 (≠ E347), G333 (= G348), I336 (≠ E351), D357 (≠ L372), E366 (≠ L381), K427 (= K448)
- binding pyrophosphate 2-: S233 (= S233), G235 (= G235), D237 (= D237), S238 (= S238), D335 (= D350), K407 (= K428), K427 (= K448), L428 (≠ E449)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 72% coverage: 60:458/552 of query aligns to 56:442/496 of 1mbzA
- active site: A69 (= A73), G70 (= G76), D311 (≠ T320), Y337 (≠ E347), E371 (≠ L381), K432 (= K448)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L231), L237 (= L232), S238 (= S233), S243 (= S238), S261 (≠ A270), M262 (≠ V271), Y315 (≠ A324), L319 (≠ M328), G336 (= G346), Y337 (≠ E347), G338 (= G348), D340 (= D350), I341 (≠ E351), D362 (≠ L372), E371 (≠ L381), K432 (= K448), G434 (≠ Q450), V435 (≠ F451)
- binding magnesium ion: D242 (= D237), D340 (= D350)
- binding pyrophosphate 2-: S238 (= S233), G240 (= G235), D242 (= D237), S243 (= S238), D340 (= D350), K412 (= K428), K432 (= K448), L433 (≠ E449)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 70% coverage: 60:448/552 of query aligns to 60:440/500 of 1jgtB
- active site: A73 (= A73), G74 (= G76), D319 (≠ T320), Y345 (≠ E347), E379 (≠ L381), K440 (= K448)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L231), L245 (= L232), S246 (= S233), G248 (= G235), I249 (≠ L236), D250 (= D237), S251 (= S238), S269 (≠ A270), M270 (≠ V271), L327 (≠ M328), G344 (= G346), Y345 (≠ E347), D348 (= D350), K420 (= K428), K440 (= K448)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A324), Y345 (≠ E347), G346 (= G348), D348 (= D350), I349 (≠ E351), M354 (≠ Y356), D370 (≠ L372), E379 (≠ L381)
- binding magnesium ion: D250 (= D237), D348 (= D350)
1q19A Carbapenam synthetase (see paper)
24% identity, 74% coverage: 76:485/552 of query aligns to 56:474/500 of 1q19A