SitesBLAST
Comparing WP_017223547.1 NCBI__GCF_000276805.1:WP_017223547.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 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)
71% identity, 100% coverage: 1:554/555 of query aligns to 1:554/554 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 (= E349) 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: 2:516/555 of query aligns to 1:496/497 of 1ct9A
- active site: A1 (≠ C2), L50 (= L51), N74 (= N75), G75 (= G76), T305 (= T322), R308 (= R325), E332 (= E349), M366 (= M383)
- binding adenosine monophosphate: L232 (= L233), L233 (= L234), S234 (= S235), S239 (= S240), A255 (≠ S272), V256 (= V273), D263 (= D280), M316 (= M333), S330 (= S347), G331 (= G348), E332 (= E349)
- binding glutamine: A1 (≠ C2), R49 (= R50), L50 (= L51), I52 (= I53), V53 (= V54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D99)
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)
49% identity, 99% coverage: 1:552/555 of query aligns to 1:555/557 of P78753
- S391 (≠ F384) modified: Phosphoserine
- S489 (= S474) 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)
41% identity, 92% coverage: 1:508/555 of query aligns to 1:528/561 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 (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)
41% identity, 87% coverage: 28:508/555 of query aligns to 23:502/509 of 6gq3A
- active site: L49 (= L51), N74 (= N75), G75 (= G76), T324 (= T322), R327 (= R325)
- 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: 60:454/555 of query aligns to 57:435/485 of 1mb9A
- active site: A70 (= A73), G71 (= G76), D310 (≠ T322), Y336 (≠ E349), E370 (≠ M383), K431 (= K450)
- binding adenosine monophosphate: V235 (≠ L233), L236 (= L234), S242 (= S240), S260 (= S272), M261 (≠ V273), Y314 (≠ A326), L318 (≠ M330), G335 (= G348), Y336 (≠ E349)
- binding adenosine-5'-triphosphate: V235 (≠ L233), L236 (= L234), S237 (= S235), G239 (= G237), D241 (= D239), S242 (= S240), S260 (= S272), M261 (≠ V273), L318 (≠ M330), G335 (= G348), D339 (= D352), K411 (= K430), K431 (= K450)
- binding magnesium ion: D241 (= D239), D339 (= D352)
- binding pyrophosphate 2-: S237 (= S235), G239 (= G237), D241 (= D239), S242 (= S240), D339 (= D352), K411 (= K430), K431 (= K450)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 72% coverage: 60:460/555 of query aligns to 52:437/491 of 1mc1A
- active site: A65 (= A73), G66 (= G76), D306 (≠ T322), Y332 (≠ E349), E366 (≠ M383), K427 (= K450)
- binding adenosine monophosphate: V231 (≠ L233), S233 (= S235), S238 (= S240), S256 (= S272), M257 (≠ V273), G331 (= G348), K427 (= K450), V430 (≠ F453)
- binding magnesium ion: D237 (= D239), D335 (= D352)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A326), Y332 (≠ E349), G333 (= G350), I336 (≠ E353), D357 (≠ T374), E366 (≠ M383), K427 (= K450)
- binding pyrophosphate 2-: S233 (= S235), G235 (= G237), D237 (= D239), S238 (= S240), D335 (= D352), K407 (= K430), K427 (= K450), L428 (≠ E451)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 72% coverage: 60:460/555 of query aligns to 56:442/496 of 1mbzA
- active site: A69 (= A73), G70 (= G76), D311 (≠ T322), Y337 (≠ E349), E371 (≠ M383), K432 (= K450)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L233), L237 (= L234), S238 (= S235), S243 (= S240), S261 (= S272), M262 (≠ V273), Y315 (≠ A326), L319 (≠ M330), G336 (= G348), Y337 (≠ E349), G338 (= G350), D340 (= D352), I341 (≠ E353), D362 (≠ T374), E371 (≠ M383), K432 (= K450), G434 (≠ Q452), V435 (≠ F453)
- binding magnesium ion: D242 (= D239), D340 (= D352)
- binding pyrophosphate 2-: S238 (= S235), G240 (= G237), D242 (= D239), S243 (= S240), D340 (= D352), K412 (= K430), K432 (= K450), L433 (≠ E451)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
26% identity, 70% coverage: 60:450/555 of query aligns to 60:440/500 of 1jgtB
- active site: A73 (= A73), G74 (= G76), D319 (≠ T322), Y345 (≠ E349), E379 (≠ M383), K440 (= K450)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L233), L245 (= L234), S246 (= S235), G248 (= G237), I249 (≠ L238), D250 (= D239), S251 (= S240), S269 (= S272), M270 (≠ V273), L327 (≠ M330), G344 (= G348), Y345 (≠ E349), D348 (= D352), K420 (= K430), K440 (= K450)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A326), Y345 (≠ E349), G346 (= G350), D348 (= D352), I349 (≠ E353), M354 (≠ Y358), D370 (≠ T374), E379 (≠ M383)
- binding magnesium ion: D250 (= D239), D348 (= D352)
1q19A Carbapenam synthetase (see paper)
27% identity, 46% coverage: 231:487/555 of query aligns to 241:476/500 of 1q19A