SitesBLAST
Comparing WP_092994459.1 NCBI__GCF_900102855.1:WP_092994459.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 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)
29% identity, 88% coverage: 1:523/597 of query aligns to 1:453/554 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 (vs. gap) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K106) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q370) 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)
29% identity, 84% coverage: 24:523/597 of query aligns to 23:433/497 of 1ct9A
- active site: L50 (= L50), N74 (= N75), G75 (= G76), T305 (≠ G346), R308 (≠ Q347), E332 (≠ Q370), M366 (≠ G434)
- binding adenosine monophosphate: L232 (= L265), L233 (= L266), S234 (= S267), S239 (= S272), A255 (≠ S291), V256 (= V292), D263 (≠ E299), M316 (≠ L355), S330 (= S368), G331 (= G369), E332 (≠ Q370)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ I53), N74 (= N75), G75 (= G76), E76 (≠ T77), D98 (= D100)
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, 80% coverage: 26:505/597 of query aligns to 27:442/557 of P78753
- S391 (≠ D453) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
27% identity, 83% coverage: 26:522/597 of query aligns to 22:456/509 of 6gq3A
- active site: L49 (= L50), N74 (= N75), G75 (= G76), T324 (≠ M344), R327 (≠ Q347)
- binding 5-oxo-l-norleucine: R48 (= R49), V51 (≠ I52), V52 (≠ I53), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (≠ T77), V95 (≠ G99), D96 (= D100)
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)
25% identity, 91% coverage: 4:547/597 of query aligns to 1:493/561 of P08243
- C2 (= C5) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- A6 (≠ R9) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ R220) to E: in dbSNP:rs1049674
- F362 (≠ Q367) 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
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 60% coverage: 36:396/597 of query aligns to 25:366/496 of 1mbzA
- active site: A69 (≠ N75), G70 (= G76), D311 (≠ M344), Y337 (≠ Q370)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L265), L237 (= L266), S238 (= S267), S243 (= S272), S261 (= S291), M262 (≠ V292), Y315 (≠ D348), L319 (≠ F352), G336 (= G369), Y337 (≠ Q370), G338 (= G371), D340 (= D373), I341 (≠ E374), D362 (= D392)
- binding magnesium ion: D242 (= D271), D340 (= D373)
- binding pyrophosphate 2-: S238 (= S267), G240 (= G269), D242 (= D271), S243 (= S272), D340 (= D373)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
28% identity, 60% coverage: 36:396/597 of query aligns to 29:374/500 of 1jgtB
- active site: A73 (≠ N75), G74 (= G76), D319 (≠ M344), Y345 (≠ Q370)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L265), L245 (= L266), S246 (= S267), G248 (= G269), I249 (≠ L270), D250 (= D271), S251 (= S272), S269 (= S291), M270 (≠ V292), L327 (≠ F352), G344 (= G369), Y345 (≠ Q370), D348 (= D373)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ D348), Y345 (≠ Q370), G346 (= G371), D348 (= D373), I349 (≠ E374), M354 (≠ Y379), D370 (= D392)
- binding magnesium ion: D250 (= D271), D348 (= D373)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 61% coverage: 30:396/597 of query aligns to 13:361/491 of 1mc1A
- active site: A65 (≠ N75), G66 (= G76), D306 (≠ M344), Y332 (≠ Q370)
- binding adenosine monophosphate: V231 (≠ L265), S233 (= S267), S238 (= S272), S256 (= S291), M257 (≠ V292), G331 (= G369)
- binding magnesium ion: D237 (= D271), D335 (= D373)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ D348), Y332 (≠ Q370), G333 (= G371), I336 (≠ E374), D357 (= D392)
- binding pyrophosphate 2-: S233 (= S267), G235 (= G269), D237 (= D271), S238 (= S272), D335 (= D373)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 60% coverage: 36:396/597 of query aligns to 26:365/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (≠ M344), Y336 (≠ Q370)
- binding adenosine monophosphate: V235 (≠ L265), L236 (= L266), S242 (= S272), S260 (= S291), M261 (≠ V292), Y314 (≠ D348), L318 (≠ F352), G335 (= G369), Y336 (≠ Q370)
- binding adenosine-5'-triphosphate: V235 (≠ L265), L236 (= L266), S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), S260 (= S291), M261 (≠ V292), L318 (≠ F352), G335 (= G369), D339 (= D373)
- binding magnesium ion: D241 (= D271), D339 (= D373)
- binding pyrophosphate 2-: S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), D339 (= D373)
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
24% identity, 55% coverage: 195:520/597 of query aligns to 171:442/500 of 1q19A
- active site: L318 (≠ M344), E321 (≠ Q347), Y344 (≠ Q370), E379 (≠ D420), K442 (= K520)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L265), L244 (= L266), S245 (= S267), D249 (= D271), S250 (= S272), S268 (= S291), I269 (≠ V292), T342 (≠ S368), G343 (= G369), D347 (= D373), K442 (= K520)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q370), G345 (= G371), L348 (≠ E374), R373 (≠ P414), E379 (≠ D420)
Sites not aligning to the query:
Q9XB61 Carbapenam-3-carboxylate synthase; Carbapenam-3-carboxylate ligase; EC 6.3.3.6 from Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) (see 3 papers)
28% identity, 31% coverage: 195:378/597 of query aligns to 172:353/503 of Q9XB61