SitesBLAST
Comparing WP_041751063.1 NCBI__GCF_000015165.1:WP_041751063.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
31% identity, 85% coverage: 19:520/590 of query aligns to 23:433/497 of 1ct9A
- active site: L50 (= L49), N74 (= N74), G75 (= G75), T305 (≠ S347), R308 (≠ H348), E332 (≠ Q371), M366 (= M451)
- binding adenosine monophosphate: L232 (= L266), L233 (= L267), S234 (= S268), S239 (= S273), A255 (≠ S292), V256 (≠ I293), D263 (≠ E305), M316 (≠ L356), S330 (= S369), G331 (= G370), E332 (≠ Q371)
- binding glutamine: R49 (= R48), L50 (= L49), I52 (= I51), V53 (≠ L52), N74 (= N74), G75 (= G75), E76 (≠ C76), D98 (= D99)
Sites not aligning to the query:
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: 1:520/590 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 (≠ A28) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D32) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ F80) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K105) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q371) 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.
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)
27% identity, 85% coverage: 1:503/590 of query aligns to 1:443/557 of P78753
- S391 (≠ D446) 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)
25% identity, 65% coverage: 2:383/590 of query aligns to 1:364/509 of 6gq3A
- active site: W4 (≠ C5), L49 (= L49), N74 (= N74), G75 (= G75), T324 (≠ S347), R327 (≠ H348)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R48), V51 (≠ I51), V52 (≠ L52), Y73 (≠ F73), N74 (= N74), G75 (= G75), E76 (≠ C76), V95 (≠ G98), D96 (= D99)
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, 65% coverage: 1:383/590 of query aligns to 1:377/561 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 (≠ R218) to E: in dbSNP:rs1049674
- F362 (≠ Q368) 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)
27% identity, 56% coverage: 72:402/590 of query aligns to 67:367/496 of 1mbzA
- active site: A69 (≠ N74), G70 (= G75), D311 (= D349), Y337 (≠ Q371)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L266), L237 (= L267), S238 (= S268), S243 (= S273), S261 (= S292), M262 (≠ I293), Y315 (≠ F353), L319 (≠ S357), G336 (= G370), Y337 (≠ Q371), G338 (= G372), D340 (= D374), I341 (≠ E375), D362 (≠ Q397)
- binding magnesium ion: D242 (= D272), D340 (= D374)
- binding pyrophosphate 2-: S238 (= S268), G240 (= G270), D242 (= D272), S243 (= S273), D340 (= D374)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 56% coverage: 72:402/590 of query aligns to 71:375/500 of 1jgtB
- active site: A73 (≠ N74), G74 (= G75), D319 (= D349), Y345 (≠ Q371)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L266), L245 (= L267), S246 (= S268), G248 (= G270), I249 (≠ L271), D250 (= D272), S251 (= S273), S269 (= S292), M270 (≠ I293), L327 (≠ S357), G344 (= G370), Y345 (≠ Q371), D348 (= D374)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ F353), Y345 (≠ Q371), G346 (= G372), D348 (= D374), I349 (≠ E375), M354 (≠ Y380), D370 (≠ Q397)
- binding magnesium ion: D250 (= D272), D348 (= D374)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 56% coverage: 72:402/590 of query aligns to 63:362/491 of 1mc1A
- active site: A65 (≠ N74), G66 (= G75), D306 (= D349), Y332 (≠ Q371)
- binding adenosine monophosphate: V231 (≠ L266), S233 (= S268), S238 (= S273), S256 (= S292), M257 (≠ I293), G331 (= G370)
- binding magnesium ion: D237 (= D272), D335 (= D374)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ F353), Y332 (≠ Q371), G333 (= G372), I336 (≠ E375), D357 (≠ Q397)
- binding pyrophosphate 2-: S233 (= S268), G235 (= G270), D237 (= D272), S238 (= S273), D335 (= D374)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 56% coverage: 72:402/590 of query aligns to 68:366/485 of 1mb9A
- active site: A70 (≠ N74), G71 (= G75), D310 (= D349), Y336 (≠ Q371)
- binding adenosine monophosphate: V235 (≠ L266), L236 (= L267), S242 (= S273), S260 (= S292), M261 (≠ I293), Y314 (≠ F353), L318 (≠ S357), G335 (= G370), Y336 (≠ Q371)
- binding adenosine-5'-triphosphate: V235 (≠ L266), L236 (= L267), S237 (= S268), G239 (= G270), D241 (= D272), S242 (= S273), S260 (= S292), M261 (≠ I293), L318 (≠ S357), G335 (= G370), D339 (= D374)
- binding magnesium ion: D241 (= D272), D339 (= D374)
- binding pyrophosphate 2-: S237 (= S268), G239 (= G270), D241 (= D272), S242 (= S273), D339 (= D374)
Sites not aligning to the query:
P14742 Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; GFAT; D-fructose-6-phosphate amidotransferase; Hexosephosphate aminotransferase; EC 2.6.1.16 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 18% coverage: 1:107/590 of query aligns to 1:148/717 of P14742
- M1 (= M1) modified: Initiator methionine, Removed
- C2 (= C2) active site, For GATase activity
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, 20% coverage: 263:379/590 of query aligns to 241:353/503 of Q9XB61
- 244:251 (vs. 266:273, 88% identical) binding ATP
- I270 (= I293) binding ATP
- GYGSD 344:348 (≠ GQGAD 370:374) binding ATP
- Y345 (≠ Q371) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G372) binding substrate
Sites not aligning to the query:
- 371 binding substrate
- 374 binding substrate
- 380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
- 421 binding ATP
- 443 mutation K->A,M: Loss of activity.
- 444:446 binding ATP
1q19A Carbapenam synthetase (see paper)
28% identity, 20% coverage: 263:379/590 of query aligns to 240:352/500 of 1q19A
- active site: L318 (≠ M345), E321 (≠ H348), Y344 (≠ Q371)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L266), L244 (= L267), S245 (= S268), D249 (= D272), S250 (= S273), S268 (= S292), I269 (= I293), T342 (≠ S369), G343 (= G370), D347 (= D374)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q371), G345 (= G372), L348 (≠ E375)
Sites not aligning to the query:
1xfgA Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate (see paper)
34% identity, 17% coverage: 2:103/590 of query aligns to 1:127/238 of 1xfgA
- active site: C1 (= C2), R26 (= R29), G27 (= G30), W74 (vs. gap), N98 (= N74), G99 (= G75)
- binding glutamine hydroxamate: C1 (= C2), R73 (vs. gap), W74 (vs. gap), T76 (vs. gap), H86 (vs. gap), N98 (= N74), G99 (= G75), D123 (= D99)
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
34% identity, 17% coverage: 2:103/590 of query aligns to 1:127/238 of 1xffA
- active site: C1 (= C2), R26 (= R29), G27 (= G30), W74 (vs. gap), N98 (= N74), G99 (= G75)
- binding glutamic acid: C1 (= C2), R73 (vs. gap), W74 (vs. gap), T76 (vs. gap), H86 (vs. gap), N98 (= N74), G99 (= G75), D123 (= D99)
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
34% identity, 17% coverage: 2:103/590 of query aligns to 1:127/608 of 4amvA