SitesBLAST
Comparing WP_104488606.1 NCBI__GCF_002936955.1:WP_104488606.1 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)
73% identity, 100% coverage: 1:554/554 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 (= 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)
71% identity, 93% coverage: 2:516/554 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 (≠ Q383)
- binding adenosine monophosphate: L232 (= L233), L233 (= L234), S234 (= S235), S239 (= S240), A255 (= A272), 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)
52% identity, 99% coverage: 1:548/554 of query aligns to 1:551/557 of P78753
- S391 (≠ F384) modified: Phosphoserine
- S489 (≠ T474) 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, 99% coverage: 1:546/554 of query aligns to 1:552/561 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 (≠ E9) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ W196) to E: in dbSNP:rs1049674
- F362 (≠ L346) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
- R550 (= R544) to 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, 91% coverage: 6:507/554 of query aligns to 2:501/509 of 6gq3A
- active site: W4 (≠ L8), 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, 74% coverage: 44:454/554 of query aligns to 42:435/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (≠ T322), Y336 (≠ E349), E370 (≠ Q383), K431 (= K450)
- binding adenosine monophosphate: V235 (≠ L233), L236 (= L234), S242 (= S240), S260 (≠ A272), 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 (≠ A272), 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)
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)
26% identity, 69% coverage: 76:456/554 of query aligns to 57:449/503 of Q9XB61
- 244:251 (vs. 233:240, 88% identical) binding ATP
- I270 (≠ V273) binding ATP
- GYGSD 344:348 (≠ GEGSD 348:352) binding ATP
- Y345 (≠ E349) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G350) binding substrate
- Q371 (≠ T374) binding substrate
- R374 (≠ K377) binding substrate
- E380 (≠ Q383) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K430) binding ATP
- K443 (= K450) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ EQF 451:453) binding ATP
1q19A Carbapenam synthetase (see paper)
26% identity, 69% coverage: 76:456/554 of query aligns to 56:448/500 of 1q19A
- active site: G56 (= G76), L318 (≠ T322), E321 (≠ R325), Y344 (≠ E349), E379 (≠ Q383), K442 (= K450)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L233), L244 (= L234), S245 (= S235), D249 (= D239), S250 (= S240), S268 (≠ A272), I269 (≠ V273), T342 (≠ S347), G343 (= G348), D347 (= D352), K442 (= K450), I443 (≠ E451), G444 (≠ Q452), I445 (≠ F453)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E349), G345 (= G350), L348 (≠ E353), R373 (≠ K377), E379 (≠ Q383)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 75% coverage: 44:460/554 of query aligns to 37:437/491 of 1mc1A
- active site: A65 (≠ N75), G66 (= G76), D306 (≠ T322), Y332 (≠ E349), E366 (≠ Q383), K427 (= K450)
- binding adenosine monophosphate: V231 (≠ L233), S233 (= S235), S238 (= S240), S256 (≠ A272), 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 (≠ Q383), 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, 75% coverage: 44:460/554 of query aligns to 41:442/496 of 1mbzA