SitesBLAST
Comparing WP_057507873.1 NCBI__GCF_001431535.1:WP_057507873.1 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 14 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)
60% identity, 100% coverage: 1:561/563 of query aligns to 1:552/554 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 (= H32) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D36) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H83) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A107) mutation to H: Little effect on the kinetic properties.
- E349 (= E352) 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)
58% identity, 93% coverage: 3:525/563 of query aligns to 2:497/497 of 1ct9A
- active site: L50 (= L53), N74 (= N77), G75 (= G78), T305 (= T325), R308 (= R328), E332 (= E352), M366 (≠ N386)
- binding adenosine monophosphate: L232 (= L236), L233 (= L237), S234 (= S238), S239 (= S243), A255 (= A275), V256 (≠ I276), D263 (= D283), M316 (≠ L336), S330 (= S350), G331 (= G351), E332 (= E352)
- binding glutamine: R49 (= R52), L50 (= L53), I52 (= I55), V53 (= V56), N74 (= N77), G75 (= G78), E76 (= E79), D98 (= D101)
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)
51% identity, 100% coverage: 1:562/563 of query aligns to 1:556/557 of P78753
- S391 (≠ Y387) modified: Phosphoserine
- S489 (= S482) 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)
37% identity, 100% coverage: 1:563/563 of query aligns to 1:561/561 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 (≠ L349) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
- R550 (= R552) 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)
37% identity, 92% coverage: 2:518/563 of query aligns to 1:504/509 of 6gq3A
- active site: W4 (≠ F5), L49 (= L53), N74 (= N77), G75 (= G78), T324 (= T325), R327 (= R328)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R52), V51 (≠ I55), V52 (= V56), Y73 (≠ V76), N74 (= N77), G75 (= G78), E76 (= E79), V95 (≠ S100), D96 (= D101)
1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 68% coverage: 78:462/563 of query aligns to 71:435/485 of 1mb9A
- active site: G71 (= G78), D310 (≠ T325), Y336 (≠ E352), E370 (≠ C389), K431 (= K458)
- binding adenosine monophosphate: V235 (≠ L236), L236 (= L237), S242 (= S243), S260 (≠ A275), M261 (≠ I276), Y314 (≠ A329), L318 (≠ M333), G335 (= G351), Y336 (≠ E352)
- binding adenosine-5'-triphosphate: V235 (≠ L236), L236 (= L237), S237 (= S238), G239 (= G240), D241 (= D242), S242 (= S243), S260 (≠ A275), M261 (≠ I276), L318 (≠ M333), G335 (= G351), D339 (= D355), K411 (= K438), K431 (= K458)
- binding magnesium ion: D241 (= D242), D339 (= D355)
- binding pyrophosphate 2-: S237 (= S238), G239 (= G240), D241 (= D242), S242 (= S243), D339 (= D355), K411 (= K438), K431 (= K458)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
29% identity, 69% coverage: 78:466/563 of query aligns to 66:435/491 of 1mc1A
- active site: G66 (= G78), D306 (≠ T325), Y332 (≠ E352), E366 (≠ C389), K427 (= K458)
- binding adenosine monophosphate: V231 (≠ L236), S233 (= S238), S238 (= S243), S256 (≠ A275), M257 (≠ I276), G331 (= G351), K427 (= K458), V430 (≠ F461)
- binding magnesium ion: D237 (= D242), D335 (= D355)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A329), Y332 (≠ E352), G333 (= G353), I336 (≠ E356), D357 (≠ K380), E366 (≠ C389), K427 (= K458)
- binding pyrophosphate 2-: S233 (= S238), G235 (= G240), D237 (= D242), S238 (= S243), D335 (= D355), K407 (= K438), K427 (= K458), L428 (≠ E459)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
29% identity, 69% coverage: 78:466/563 of query aligns to 70:440/496 of 1mbzA
- active site: G70 (= G78), D311 (≠ T325), Y337 (≠ E352), E371 (≠ C389), K432 (= K458)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L236), L237 (= L237), S238 (= S238), S243 (= S243), S261 (≠ A275), M262 (≠ I276), Y315 (≠ A329), L319 (≠ M333), G336 (= G351), Y337 (≠ E352), G338 (= G353), D340 (= D355), I341 (≠ E356), D362 (≠ K380), E371 (≠ C389), K432 (= K458), G434 (≠ Q460), V435 (≠ F461)
- binding magnesium ion: D242 (= D242), D340 (= D355)
- binding pyrophosphate 2-: S238 (= S238), G240 (= G240), D242 (= D242), S243 (= S243), D340 (= D355), K412 (= K438), K432 (= K458), L433 (≠ E459)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
29% identity, 68% coverage: 78:458/563 of query aligns to 74:440/500 of 1jgtB
- active site: G74 (= G78), D319 (≠ T325), Y345 (≠ E352), E379 (≠ C389), K440 (= K458)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L236), L245 (= L237), S246 (= S238), G248 (= G240), I249 (≠ L241), D250 (= D242), S251 (= S243), S269 (≠ A275), M270 (≠ I276), L327 (≠ M333), G344 (= G351), Y345 (≠ E352), D348 (= D355), K420 (= K438), K440 (= K458)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A329), Y345 (≠ E352), G346 (= G353), D348 (= D355), I349 (≠ E356), M354 (≠ F364), D370 (≠ K380), E379 (≠ C389)
- binding magnesium ion: D250 (= D242), D348 (= D355)
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)
26% identity, 41% coverage: 234:464/563 of query aligns to 242:449/503 of Q9XB61
- 244:251 (vs. 236:243, 88% identical) binding
- I270 (= I276) binding
- GYGSD 344:348 (≠ GEGSD 351:355) binding
- Y345 (≠ E352) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G353) binding
- Q371 (≠ L381) binding
- R374 (≠ L384) binding
- E380 (≠ L390) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K438) binding
- K443 (= K458) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ EQF 459:461) binding
1q19A Carbapenam synthetase (see paper)
26% identity, 41% coverage: 234:464/563 of query aligns to 241:448/500 of 1q19A
- active site: L318 (≠ T325), E321 (≠ R328), Y344 (≠ E352), E379 (≠ L390), K442 (= K458)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L236), L244 (= L237), S245 (= S238), D249 (= D242), S250 (= S243), S268 (≠ A275), I269 (= I276), T342 (≠ S350), G343 (= G351), D347 (= D355), K442 (= K458), I443 (≠ E459), G444 (≠ Q460), I445 (≠ F461)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E352), G345 (= G353), L348 (≠ E356), R373 (≠ L384), E379 (≠ L390)
Sites not aligning to the query:
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
31% identity, 31% coverage: 2:173/563 of query aligns to 12:208/476 of P00497
- C12 (= C2) active site, Nucleophile; mutation to F: Loss of enzyme activity and N-terminal processing.
Sites not aligning to the query:
- 1:11 modified: propeptide
- 247 binding
- 294 binding
- 356 binding
- 357 binding
- 393 binding
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding ; C→S: Loss of activity.
- 451 binding ; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
31% identity, 31% coverage: 2:173/563 of query aligns to 1:197/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
31% identity, 31% coverage: 2:173/563 of query aligns to 1:193/455 of 1ao0A
Sites not aligning to the query:
- active site: 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436
Query Sequence
>WP_057507873.1 NCBI__GCF_001431535.1:WP_057507873.1
MCSIFGIFGLQAGDDLPALRRHALESSQRQRHRGPDWSGVYLDDGALLVHERLAIVDPAG
GSQPLLSEDGGLALAVNGEIYNHQQLKAGLDQPYAFQTGSDCEVINALYRQGEPSQWLER
LNGIFAFALWDKAAGRVLVARDPIGVVPLYWGHDAQGRLRVASELKALVDTCADAAQFPP
GHYYDSATGALVRYYQQSWREYDAVQGKPVDLAELREAFERAVERQLMSDVPYGVLLSGG
LDSSLVAAVAARYARRRIEDGGESEAWWPRLHSFAIGLKGSPDLAAAAIAAEALGTVHHG
FEYTFEEGLDVLPEVIRHIETYDVTTIRASTPMFLLARRIKAMGVKMVLSGEGSDEIFGG
YLYFHKAPDAREFHSELVRKLDALHNYDCLRANKSMMAWGVEPRVPFLDREFLDVAMRFD
AAHKMVGSEASGGRRVEKGVLRAAFEGYLPESILWRQKEQFSDGVGYGWIDGLKAHAEAQ
VSDRVLAAADKRFPHNPPQTKEAYYYRHVFEQYFPSHAAAETVPGGKSIACSSPAAIAWD
ASFAAAADPSGRAIAGVHEAALA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory