SitesBLAST
Comparing WP_013644771.1 NCBI__GCF_000191585.1:WP_013644771.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
30% identity, 91% coverage: 25:475/495 of query aligns to 25:437/497 of 1ct9A
- active site: L50 (= L65), N74 (= N86), G75 (≠ A87), T305 (≠ M334), R308 (≠ G337), E332 (≠ Q361), M366 (≠ H397)
- binding adenosine monophosphate: L232 (≠ I259), L233 (≠ F260), S234 (= S261), S239 (= S266), A255 (≠ T284), V256 (= V285), D263 (= D292), M316 (≠ A345), S330 (= S359), G331 (= G360), E332 (≠ Q361)
- binding glutamine: R49 (≠ L64), L50 (= L65), I52 (= I67), V53 (= V68), N74 (= N86), G75 (≠ A87), E76 (= E88), D98 (= D108)
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)
28% identity, 96% coverage: 1:475/495 of query aligns to 1:457/554 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 (= H29) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y92) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ T114) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q361) 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)
29% identity, 88% coverage: 1:436/495 of query aligns to 1:429/557 of P78753
- S391 (≠ V398) modified: Phosphoserine
Sites not aligning to the query:
- 489 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)
29% identity, 96% coverage: 1:475/495 of query aligns to 1:474/561 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 (≠ M214) to E: in dbSNP:rs1049674
- F362 (≠ L358) 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)
28% identity, 93% coverage: 5:465/495 of query aligns to 1:453/509 of 6gq3A
- active site: W4 (≠ L8), L49 (= L65), N74 (= N86), G75 (≠ A87), T324 (≠ M334), R327 (≠ G337)
- binding 5-oxo-l-norleucine: C1 (≠ A5), R48 (≠ L64), V51 (≠ I67), V52 (= V68), Y73 (≠ A85), N74 (= N86), G75 (≠ A87), E76 (= E88), V95 (≠ S107), D96 (= D108)
1q19A Carbapenam synthetase (see paper)
25% identity, 76% coverage: 101:477/495 of query aligns to 74:453/500 of 1q19A
- active site: L318 (≠ M340), E321 (≠ Y343), Y344 (≠ Q361), E379 (≠ D403), K442 (= K466)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ I259), L244 (≠ F260), S245 (= S261), D249 (= D265), S250 (= S266), S268 (≠ T284), I269 (≠ V285), T342 (≠ S359), G343 (= G360), D347 (= D364), K442 (= K466), I443 (≠ K467), G444 (≠ A468), I445 (≠ A469)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q361), G345 (= G362), L348 (≠ E365), R373 (≠ H397), E379 (≠ D403)
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)
25% identity, 76% coverage: 101:477/495 of query aligns to 75:454/503 of Q9XB61
- 244:251 (vs. 259:266, 75% identical) binding ATP
- I270 (≠ V285) binding ATP
- GYGSD 344:348 (≠ GQGAD 360:364) binding ATP
- Y345 (≠ Q361) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G362) binding substrate
- Q371 (≠ N394) binding substrate
- R374 (≠ H397) binding substrate
- E380 (≠ D403) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K445) binding ATP
- K443 (= K466) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ KAA 467:469) binding ATP
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
22% identity, 84% coverage: 72:487/495 of query aligns to 51:448/491 of 1mc1A
- active site: A65 (≠ N86), G66 (≠ A87), D306 (≠ M334), Y332 (≠ Q361), E366 (≠ L400), K427 (= K466)
- binding adenosine monophosphate: V231 (≠ I259), S233 (= S261), S238 (= S266), S256 (≠ T284), M257 (≠ V285), G331 (= G360), K427 (= K466), V430 (≠ A469)
- binding magnesium ion: D237 (= D265), D335 (= D364)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ V338), Y332 (≠ Q361), G333 (= G362), I336 (≠ E365), D357 (= D391), E366 (≠ L400), K427 (= K466)
- binding pyrophosphate 2-: S233 (= S261), G235 (= G263), D237 (= D265), S238 (= S266), D335 (= D364), K407 (= K445), K427 (= K466), L428 (≠ K467)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
22% identity, 84% coverage: 72:487/495 of query aligns to 55:453/496 of 1mbzA
- active site: A69 (≠ N86), G70 (≠ A87), D311 (≠ M334), Y337 (≠ Q361), E371 (≠ L400), K432 (= K466)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ I259), L237 (≠ F260), S238 (= S261), S243 (= S266), S261 (≠ T284), M262 (≠ V285), Y315 (≠ V338), L319 (≠ I344), G336 (= G360), Y337 (≠ Q361), G338 (= G362), D340 (= D364), I341 (≠ E365), D362 (= D391), E371 (≠ L400), K432 (= K466), G434 (≠ A468), V435 (≠ A469)
- binding magnesium ion: D242 (= D265), D340 (= D364)
- binding pyrophosphate 2-: S238 (= S261), G240 (= G263), D242 (= D265), S243 (= S266), D340 (= D364), K412 (= K445), K432 (= K466), L433 (≠ K467)
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
26% identity, 40% coverage: 5:201/495 of query aligns to 1:214/455 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
26% identity, 40% coverage: 5:201/495 of query aligns to 12:229/476 of P00497
- C12 (≠ A5) 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 [4Fe-4S] cluster
- 294 binding Mg(2+)
- 356 binding Mg(2+)
- 357 binding Mg(2+)
- 393 binding [4Fe-4S] cluster
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding [4Fe-4S] cluster; C→S: Loss of activity.
- 451 binding [4Fe-4S] cluster; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
26% identity, 40% coverage: 5:201/495 of query aligns to 1:218/465 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
1jgtB Crystal structure of beta-lactam synthetase (see paper)
22% identity, 85% coverage: 72:492/495 of query aligns to 59:466/500 of 1jgtB
- active site: A73 (≠ N86), G74 (≠ A87), D319 (≠ M334), Y345 (≠ Q361), E379 (≠ L400), K440 (= K466)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ I259), L245 (≠ F260), S246 (= S261), G248 (= G263), I249 (≠ L264), D250 (= D265), S251 (= S266), S269 (≠ T284), M270 (≠ V285), L327 (≠ I344), G344 (= G360), Y345 (≠ Q361), D348 (= D364), K420 (= K445), K440 (= K466)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ V338), Y345 (≠ Q361), G346 (= G362), D348 (= D364), I349 (≠ E365), M354 (≠ Y370), D370 (= D391), E379 (≠ L400)
- binding magnesium ion: D250 (= D265), D348 (= D364)
P0AG16 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Escherichia coli (strain K12) (see paper)
26% identity, 40% coverage: 1:198/495 of query aligns to 1:231/505 of P0AG16
- M1 (= M1) modified: Initiator methionine, Removed
- C2 (= C2) active site, Nucleophile
8w7dA Crystal structure of ecppat-fr901483 complex (see paper)
27% identity, 39% coverage: 5:198/495 of query aligns to 1:225/470 of 8w7dA
Sites not aligning to the query:
- binding [(1S,3S,6S,7S,8R,9S)-6-[(4-methoxyphenyl)methyl]-3-(methylamino)-7-oxidanyl-5-azatricyclo[6.3.1.0^1,5]dodecan-9-yl] dihydrogen phosphate: 249, 253, 355, 356, 358, 359, 360, 361, 362, 397
1ecbA Escherichia coli glutamine phosphoribosylpyrophosphate (prpp) amidotransferase complexed with 2 gmp, 1 mg per subunit (see paper)
26% identity, 39% coverage: 5:198/495 of query aligns to 1:230/475 of 1ecbA
Sites not aligning to the query:
- active site: 258, 321, 326, 336, 438
- binding guanosine-5'-monophosphate: 258, 258, 260, 261, 275, 302, 303, 304, 325, 326, 326, 328, 360, 361, 364, 365, 366, 368
- binding magnesium ion: 360, 361
6czfA The structure of e. Coli purf in complex with ppgpp-mg (see paper)
26% identity, 39% coverage: 5:198/495 of query aligns to 1:230/498 of 6czfA
- active site: C1 (≠ A5), G27 (= G31), N101 (= N86), G102 (≠ A87)
- binding guanosine-5',3'-tetraphosphate: R45 (≠ K42), K46 (vs. gap), N48 (vs. gap), R62 (≠ F55), A82 (vs. gap), S83 (vs. gap), E84 (vs. gap)
Sites not aligning to the query:
1ecfB Escherichia coli glutamine phosphoribosylpyrophosphate (prpp) amidotransferase (see paper)
26% identity, 39% coverage: 5:198/495 of query aligns to 1:230/500 of 1ecfB
- active site: C1 (≠ A5), G27 (= G31), N101 (= N86), G102 (≠ A87)
- binding piperazine-n,n'-bis(2-ethanesulfonic acid): R45 (≠ K42), K46 (vs. gap), R62 (≠ F55), E84 (vs. gap), Y89 (vs. gap), V90 (vs. gap), N91 (vs. gap)
Sites not aligning to the query:
- active site: 258, 321, 326, 336, 444
- binding piperazine-n,n'-bis(2-ethanesulfonic acid): 303, 304, 366, 367, 368, 369, 370, 372, 373, 374, 375
6ottA Structure of purf in complex with ppapp (see paper)
26% identity, 39% coverage: 5:198/495 of query aligns to 1:230/496 of 6ottA
Sites not aligning to the query:
1ecjA Escherichia coli glutamine phosphoribosylpyrophosphate (prpp) amidotransferase complexed with 2 amp per tetramer (see paper)
26% identity, 39% coverage: 5:198/495 of query aligns to 1:230/492 of 1ecjA
Sites not aligning to the query:
- active site: 258, 321, 326, 336, 444
- binding adenosine monophosphate: 366, 367, 368, 370, 371, 372, 374
Query Sequence
>WP_013644771.1 NCBI__GCF_000191585.1:WP_013644771.1
MCAIAGILSINGKQALGEDLICMLKTMEHRGPDGSRICLDGKLVTGDLETTDLPFANIGL
GHNLLSIVGTEVSQPLVKHGLVLVANAEIYNYRELKNFYDECYFTDSDCEVILTLVNKYY
KNSLVDAVNTTIKELDGDYAFAISNGKELVVVRDELGVKPVYYATDHKRDLFAFASERKA
LWKLGIKDVNVLKPGEMILNNKTISKPQTKKKTMPIPNVRDGNESFPQYGSNYYKNLLKK
VLIDSVKKRVVGLDRVGIIFSGGLDSSILAKLSKDLEVETFLYTVGTENSSDMKYAKQVA
NSLDLPLKSKIVALDDIKHYTGLVLNAIEEYNVMKIGVGMPSYIASELASQDGIRVMLSG
QGADEIFAGYQRYTQFYQEYGEKTTEYLEADVSNLYHVNLQRDDAVTMANSVELRVPYLD
SKVVNVGLNIPMKYKLGHDPDDLRKCILRRLALDLEVPMEAVLRPKKAAQYGSGIHRLLV
KKVLKDGSYKAQFES
Or try a new SitesBLAST search
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