SitesBLAST
Comparing WP_012043792.1 NCBI__GCF_000015165.1:WP_012043792.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
31% identity, 54% coverage: 25:371/647 of query aligns to 26:341/497 of 1ct9A
- active site: L50 (= L51), N74 (= N75), G75 (= G76), T305 (≠ N337), R308 (vs. gap), E332 (= E362)
- binding adenosine monophosphate: L232 (≠ Y259), L233 (= L260), S234 (= S261), S239 (= S266), A255 (≠ T285), V256 (≠ I286), D263 (≠ E295), M316 (≠ L346), S330 (≠ T360), G331 (= G361), E332 (= E362)
- binding glutamine: R49 (= R50), L50 (= L51), I52 (= I53), V53 (≠ I54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D100)
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, 57% coverage: 1:371/647 of query aligns to 1:358/554 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 (= H28) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D32) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ W106) mutation to H: Little effect on the kinetic properties.
- E349 (= E362) 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)
30% identity, 58% coverage: 1:375/647 of query aligns to 1:374/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 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)
25% identity, 57% coverage: 1:371/647 of query aligns to 1:374/561 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 (≠ A219) to E: in dbSNP:rs1049674
- F362 (≠ L359) 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)
26% identity, 53% coverage: 28:371/647 of query aligns to 25:361/509 of 6gq3A
- active site: L49 (= L51), N74 (= N75), G75 (= G76), T324 (≠ A334), R327 (≠ N337)
- binding 5-oxo-l-norleucine: R48 (= R50), V51 (≠ I53), V52 (≠ I54), Y73 (≠ V74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S99), D96 (= D100)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 58% coverage: 73:445/647 of query aligns to 67:413/496 of 1mbzA
- active site: A69 (≠ N75), G70 (= G76), D311 (≠ H339), Y337 (≠ E362), E371 (≠ Q402)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ Y259), L237 (= L260), S238 (= S261), S243 (= S266), S261 (≠ A287), M262 (≠ Y288), Y315 (≠ K343), L319 (vs. gap), G336 (= G361), Y337 (≠ E362), G338 (= G363), D340 (= D365), I341 (≠ E366), D362 (= D393), E371 (≠ Q402)
- binding magnesium ion: D242 (= D265), D340 (= D365)
- binding pyrophosphate 2-: S238 (= S261), G240 (= G263), D242 (= D265), S243 (= S266), D340 (= D365), K412 (≠ A444)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 60% coverage: 73:458/647 of query aligns to 68:438/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (≠ H339), Y336 (≠ E362), E370 (≠ Q402), K431 (≠ L451)
- binding adenosine monophosphate: V235 (≠ Y259), L236 (= L260), S242 (= S266), S260 (≠ A287), M261 (≠ Y288), Y314 (≠ K343), L318 (vs. gap), G335 (= G361), Y336 (≠ E362)
- binding adenosine-5'-triphosphate: V235 (≠ Y259), L236 (= L260), S237 (= S261), G239 (= G263), D241 (= D265), S242 (= S266), S260 (≠ A287), M261 (≠ Y288), L318 (vs. gap), G335 (= G361), D339 (= D365), K411 (≠ A444), K431 (≠ L451)
- binding magnesium ion: D241 (= D265), D339 (= D365)
- binding pyrophosphate 2-: S237 (= S261), G239 (= G263), D241 (= D265), S242 (= S266), D339 (= D365), K411 (≠ A444), K431 (≠ L451)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 58% coverage: 73:445/647 of query aligns to 71:421/500 of 1jgtB
- active site: A73 (≠ N75), G74 (= G76), D319 (≠ H339), Y345 (≠ E362), E379 (≠ Q402)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ Y259), L245 (= L260), S246 (= S261), G248 (= G263), I249 (= I264), D250 (= D265), S251 (= S266), S269 (≠ A287), M270 (≠ Y288), L327 (≠ S347), G344 (= G361), Y345 (≠ E362), D348 (= D365), K420 (≠ A444)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ K343), Y345 (≠ E362), G346 (= G363), D348 (= D365), I349 (≠ E366), M354 (≠ Y371), D370 (= D393), E379 (≠ Q402)
- binding magnesium ion: D250 (= D265), D348 (= D365)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 58% coverage: 73:445/647 of query aligns to 63:408/491 of 1mc1A
- active site: A65 (≠ N75), G66 (= G76), D306 (≠ H339), Y332 (≠ E362), E366 (≠ Q402)
- binding adenosine monophosphate: V231 (≠ Y259), S233 (= S261), S238 (= S266), S256 (≠ A287), M257 (≠ Y288), G331 (= G361)
- binding magnesium ion: D237 (= D265), D335 (= D365)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ K343), Y332 (≠ E362), G333 (= G363), I336 (≠ E366), D357 (= D393), E366 (≠ Q402)
- binding pyrophosphate 2-: S233 (= S261), G235 (= G263), D237 (= D265), S238 (= S266), D335 (= D365), K407 (≠ A444)
Sites not aligning to the query:
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
28% identity, 25% coverage: 2:165/647 of query aligns to 1:199/460 of 6lbpA
Sites not aligning to the query:
- active site: 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 25% coverage: 2:165/647 of query aligns to 87:285/561 of Q9STG9
- H187 (≠ V74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K145) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P146) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
Sites not aligning to the query:
- 371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
- 476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
- 494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
28% identity, 27% coverage: 2:177/647 of query aligns to 1:206/455 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)
28% identity, 27% coverage: 2:177/647 of query aligns to 12:221/476 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)
28% identity, 27% coverage: 2:177/647 of query aligns to 1:210/465 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
Query Sequence
>WP_012043792.1 NCBI__GCF_000015165.1:WP_012043792.1
MCGLAGVWCWDTPIDRPAIARALGLLDHRGPDGNGLWISEDGKVALGHTRLSIIDLVTGE
QPLSHPNGKLQLVVNGEFYDYERIRNDLTARGARFRTRSDSEIALWLYDESGTRCFADLN
GEFAFILWDAGAGRLIAARDRFGIKPLFYAVQSGRILLASEIKALLAMGVPAQWDVEGYL
DAAHVLQNGTLFSGIRQVPPGCYLSATRHGITIQRYWDAPFASALSPIEDEHGALDQIRA
QMSRATRWRMRADVPVAAYLSGGIDSMSVLALAAATTNRAPDAFTIAYEDAAYDESHRAE
SFATQLGTRFHRVPVNGAALADHFATSLWHSETACFNPHGTAKFILSKAVRDAGYKVVLT
GEGADEIFAGYAPSRVDALGGSAAMQAMIATRDRATYAVTPQHTATDQLPLIAQRFGTVP
TWLRHQMAHLLGVADLLRDDLRTAWSTDRPLAAFLKYLEPWTVPALDTVDLGIALMLKTT
LPNYVLVTLGDRMEMAHSIEGRLPFLDHQVVELAWRLPSHLKIRDGVEKFALRQAMRNLL
PADAVDRQKHPFIAPPTATDAKHPFGAMIRDVLHGPALAALPFFEPRKVRKLIDRLTSLP
PEDRLRLEPLLVEIASLCIIHDLFKMSSSSDPSAQLSIQMPSTEALA
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