SitesBLAST
Comparing WP_010959890.1 NCBI__GCF_000008325.1:WP_010959890.1 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 15 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)
33% identity, 63% coverage: 1:379/606 of query aligns to 1:365/554 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 (≠ F79) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H104) mutation to H: Little effect on the kinetic properties.
- E349 (= E363) 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)
34% identity, 62% coverage: 3:379/606 of query aligns to 2:348/497 of 1ct9A
- active site: L50 (= L49), N74 (= N73), G75 (= G74), T305 (≠ M337), R308 (≠ N340), E332 (= E363)
- binding adenosine monophosphate: L232 (≠ F260), L233 (= L261), S234 (= S262), S239 (= S267), A255 (≠ S286), V256 (= V287), D263 (≠ E297), M316 (≠ L348), S330 (= S361), G331 (= G362), E332 (= E363)
- binding glutamine: R49 (= R48), L50 (= L49), I52 (= I51), V53 (≠ I52), N74 (= N73), G75 (= G74), E76 (= E75), D98 (= D98)
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)
30% identity, 64% coverage: 1:386/606 of query aligns to 1:379/557 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)
28% identity, 63% coverage: 1:379/606 of query aligns to 1:381/561 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 (= F360) 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)
29% identity, 62% coverage: 2:379/606 of query aligns to 1:368/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L49), N74 (= N73), G75 (= G74), T324 (≠ M337), R327 (≠ N340)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R48), V51 (≠ I51), V52 (≠ I52), Y73 (≠ A72), N74 (= N73), G75 (= G74), E76 (= E75), V95 (≠ S97), D96 (= D98)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
29% identity, 52% coverage: 58:374/606 of query aligns to 49:356/500 of 1jgtB
- active site: A73 (≠ N73), G74 (= G74), D319 (= D339), Y345 (≠ E363)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F260), L245 (= L261), S246 (= S262), G248 (= G264), I249 (≠ V265), D250 (= D266), S251 (= S267), S269 (= S286), M270 (≠ V287), L327 (≠ T345), G344 (= G362), Y345 (≠ E363), D348 (= D366)
- binding n2-(carboxyethyl)-l-arginine: Y323 (vs. gap), Y345 (≠ E363), G346 (= G364), D348 (= D366), I349 (≠ E367), M354 (≠ Y372)
- binding magnesium ion: D250 (= D266), D348 (= D366)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 52% coverage: 58:374/606 of query aligns to 46:347/485 of 1mb9A
- active site: A70 (≠ N73), G71 (= G74), D310 (= D339), Y336 (≠ E363)
- binding adenosine monophosphate: V235 (≠ F260), L236 (= L261), S242 (= S267), S260 (= S286), M261 (≠ V287), Y314 (vs. gap), L318 (≠ T345), G335 (= G362), Y336 (≠ E363)
- binding adenosine-5'-triphosphate: V235 (≠ F260), L236 (= L261), S237 (= S262), G239 (= G264), D241 (= D266), S242 (= S267), S260 (= S286), M261 (≠ V287), L318 (≠ T345), G335 (= G362), D339 (= D366)
- binding magnesium ion: D241 (= D266), D339 (= D366)
- binding pyrophosphate 2-: S237 (= S262), G239 (= G264), D241 (= D266), S242 (= S267), D339 (= D366)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
29% identity, 52% coverage: 58:374/606 of query aligns to 41:343/491 of 1mc1A
- active site: A65 (≠ N73), G66 (= G74), D306 (= D339), Y332 (≠ E363)
- binding adenosine monophosphate: V231 (≠ F260), S233 (= S262), S238 (= S267), S256 (= S286), M257 (≠ V287), G331 (= G362)
- binding magnesium ion: D237 (= D266), D335 (= D366)
- binding deoxyguanidinoproclavaminic acid: Y310 (vs. gap), Y332 (≠ E363), G333 (= G364), I336 (≠ E367)
- binding pyrophosphate 2-: S233 (= S262), G235 (= G264), D237 (= D266), S238 (= S267), D335 (= D366)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
29% identity, 52% coverage: 58:374/606 of query aligns to 45:348/496 of 1mbzA
- active site: A69 (≠ N73), G70 (= G74), D311 (= D339), Y337 (≠ E363)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F260), L237 (= L261), S238 (= S262), S243 (= S267), S261 (= S286), M262 (≠ V287), Y315 (vs. gap), L319 (≠ T345), G336 (= G362), Y337 (≠ E363), G338 (= G364), D340 (= D366), I341 (≠ E367)
- binding magnesium ion: D242 (= D266), D340 (= D366)
- binding pyrophosphate 2-: S238 (= S262), G240 (= G264), D242 (= D266), S243 (= S267), D340 (= D366)
Sites not aligning to the query:
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)
32% identity, 21% coverage: 38:163/606 of query aligns to 149:285/561 of Q9STG9
- H187 (≠ A72) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K143) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P144) 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.
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
32% identity, 21% coverage: 38:163/606 of query aligns to 63:199/460 of 6lbpA
Sites not aligning to the query:
- active site: 1, 27, 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
28% identity, 30% coverage: 38:217/606 of query aligns to 62:227/465 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
28% identity, 30% coverage: 38:217/606 of query aligns to 73:238/476 of P00497
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 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.
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
28% identity, 30% coverage: 38:217/606 of query aligns to 62:223/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 27, 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 25, 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
Q27601 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPAT; Phosphoribosylamidotransferase; PRAT; EC 2.4.2.14 from Drosophila melanogaster (Fruit fly) (see paper)
31% identity, 19% coverage: 32:149/606 of query aligns to 118:252/546 of Q27601
- S120 (≠ R34) modified: Phosphoserine
Sites not aligning to the query:
- 113 modified: Phosphoserine
- 114 modified: Phosphothreonine
Query Sequence
>WP_010959890.1 NCBI__GCF_000008325.1:WP_010959890.1
MCGIAGLFNCNLPADELRLDQAVAKLTHRGPDDRGIFLDGRFGMGHTRLSIIDLAGGHQP
LFSEDRRLALIANGEIYNFIELRSELTAAGFRFQTQSDSEVILHAYLAFGEGFLERIQGM
FAFALYDALEGRLILARDRLGIKPLFLARRPDGIAFASEIKALLPLLDQPREIDPQGLAQ
YFQNQFSTGATTVLRGVERVLPGEAVVVEAGKTTRRFRYWSPLAVRTEELDFDEAAARFD
ALMERVMVEHMRSDVPFGLFLSGGVDSSLLLALLTRYSGEPIRTFSVGFPGTSLTDELPL
AEGLARRFRSRHREIRPGPQDILHSLPLTVWAADDLMRDNASLPTSLLARAAGEELKVVF
SGEGGDEVFAGYGRYRTSPLERLFKSLLAPGSGGFRTRGSFRGRWPKTLFGPALLAAAQS
ARRPVQESWRETPREWSDLQRMQYVDLCHALPDNLLVKADRMLMAWGVEGRVPFLDHRVV
EFGLSLPDRLKIEGRQGKLFLKRWGERLVPAEQLYARKRGFHVPLGEWLDEPFLERLNRI
LPEHPALTPWFKPAGIRALIARCRDERQGSAMLWAIIQFAIWHRLFISGNGERPEALTDP
LEILQR
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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