SitesBLAST
Comparing WP_055067462.1 NCBI__GCF_001406815.1:WP_055067462.1 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 13 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)
27% identity, 87% coverage: 1:537/615 of query aligns to 1:453/554 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 (= H34) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D38) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H87) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ C112) mutation to H: Little effect on the kinetic properties.
- E349 (= E382) 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)
27% identity, 83% coverage: 26:537/615 of query aligns to 21:433/497 of 1ct9A
- active site: L50 (= L55), N74 (= N81), G75 (= G82), T305 (= T358), R308 (≠ D361), E332 (= E382), M366 (≠ E430)
- binding adenosine monophosphate: L232 (≠ F267), L233 (= L268), S234 (= S269), S239 (= S274), A255 (≠ S296), V256 (≠ F297), D263 (= D316), M316 (≠ C368), S330 (≠ T380), G331 (= G381), E332 (= E382)
- binding glutamine: R49 (= R54), L50 (= L55), I52 (= I57), V53 (≠ R58), N74 (= N81), G75 (= G82), E76 (= E83), D98 (= D106)
Sites not aligning to the query:
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)
26% identity, 82% coverage: 32:537/615 of query aligns to 24:470/561 of P08243
- V210 (≠ L230) to E: in dbSNP:rs1049674
- F362 (≠ L379) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
Sites not aligning to the query:
- 2 active site, For GATase activity; C→A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- 6 A → E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- 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, 81% coverage: 32:532/615 of query aligns to 23:452/509 of 6gq3A
- active site: L49 (= L55), N74 (= N81), G75 (= G82), T324 (= T358), R327 (≠ D361)
- binding 5-oxo-l-norleucine: R48 (= R54), V51 (≠ I57), V52 (≠ R58), Y73 (= Y80), N74 (= N81), G75 (= G82), E76 (= E83), V95 (≠ S105), D96 (= D106)
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)
27% identity, 83% coverage: 26:537/615 of query aligns to 22:468/557 of P78753
- S391 (≠ D447) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
1jgtB Crystal structure of beta-lactam synthetase (see paper)
24% identity, 53% coverage: 65:390/615 of query aligns to 57:353/500 of 1jgtB
- active site: A73 (≠ N81), G74 (= G82), D319 (≠ G356), Y345 (≠ E382)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F267), L245 (= L268), S246 (= S269), G248 (= G271), I249 (= I272), D250 (= D273), S251 (= S274), S269 (= S296), M270 (≠ F297), L327 (= L364), G344 (= G381), Y345 (≠ E382), D348 (= D385)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ V360), Y345 (≠ E382), G346 (≠ C383), D348 (= D385), I349 (≠ E386)
- binding magnesium ion: D250 (= D273), D348 (= D385)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
24% identity, 53% coverage: 65:390/615 of query aligns to 53:345/496 of 1mbzA
- active site: A69 (≠ N81), G70 (= G82), D311 (≠ G356), Y337 (≠ E382)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F267), L237 (= L268), S238 (= S269), S243 (= S274), S261 (= S296), M262 (≠ F297), Y315 (≠ V360), L319 (= L364), G336 (= G381), Y337 (≠ E382), G338 (≠ C383), D340 (= D385), I341 (≠ E386)
- binding magnesium ion: D242 (= D273), D340 (= D385)
- binding pyrophosphate 2-: S238 (= S269), G240 (= G271), D242 (= D273), S243 (= S274), D340 (= D385)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
24% identity, 53% coverage: 65:390/615 of query aligns to 49:340/491 of 1mc1A
- active site: A65 (≠ N81), G66 (= G82), D306 (≠ G356), Y332 (≠ E382)
- binding adenosine monophosphate: V231 (≠ F267), S233 (= S269), S238 (= S274), S256 (= S296), M257 (≠ F297), G331 (= G381)
- binding magnesium ion: D237 (= D273), D335 (= D385)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ V360), Y332 (≠ E382), G333 (≠ C383), I336 (≠ E386)
- binding pyrophosphate 2-: S233 (= S269), G235 (= G271), D237 (= D273), S238 (= S274), D335 (= D385)
Sites not aligning to the query:
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
29% identity, 17% coverage: 64:170/615 of query aligns to 80:193/455 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
29% identity, 17% coverage: 64:170/615 of query aligns to 95:208/476 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.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
29% identity, 17% coverage: 64:170/615 of query aligns to 84:197/465 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
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)
27% identity, 20% coverage: 48:171/615 of query aligns to 153:285/561 of Q9STG9
- H187 (≠ Y80) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K151) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P152) 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)
27% identity, 20% coverage: 48:171/615 of query aligns to 67:199/460 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
Query Sequence
>WP_055067462.1 NCBI__GCF_001406815.1:WP_055067462.1
MCGISGFCDFSLNYYDKKTFWETILVQMHETLKHRGPDQAMIDLQPHVGLSHARLSIRDL
KSGIQPMTRTFHGKTCSIVYNGEIYNHRELLPELQAAGYRFTTTSDTEIILCAYMHFGKN
FVEKLNGIFAFAIWDDTTRELLLYRDRAGTKPLFYTQTGSSFVFGSEPKALFCHPDVTPS
IDKNSLQEILAVGPARTYGNGVFTGVKEVMPGHYHIFCPDGQHDILYWDLPCREHKDSYA
QTVQTVSFLVRDTVERQMVSDVPVCTFLSGGIDSSIVTALAARHMQKEGKILNTFSFDFS
ENEKYFKSNAFQPERDLPYVNRMLQYCKTSHTYLECSQEALFAALSDAVTAKDLPGMTDV
DASLLYFCSEVAKHNKVTLTGECADEIFGGYPWFYRPELMNRDGFPWSADPAARTSILSD
DVLRTLDLAEYSHARYEETLSHVPHLDGESPEEARRRDIGYLNIKWFMQTLLDRMDRTSM
YSSLEARVPFADHRIMEYVFNVPWQMKYRNGVEKSLLRDACADLLPRELLWRKKSPYPKT
YHPAYEQMLIRRMREILNDPNSPVLPLLDRSKTEAFLAAPKELGKPWFGQLMAGPQLIAY
FIQINTWMQIYHLSI
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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