SitesBLAST
Comparing WP_011606722.1 NCBI__GCF_000058485.1:WP_011606722.1 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 11 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)
28% identity, 88% coverage: 1:539/613 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 (≠ R30) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H83) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H108) mutation to H: Little effect on the kinetic properties.
- E349 (= E383) 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)
28% identity, 88% coverage: 3:539/613 of query aligns to 2:433/497 of 1ct9A
- active site: L50 (= L51), N74 (≠ S77), G75 (= G78), T305 (vs. gap), R308 (vs. gap), E332 (= E383), M366 (≠ G450)
- binding adenosine monophosphate: L232 (= L262), L233 (= L263), S234 (= S264), S239 (= S269), A255 (= A294), V256 (= V295), D263 (= D314), M316 (≠ L368), S330 (= S381), G331 (= G382), E332 (= E383)
- binding glutamine: R49 (= R50), L50 (= L51), I52 (≠ V53), V53 (≠ I54), N74 (≠ S77), G75 (= G78), E76 (= E79), D98 (= D102)
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, 88% coverage: 1:539/613 of query aligns to 1:468/557 of P78753
- S391 (≠ T467) 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)
26% identity, 65% coverage: 1:397/613 of query aligns to 1:379/561 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 (≠ V8) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ G212) to E: in dbSNP:rs1049674
- F362 (≠ L380) 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)
25% identity, 65% coverage: 2:397/613 of query aligns to 1:366/509 of 6gq3A
- active site: W4 (= W7), L49 (= L51), N74 (≠ S77), G75 (= G78), T324 (≠ G357), R327 (≠ D360)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (= V53), V52 (≠ I54), Y73 (= Y76), N74 (≠ S77), G75 (= G78), E76 (= E79), V95 (≠ S101), D96 (= D102)
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
33% identity, 20% coverage: 45:167/613 of query aligns to 68:199/460 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
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)
33% identity, 20% coverage: 45:167/613 of query aligns to 154:285/561 of Q9STG9
- H187 (≠ Y76) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K147) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P148) 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.
1mb9A Beta-lactam synthetase complexed with atp (see paper)
31% identity, 47% coverage: 69:357/613 of query aligns to 62:343/485 of 1mb9A
- active site: A70 (≠ S77), G71 (= G78), D310 (= D328), Y336 (≠ A350)
- binding adenosine monophosphate: V235 (≠ L262), L236 (= L263), S242 (= S269), S260 (= S292), M261 (≠ F293), Y314 (≠ V332), L318 (≠ H337), G335 (≠ V349), Y336 (≠ A350)
- binding adenosine-5'-triphosphate: V235 (≠ L262), L236 (= L263), S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), S260 (= S292), M261 (≠ F293), L318 (≠ H337), G335 (≠ V349), D339 (= D353)
- binding magnesium ion: D241 (= D268), D339 (= D353)
- binding pyrophosphate 2-: S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), D339 (= D353)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
31% identity, 47% coverage: 69:357/613 of query aligns to 65:352/500 of 1jgtB
- active site: A73 (≠ S77), G74 (= G78), D319 (= D328), Y345 (≠ A350)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L262), L245 (= L263), S246 (= S264), G248 (= G266), I249 (≠ L267), D250 (= D268), S251 (= S269), S269 (= S292), M270 (≠ F293), L327 (≠ H337), G344 (≠ V349), Y345 (≠ A350), D348 (= D353)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ V332), Y345 (≠ A350), G346 (≠ A351), D348 (= D353), I349 (≠ S354)
- binding magnesium ion: D250 (= D268), D348 (= D353)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
32% identity, 47% coverage: 69:357/613 of query aligns to 61:344/496 of 1mbzA
- active site: A69 (≠ S77), G70 (= G78), D311 (= D328), Y337 (≠ A350)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L262), L237 (= L263), S238 (= S264), S243 (= S269), S261 (= S292), M262 (≠ F293), Y315 (≠ V332), L319 (≠ H337), G336 (≠ V349), Y337 (≠ A350), G338 (≠ A351), D340 (= D353), I341 (≠ S354)
- binding magnesium ion: D242 (= D268), D340 (= D353)
- binding pyrophosphate 2-: S238 (= S264), G240 (= G266), D242 (= D268), S243 (= S269), D340 (= D353)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
31% identity, 47% coverage: 69:357/613 of query aligns to 57:339/491 of 1mc1A
- active site: A65 (≠ S77), G66 (= G78), D306 (= D328), Y332 (≠ A350)
- binding adenosine monophosphate: V231 (≠ L262), S233 (= S264), S238 (= S269), S256 (= S292), M257 (≠ F293), G331 (≠ V349)
- binding magnesium ion: D237 (= D268), D335 (= D353)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ V332), Y332 (≠ A350), G333 (≠ A351), I336 (≠ S354)
- binding pyrophosphate 2-: S233 (= S264), G235 (= G266), D237 (= D268), S238 (= S269), D335 (= D353)
Sites not aligning to the query:
Query Sequence
>WP_011606722.1 NCBI__GCF_000058485.1:WP_011606722.1
MCGITGWVSFGQDDYEQKTVIEAMTATLRRRGPDAGGTWVGAHAAIGHRRLAVIDLVGGV
QPMVSDQDGAETVLTYSGEIYNHHELRGELVRRGHTLRTRSDTEVVLHAYLEWGDLLVDR
LEGMYAFAVWDERAGRLLLVRDRLGVKPLFYAEIPGGVVFGSEPKALFCHPLVRPRVNAD
GLREAYSLLFNTGPTVWTGVRELAPGALATFGPHGLTERTYWALDAAAMAAVSPQAAVEQ
VRVHLERATAAQLEADVPLCSLLSGGLDSTVLTALLADELRRREGPHARIRSFAVDYSDQ
AVQFTGDVLRTGHDAPYAVEASRYIGTDHSTVVLDPHTLLDPEHRLAVVAARDSPIGVGD
MDTSLYVLFGKIAQSSTVALSGEAADEVFGGYPWFHSPAALSAPTFPWLLVTGDEAAMPL
HPDLAATLRIEEFRADTYRDALAAVPHLDGEDPTEHRQREMAHLSLTRWLRQLLHRKDRL
SMAQGIEVRVPYCDHRLVEYAFGVPWAVRSFDGREKSLLRAAGAGRCPESVLIREKNHYP
TTHHPDYNRGLQAMALDALDAHGGRVRDLADVSRLRPLIDGPPERLEWGQRLSLERVVDL
ALWLDHHHPELTL
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