SitesBLAST
Comparing WP_012469560.1 NCBI__GCF_000020385.1:WP_012469560.1 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 8 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
30% identity, 58% coverage: 22:375/614 of query aligns to 22:344/497 of 1ct9A
- active site: L50 (= L50), N74 (= N74), G75 (= G75), T305 (≠ G339), R308 (≠ L342), E332 (≠ Q363)
- binding adenosine monophosphate: L232 (≠ Y261), L233 (= L262), S234 (= S263), S239 (= S268), A255 (≠ T286), V256 (≠ F287), D263 (≠ R294), M316 (≠ V348), S330 (≠ G361), G331 (= G362), E332 (≠ Q363)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ I53), N74 (= N74), G75 (= G75), E76 (= E76), D98 (= D99)
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)
29% identity, 61% coverage: 1:377/614 of query aligns to 1:370/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 489 modified: Phosphoserine
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
29% identity, 61% coverage: 1:375/614 of query aligns to 1:361/554 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 (≠ Y80) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A105) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q363) 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.
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
27% identity, 57% coverage: 27:375/614 of query aligns to 23:364/509 of 6gq3A
- active site: L49 (= L50), N74 (= N74), G75 (= G75), T324 (≠ G339), R327 (vs. gap)
- binding 5-oxo-l-norleucine: R48 (= R49), V51 (≠ I52), V52 (≠ I53), Y73 (≠ F73), N74 (= N74), G75 (= G75), E76 (= E76), V95 (≠ S98), D96 (= D99)
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, 61% coverage: 1:375/614 of query aligns to 1:377/561 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 (= V225) to E: in dbSNP:rs1049674
- F362 (≠ L360) 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
1jgtB Crystal structure of beta-lactam synthetase (see paper)
25% identity, 56% coverage: 60:405/614 of query aligns to 49:387/500 of 1jgtB
- active site: A73 (≠ N74), G74 (= G75), D319 (≠ E337), Y345 (≠ Q363), E379 (≠ K397)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ Y261), L245 (= L262), S246 (= S263), G248 (= G265), I249 (= I266), D250 (= D267), S251 (= S268), S269 (= S283), M270 (≠ T284), L327 (≠ Q345), G344 (= G362), Y345 (≠ Q363), D348 (= D366)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ S341), Y345 (≠ Q363), G346 (= G364), D348 (= D366), I349 (≠ E367), M354 (≠ Y372), D370 (≠ S388), E379 (≠ K397)
- binding magnesium ion: D250 (= D267), D348 (= D366)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
25% identity, 56% coverage: 60:405/614 of query aligns to 45:379/496 of 1mbzA
- active site: A69 (≠ N74), G70 (= G75), D311 (≠ E337), Y337 (≠ Q363), E371 (≠ K397)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ Y261), L237 (= L262), S238 (= S263), S243 (= S268), S261 (= S283), M262 (≠ T284), Y315 (≠ S341), L319 (≠ Q345), G336 (= G362), Y337 (≠ Q363), G338 (= G364), D340 (= D366), I341 (≠ E367), D362 (≠ S388), E371 (≠ K397)
- binding magnesium ion: D242 (= D267), D340 (= D366)
- binding pyrophosphate 2-: S238 (= S263), G240 (= G265), D242 (= D267), S243 (= S268), D340 (= D366)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
25% identity, 56% coverage: 60:405/614 of query aligns to 41:374/491 of 1mc1A
- active site: A65 (≠ N74), G66 (= G75), D306 (≠ E337), Y332 (≠ Q363), E366 (≠ K397)
- binding adenosine monophosphate: V231 (≠ Y261), S233 (= S263), S238 (= S268), S256 (= S283), M257 (≠ T284), G331 (= G362)
- binding magnesium ion: D237 (= D267), D335 (= D366)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ S341), Y332 (≠ Q363), G333 (= G364), I336 (≠ E367), D357 (≠ S388), E366 (≠ K397)
- binding pyrophosphate 2-: S233 (= S263), G235 (= G265), D237 (= D267), S238 (= S268), D335 (= D366)
Sites not aligning to the query:
Query Sequence
>WP_012469560.1 NCBI__GCF_000020385.1:WP_012469560.1
MCGIAGIVYRNKKSNHSEQIAEMLKLIHHRGPDGMGVFEAENVVLGHRRLAIIDLSPSGH
QPMCYLDRFIITFNGEIYNYLELKEELSNKGYYFISTSDTEVILAAYAEWGEDCVTHLNG
MFAFGLYDLLERTLFLARDRVGEKPLYYSKNENEFFFFSEPKQVISSGIIEGIPNEVAIR
QYLEYQFTLSAQTFFTGIYKLLPGHCATLRNGVFKSREYWSLADVEVDYSISYAEAKLRI
KNLVEDSLKIRLRSDVPVASYLSGGIDSTIIATSAAKELSSLSTYTFTSKKYPRFDESQN
ARLTADLIHADHHEIEIENADTLSLWQNSTYFMDEPEVGYSLLSQMAVSREVAKQTKVVL
GGQGGDELFFGYAWYSNLLLKSFLSFSSVADFKLLDKVKVVISFLLNSPKRTALRLIFDS
FKSFGRPLSEIYIDTWRGYGCFSLLQDIKIKEGANSPVSGCLKLSELKKFEFNYWLHGLL
HVEDRSSMAHSLESRVPLLDHRLVEFVFSLPPHFMIDGVLNKKIFIDAFSDILPNHVKNN
KQKMGYVSPIHSWLSDQHVTAFIKDVISNKSSFIYHFVDYYKMKSLQINDRQLWMLISLE
IWHNIFIKRDIKSC
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