SitesBLAST
Comparing WP_012504711.1 NCBI__GCF_000020625.1:WP_012504711.1 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 12 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
28% identity, 89% coverage: 26:550/592 of query aligns to 26:457/497 of 1ct9A
- active site: L50 (= L50), N74 (= N75), G75 (= G76), T305 (≠ I351), R308 (vs. gap), E332 (≠ Q371), M366 (≠ L453)
- binding adenosine monophosphate: L232 (= L266), L233 (= L267), S234 (= S268), S239 (= S273), A255 (≠ S292), V256 (= V293), D263 (≠ E305), M316 (≠ L356), S330 (= S369), G331 (= G370), E332 (≠ Q371)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ I53), N74 (= N75), G75 (= G76), E76 (≠ A77), 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)
27% identity, 93% coverage: 1:550/592 of query aligns to 1:477/554 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 (≠ P29) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K106) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q371) 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, 81% coverage: 27:505/592 of query aligns to 28:443/557 of P78753
- S391 (≠ D448) 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)
28% identity, 88% coverage: 1:522/592 of query aligns to 1:470/561 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 (≠ Q224) to E: in dbSNP:rs1049674
- F362 (≠ Q368) 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)
27% identity, 83% coverage: 30:518/592 of query aligns to 26:453/509 of 6gq3A
- active site: L49 (= L50), N74 (= N75), G75 (= G76), T324 (vs. gap), R327 (vs. gap)
- binding 5-oxo-l-norleucine: R48 (= R49), V51 (≠ I52), V52 (≠ I53), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (≠ A77), V95 (≠ S99), D96 (= D100)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 56% coverage: 73:401/592 of query aligns to 63:364/491 of 1mc1A
- active site: A65 (≠ N75), G66 (= G76), D306 (= D349), Y332 (≠ Q371)
- binding adenosine monophosphate: V231 (≠ L266), S233 (= S268), S238 (= S273), S256 (= S292), M257 (≠ V293), G331 (= G370)
- binding magnesium ion: D237 (= D272), D335 (= D374)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ F353), Y332 (≠ Q371), G333 (= G372), I336 (≠ E375), D357 (≠ A394)
- binding pyrophosphate 2-: S233 (= S268), G235 (= G270), D237 (= D272), S238 (= S273), D335 (= D374)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 56% coverage: 73:401/592 of query aligns to 67:369/496 of 1mbzA
- active site: A69 (≠ N75), G70 (= G76), D311 (= D349), Y337 (≠ Q371)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L266), L237 (= L267), S238 (= S268), S243 (= S273), S261 (= S292), M262 (≠ V293), Y315 (≠ F353), L319 (vs. gap), G336 (= G370), Y337 (≠ Q371), G338 (= G372), D340 (= D374), I341 (≠ E375), D362 (≠ A394)
- binding magnesium ion: D242 (= D272), D340 (= D374)
- binding pyrophosphate 2-: S238 (= S268), G240 (= G270), D242 (= D272), S243 (= S273), D340 (= D374)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 56% coverage: 73:401/592 of query aligns to 68:368/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (= D349), Y336 (≠ Q371)
- binding adenosine monophosphate: V235 (≠ L266), L236 (= L267), S242 (= S273), S260 (= S292), M261 (≠ V293), Y314 (≠ F353), L318 (vs. gap), G335 (= G370), Y336 (≠ Q371)
- binding adenosine-5'-triphosphate: V235 (≠ L266), L236 (= L267), S237 (= S268), G239 (= G270), D241 (= D272), S242 (= S273), S260 (= S292), M261 (≠ V293), L318 (vs. gap), G335 (= G370), D339 (= D374)
- binding magnesium ion: D241 (= D272), D339 (= D374)
- binding pyrophosphate 2-: S237 (= S268), G239 (= G270), D241 (= D272), S242 (= S273), D339 (= D374)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
26% identity, 56% coverage: 73:401/592 of query aligns to 71:377/500 of 1jgtB
- active site: A73 (≠ N75), G74 (= G76), D319 (= D349), Y345 (≠ Q371)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L266), L245 (= L267), S246 (= S268), G248 (= G270), I249 (≠ L271), D250 (= D272), S251 (= S273), S269 (= S292), M270 (≠ V293), L327 (vs. gap), G344 (= G370), Y345 (≠ Q371), D348 (= D374)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ F353), Y345 (≠ Q371), G346 (= G372), D348 (= D374), I349 (≠ E375), M354 (≠ Y380), D370 (≠ A394)
- binding magnesium ion: D250 (= D272), D348 (= D374)
Sites not aligning to the query:
Q9XB61 Carbapenam-3-carboxylate synthase; Carbapenam-3-carboxylate ligase; EC 6.3.3.6 from Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) (see 3 papers)
23% identity, 51% coverage: 76:379/592 of query aligns to 57:353/503 of Q9XB61
- 244:251 (vs. 266:273, 88% identical) binding
- I270 (≠ V293) binding
- GYGSD 344:348 (≠ GQGAD 370:374) binding
- Y345 (≠ Q371) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G372) binding
Sites not aligning to the query:
- 371 binding
- 374 binding
- 380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
- 421 binding
- 443 mutation K->A,M: Loss of activity.
- 444:446 binding
1q19A Carbapenam synthetase (see paper)
23% identity, 51% coverage: 76:379/592 of query aligns to 56:352/500 of 1q19A
- active site: G56 (= G76), L318 (≠ M345), E321 (≠ H348), Y344 (≠ Q371)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L266), L244 (= L267), S245 (= S268), D249 (= D272), S250 (= S273), S268 (= S292), I269 (≠ V293), T342 (≠ S369), G343 (= G370), D347 (= D374)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q371), G345 (= G372), L348 (≠ E375)
Sites not aligning to the query:
P14742 Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; GFAT; D-fructose-6-phosphate amidotransferase; Hexosephosphate aminotransferase; EC 2.6.1.16 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
54% identity, 7% coverage: 70:108/592 of query aligns to 110:148/717 of P14742
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 active site, For GATase activity
Query Sequence
>WP_012504711.1 NCBI__GCF_000020625.1:WP_012504711.1
MCGIAGELRFDSAAASSTTVDAMLGILEPRGPDAQGVFAHNRICFGHRRLKIIDLSDCAS
QPMVDSALGLVLVFNGAVYNYRELCTELVGKGYSFFSQSDTEIIIKAYHAWGEDCVGHLQ
GMFAFAIWERDTGRTFFARDRLGIKPLYFTEDNASMRFASSLPALLKSGAVDTAIDPAAL
DCYMSFHSVVPAPWTIFRGIRKLPPATTMMVEPDGRKQQRTYWQPDYSRSDEERRRSAGE
WIDAVHDALKLAVQRRLVADVPVGVLLSGGLDSSLVVGLLSELVQRHLSTFSVGFEDVAE
EEGNEFRYSDIIAERYSTDHHKIFVDHRELQTHLSDCVRAMSEPMVSHDVIGFYLLSREV
SQHVRVVQSGQGADEVFAGYHWYPPMMNTPPTEAYSTYSGVFFDRDFNEYRQAVNSSFIT
EDHAAAFVRNHFAMPGAEEPIDKALRLDSTIMLVDDPVKRVDNMTMAWGLEARVPFLDHE
LVELAAKIPAEYKVKDGGKYVLKEVGRRIIPHEVIDRPKGYFPVPALKYLEGEYLDMAKN
ILNQDAAKQRKIFNREYVDMLLNAPQDHITPLRGSKLWQITLLEYWLQEQGL
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