SitesBLAST
Comparing WP_015926901.1 NCBI__GCF_000022085.1:WP_015926901.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
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, 85% coverage: 4:503/590 of query aligns to 1:443/557 of P78753
- S391 (≠ V452) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
28% identity, 84% coverage: 27:520/590 of query aligns to 27:433/497 of 1ct9A
- active site: L50 (= L50), N74 (= N75), G75 (= G76), T305 (≠ S347), R308 (≠ H348), E332 (≠ Q371), M366 (≠ L416)
- binding adenosine monophosphate: L232 (= L266), L233 (= L267), S234 (= S268), S239 (= S273), A255 (≠ S292), V256 (≠ I293), D263 (≠ E305), M316 (≠ L356), S330 (= S369), G331 (= G370), E332 (≠ Q371)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ L53), N74 (= N75), G75 (= G76), E76 (≠ C77), 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)
28% identity, 88% coverage: 1:520/590 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 (≠ A29) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ F81) 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.
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)
25% identity, 88% coverage: 1:520/590 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 (≠ R217) 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)
24% identity, 87% coverage: 5:519/590 of query aligns to 1:456/509 of 6gq3A
- active site: W4 (≠ I8), L49 (= L50), N74 (= N75), G75 (= G76), T324 (≠ S347), R327 (≠ H348)
- binding 5-oxo-l-norleucine: C1 (= C5), R48 (= R49), V51 (≠ I52), V52 (≠ L53), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (≠ C77), V95 (≠ G99), D96 (= D100)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
29% identity, 52% coverage: 73:381/590 of query aligns to 67:347/496 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 (≠ I293), Y315 (≠ F353), L319 (vs. gap), G336 (= G370), Y337 (≠ Q371), G338 (= G372), D340 (= D374), I341 (≠ E375)
- 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:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
29% identity, 52% coverage: 73:381/590 of query aligns to 71:355/500 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 (≠ I293), 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)
- binding magnesium ion: D250 (= D272), D348 (= D374)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
29% identity, 52% coverage: 73:381/590 of query aligns to 63:342/491 of 1mc1A
- active site: A65 (≠ N75), G66 (= G76), D306 (= D349), Y332 (≠ Q371)
- binding adenosine monophosphate: V231 (≠ L266), S233 (= S268), S238 (= S273), S256 (= S292), M257 (≠ I293), G331 (= G370)
- binding magnesium ion: D237 (= D272), D335 (= D374)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ F353), Y332 (≠ Q371), G333 (= G372), I336 (≠ E375)
- binding pyrophosphate 2-: S233 (= S268), G235 (= G270), D237 (= D272), S238 (= S273), D335 (= D374)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
30% identity, 52% coverage: 73:381/590 of query aligns to 68:346/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (= D349), Y336 (≠ Q371)
- binding adenosine monophosphate: V235 (≠ L266), L236 (= L267), S242 (= S273), S260 (= S292), M261 (≠ I293), 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 (≠ I293), 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:
1q19A Carbapenam synthetase (see paper)
22% identity, 72% coverage: 91:517/590 of query aligns to 72:442/500 of 1q19A
- active site: L318 (≠ M345), E321 (≠ H348), Y344 (≠ Q371), E379 (≠ H429), K442 (= K517)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L266), L244 (= L267), S245 (= S268), D249 (= D272), S250 (= S273), S268 (= S292), I269 (= I293), T342 (≠ S369), G343 (= G370), D347 (= D374), K442 (= K517)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q371), G345 (= G372), L348 (≠ E375), R373 (= R423), E379 (≠ H429)
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)
22% identity, 72% coverage: 91:517/590 of query aligns to 73:443/503 of Q9XB61
- 244:251 (vs. 266:273, 88% identical) binding ATP
- I270 (= I293) binding ATP
- GYGSD 344:348 (≠ GQGAD 370:374) binding ATP
- Y345 (≠ Q371) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G372) binding substrate
- Q371 (≠ D420) binding substrate
- R374 (= R423) binding substrate
- E380 (≠ H429) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K497) binding ATP
- K443 (= K517) mutation K->A,M: Loss of activity.
Sites not aligning to the query:
1xfgA Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate (see paper)
42% identity, 11% coverage: 40:104/590 of query aligns to 64:127/238 of 1xfgA
Sites not aligning to the query:
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
42% identity, 11% coverage: 40:104/590 of query aligns to 64:127/238 of 1xffA
Sites not aligning to the query:
2j6hA E. Coli glucosamine-6-p synthase in complex with glucose-6p and 5-oxo- l-norleucine (see paper)
42% identity, 11% coverage: 40:104/590 of query aligns to 64:127/608 of 2j6hA
Sites not aligning to the query:
- active site: 1, 26, 27, 248, 481, 485, 488, 504, 603
- binding glucose-6-phosphate: 302, 347, 348, 349, 352, 399, 401, 488
- binding 5-oxo-l-norleucine: 1
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
42% identity, 11% coverage: 40:104/590 of query aligns to 64:127/608 of 4amvA
Sites not aligning to the query:
- active site: 1, 26, 27, 248, 481, 485, 488, 504, 603
- binding fructose -6-phosphate: 301, 302, 303, 347, 348, 349, 352, 401, 485, 488
1jxaA Glucosamine 6-phosphate synthase with glucose 6-phosphate (see paper)
42% identity, 11% coverage: 40:104/590 of query aligns to 64:127/608 of 1jxaA
Sites not aligning to the query:
- active site: 1, 26, 27, 248, 481, 485, 488, 504, 603
- binding glucose-6-phosphate: 302, 303, 347, 348, 349, 352, 401, 485, 488
Query Sequence
>WP_015926901.1 NCBI__GCF_000022085.1:WP_015926901.1
MCGICGEIRLDGAPPDAAAVAAMAVPLRARGPDAGGSFAQGGIAFGHRRLSILDLSPASQ
QPMVDPGLGLAIVFNGCIYNFRSLREELRAKGYAFFSEGDTEVILKAYHAWGPRCVERFY
GMFAFVLWERDSGRVVIARDRLGIKPLYYAESGSRLRFASSLPALLAAGDLDRSIDPAAL
HHYMSFHAVVPAPLTILKGVRKVPPATIITIEPDGRRRQETYWEAVVTERPDDRHMTESD
WCEAVLATLRKAVERRLVSDVPVGVLLSGGLDSSIVVALLAEAGQRGLKTFSIGFESVGG
EAGDEFTYSDIIAERFATDHHRIRIDSARALPALHGAVAAMSEPMVSHDAVGFYLLSEEV
SKHVKVVQSGQGADEIFGGYHWYPPMMQSTDAVADYARVFFDRDHAEMREALSPSLVDGD
VSRAFVEAHFARAGAPRPIDKALRIDTEIMLVDDPVKRVDNMTMAWGLEARVPFLDHDLV
ELAGRVPADLKIRDGGKFILKQAGRRVVPSEVIDRPKGYFPVPALKYLRGPFLDLVRDVL
NEPVARERGLFNRAYVDRLLAEPEAHMTPLRGSKLWQVALLEFWLQTHAI
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