SitesBLAST
Comparing N515DRAFT_1546 FitnessBrowser__Dyella79:N515DRAFT_1546 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 10 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)
61% identity, 100% coverage: 1:558/559 of query aligns to 1:552/554 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 (= H32) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D36) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H83) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A105) mutation to H: Little effect on the kinetic properties.
- E349 (= E354) 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)
58% identity, 93% coverage: 3:522/559 of query aligns to 2:497/497 of 1ct9A
- active site: L50 (= L53), N74 (= N77), G75 (= G78), T305 (= T327), R308 (= R330), E332 (= E354), M366 (≠ S388)
- binding adenosine monophosphate: L232 (= L238), L233 (= L239), S234 (= S240), S239 (= S245), A255 (= A277), V256 (≠ I278), D263 (= D285), M316 (≠ L338), S330 (= S352), G331 (= G353), E332 (= E354)
- binding glutamine: R49 (= R52), L50 (= L53), I52 (= I55), V53 (= V56), N74 (= N77), G75 (= G78), E76 (= E79), 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)
51% identity, 100% coverage: 1:559/559 of query aligns to 1:556/557 of P78753
- S391 (≠ F389) modified: Phosphoserine
- S489 (= S479) 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)
39% identity, 99% coverage: 1:551/559 of query aligns to 1:552/561 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 (≠ Y204) to E: in dbSNP:rs1049674
- F362 (≠ L351) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
- R550 (= R549) to 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)
40% identity, 92% coverage: 2:515/559 of query aligns to 1:504/509 of 6gq3A
- active site: W4 (≠ F5), L49 (= L53), N74 (= N77), G75 (= G78), T324 (= T327), R327 (= R330)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R52), V51 (≠ I55), V52 (= V56), Y73 (≠ V76), N74 (= N77), G75 (= G78), E76 (= E79), V95 (≠ S98), D96 (= D99)
1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 68% coverage: 78:459/559 of query aligns to 71:435/485 of 1mb9A
- active site: G71 (= G78), D310 (≠ T327), Y336 (≠ E354), E370 (≠ S388), K431 (= K455)
- binding adenosine monophosphate: V235 (≠ L238), L236 (= L239), S242 (= S245), S260 (≠ A277), M261 (≠ I278), Y314 (≠ A331), L318 (≠ M335), G335 (= G353), Y336 (≠ E354)
- binding adenosine-5'-triphosphate: V235 (≠ L238), L236 (= L239), S237 (= S240), G239 (= G242), D241 (= D244), S242 (= S245), S260 (≠ A277), M261 (≠ I278), L318 (≠ M335), G335 (= G353), D339 (= D357), K411 (= K435), K431 (= K455)
- binding magnesium ion: D241 (= D244), D339 (= D357)
- binding pyrophosphate 2-: S237 (= S240), G239 (= G242), D241 (= D244), S242 (= S245), D339 (= D357), K411 (= K435), K431 (= K455)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 69% coverage: 78:463/559 of query aligns to 66:435/491 of 1mc1A
- active site: G66 (= G78), D306 (≠ T327), Y332 (≠ E354), E366 (≠ S388), K427 (= K455)
- binding adenosine monophosphate: V231 (≠ L238), S233 (= S240), S238 (= S245), S256 (≠ A277), M257 (≠ I278), G331 (= G353), K427 (= K455), V430 (≠ F458)
- binding magnesium ion: D237 (= D244), D335 (= D357)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A331), Y332 (≠ E354), G333 (= G355), I336 (≠ E358), D357 (≠ T379), E366 (≠ S388), K427 (= K455)
- binding pyrophosphate 2-: S233 (= S240), G235 (= G242), D237 (= D244), S238 (= S245), D335 (= D357), K407 (= K435), K427 (= K455), L428 (≠ E456)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 69% coverage: 78:463/559 of query aligns to 70:440/496 of 1mbzA
- active site: G70 (= G78), D311 (≠ T327), Y337 (≠ E354), E371 (≠ S388), K432 (= K455)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L238), L237 (= L239), S238 (= S240), S243 (= S245), S261 (≠ A277), M262 (≠ I278), Y315 (≠ A331), L319 (≠ M335), G336 (= G353), Y337 (≠ E354), G338 (= G355), D340 (= D357), I341 (≠ E358), D362 (≠ T379), E371 (≠ S388), K432 (= K455), G434 (≠ Q457), V435 (≠ F458)
- binding magnesium ion: D242 (= D244), D340 (= D357)
- binding pyrophosphate 2-: S238 (= S240), G240 (= G242), D242 (= D244), S243 (= S245), D340 (= D357), K412 (= K435), K432 (= K455), L433 (≠ E456)
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
29% identity, 40% coverage: 236:461/559 of query aligns to 241:448/500 of 1q19A
- active site: L318 (≠ T327), E321 (≠ R330), Y344 (≠ E354), E379 (≠ S388), K442 (= K455)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L238), L244 (= L239), S245 (= S240), D249 (= D244), S250 (= S245), S268 (≠ A277), I269 (= I278), T342 (≠ S352), G343 (= G353), D347 (= D357), K442 (= K455), I443 (≠ E456), G444 (≠ Q457), I445 (≠ F458)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E354), G345 (= G355), L348 (≠ E358), R373 (≠ K382), E379 (≠ S388)
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)
29% identity, 40% coverage: 236:461/559 of query aligns to 242:449/503 of Q9XB61
- 244:251 (vs. 238:245, 88% identical) binding
- I270 (= I278) binding
- GYGSD 344:348 (≠ GEGSD 353:357) binding
- Y345 (≠ E354) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G355) binding
- Q371 (≠ T379) binding
- R374 (≠ K382) binding
- E380 (≠ S388) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K435) binding
- K443 (= K455) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ EQF 456:458) binding
Query Sequence
>N515DRAFT_1546 FitnessBrowser__Dyella79:N515DRAFT_1546
MCSIFGMFDLQPGDDLAGLRRQALELSQRQRHRGPDWSGVFVDAGVILVHERLAIVDPAS
GSQPLRSREETLALAVNGEIYNHRELRAASGYDFTTGSDCEVINALYRELGPEEFLARGI
KQLNGIFAFALWDSATQRYLIARDPIGVCPLYWGHDGEGRLCVASEMKALVGVCADVSAF
PPGHVYDSATGEVTRYYRKHWRSYEVTHGQQLEPSALRGAFEQAVHRQLMTDVPYGVLLS
GGLDSSLVAACAARFARERIEDDDRSEAWWPRLHSFAIGLEGSPDLAAAQVAADALGTVH
HGFVYTFWEGLDALPEVIRHIETYDVTTIRASTPMFLLARRIKAMGVKMVLSGEGSDEIF
GGYLYFHKAPSPEAFHEETVRKLDALHSFDCLRANKAMMAWGVEARVPFLDLEFLDVAMG
LDARYKMAGHGRIEKAVLREAFQGALPDSILWRQKEQFSDGVGYGWIDGLKAHAEQVVSD
REFAAASTRFPHNPPATKEAYLYRRIFEQHFPGEACAATVPGGKSIACSSPAALAWDPAF
AAAADPSGRAVRGVHQQAL
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