SitesBLAST
Comparing 5209024 FitnessBrowser__PV4:5209024 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 12 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)
70% identity, 100% coverage: 1:552/552 of query aligns to 1:553/554 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 (= H30) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A105) mutation to H: Little effect on the kinetic properties.
- E349 (= E347) 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)
69% identity, 93% coverage: 3:515/552 of query aligns to 2:497/497 of 1ct9A
- active site: L50 (= L51), N74 (= N75), G75 (= G76), T305 (= T320), R308 (= R323), E332 (= E347), M366 (≠ L381)
- binding adenosine monophosphate: L232 (= L231), L233 (= L232), S234 (= S233), S239 (= S238), A255 (= A270), V256 (= V271), D263 (= D278), M316 (= M331), S330 (= S345), G331 (= G346), E332 (= E347)
- binding glutamine: R49 (= R50), L50 (= L51), I52 (= I53), V53 (= V54), N74 (= N75), G75 (= G76), E76 (= E77), 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)
52% identity, 98% coverage: 1:542/552 of query aligns to 1:547/557 of P78753
- S391 (≠ F382) modified: Phosphoserine
- S489 (≠ D472) 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)
42% identity, 91% coverage: 1:505/552 of query aligns to 1:527/561 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 (= A6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ Q195) to E: in dbSNP:rs1049674
- F362 (vs. gap) 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)
42% identity, 86% coverage: 30:505/552 of query aligns to 25:501/509 of 6gq3A
- active site: L49 (= L51), N74 (= N75), G75 (= G76), T324 (= T320), R327 (= R323)
- binding 5-oxo-l-norleucine: R48 (= R50), V51 (≠ I53), V52 (= V54), Y73 (≠ V74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S98), D96 (= D99)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 71% coverage: 60:452/552 of query aligns to 57:435/485 of 1mb9A
- active site: A70 (= A73), G71 (= G76), D310 (≠ T320), Y336 (≠ E347), E370 (≠ L381), K431 (= K448)
- binding adenosine monophosphate: V235 (≠ L231), L236 (= L232), S242 (= S238), S260 (≠ A270), M261 (≠ V271), Y314 (≠ A324), L318 (≠ M328), G335 (= G346), Y336 (≠ E347)
- binding adenosine-5'-triphosphate: V235 (≠ L231), L236 (= L232), S237 (= S233), G239 (= G235), D241 (= D237), S242 (= S238), S260 (≠ A270), M261 (≠ V271), L318 (≠ M328), G335 (= G346), D339 (= D350), K411 (= K428), K431 (= K448)
- binding magnesium ion: D241 (= D237), D339 (= D350)
- binding pyrophosphate 2-: S237 (= S233), G239 (= G235), D241 (= D237), S242 (= S238), D339 (= D350), K411 (= K428), K431 (= K448)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 72% coverage: 60:458/552 of query aligns to 52:437/491 of 1mc1A
- active site: A65 (= A73), G66 (= G76), D306 (≠ T320), Y332 (≠ E347), E366 (≠ L381), K427 (= K448)
- binding adenosine monophosphate: V231 (≠ L231), S233 (= S233), S238 (= S238), S256 (≠ A270), M257 (≠ V271), G331 (= G346), K427 (= K448), V430 (≠ F451)
- binding magnesium ion: D237 (= D237), D335 (= D350)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A324), Y332 (≠ E347), G333 (= G348), I336 (≠ E351), D357 (≠ L372), E366 (≠ L381), K427 (= K448)
- binding pyrophosphate 2-: S233 (= S233), G235 (= G235), D237 (= D237), S238 (= S238), D335 (= D350), K407 (= K428), K427 (= K448), L428 (≠ E449)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 72% coverage: 60:458/552 of query aligns to 56:442/496 of 1mbzA
- active site: A69 (= A73), G70 (= G76), D311 (≠ T320), Y337 (≠ E347), E371 (≠ L381), K432 (= K448)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L231), L237 (= L232), S238 (= S233), S243 (= S238), S261 (≠ A270), M262 (≠ V271), Y315 (≠ A324), L319 (≠ M328), G336 (= G346), Y337 (≠ E347), G338 (= G348), D340 (= D350), I341 (≠ E351), D362 (≠ L372), E371 (≠ L381), K432 (= K448), G434 (≠ Q450), V435 (≠ F451)
- binding magnesium ion: D242 (= D237), D340 (= D350)
- binding pyrophosphate 2-: S238 (= S233), G240 (= G235), D242 (= D237), S243 (= S238), D340 (= D350), K412 (= K428), K432 (= K448), L433 (≠ E449)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 70% coverage: 60:448/552 of query aligns to 60:440/500 of 1jgtB
- active site: A73 (= A73), G74 (= G76), D319 (≠ T320), Y345 (≠ E347), E379 (≠ L381), K440 (= K448)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L231), L245 (= L232), S246 (= S233), G248 (= G235), I249 (≠ L236), D250 (= D237), S251 (= S238), S269 (≠ A270), M270 (≠ V271), L327 (≠ M328), G344 (= G346), Y345 (≠ E347), D348 (= D350), K420 (= K428), K440 (= K448)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A324), Y345 (≠ E347), G346 (= G348), D348 (= D350), I349 (≠ E351), M354 (≠ Y356), D370 (≠ L372), E379 (≠ L381)
- binding magnesium ion: D250 (= D237), D348 (= D350)
1q19A Carbapenam synthetase (see paper)
24% identity, 74% coverage: 76:485/552 of query aligns to 56:474/500 of 1q19A
- active site: G56 (= G76), L318 (≠ T320), E321 (≠ R323), Y344 (≠ E347), E379 (≠ L385), K442 (= K448)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L231), L244 (= L232), S245 (= S233), D249 (= D237), S250 (= S238), S268 (≠ A270), I269 (≠ V271), T342 (≠ S345), G343 (= G346), D347 (= D350), K442 (= K448), I443 (≠ E449), G444 (≠ Q450), I445 (≠ F451)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E347), G345 (= G348), L348 (≠ E351), R373 (= R374), E379 (≠ L385)
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)
24% identity, 74% coverage: 76:485/552 of query aligns to 57:475/503 of Q9XB61
- 244:251 (vs. 231:238, 88% identical) binding
- I270 (≠ V271) binding
- GYGSD 344:348 (≠ GEGAD 346:350) binding
- Y345 (≠ E347) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G348) binding
- Q371 (≠ E371) binding
- R374 (= R374) binding
- E380 (≠ L385) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K428) binding
- K443 (= K448) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ EQF 449:451) binding
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
28% identity, 30% coverage: 28:192/552 of query aligns to 23:222/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436
Query Sequence
>5209024 FitnessBrowser__PV4:5209024
MCSIFAILDIQTDATPLRQVALEMSKLLRHRGPDWSGIYASDKAILAHERLAIVDIEHGA
QPLLSEDESLILAVNGEIYNHKELKAELGDKYSYQTNSDCEVILALYQEYGTEFLDKLNG
IFAFVLYDKRSDSYLIGRDHMGIIPLYTGHDAEGNFYVASEMKALMPVCKTVETFKPGHY
LTKSGETHYYQRDWQSFEAVQDNAASVEELREALEAAVKRQLMSDVPYGVLLSGGLDSSV
VSAITQTFAKRRIEDDGASDAWWPQLHSFAVGLTGAPDLAAAQKVADAIGTIHHEITFSF
QEGLDALKDVIYHLETYDVTTIRAATPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFH
KAPNAQAFHEELVRKLDKLHLFDCLRANKAMAAWGLEARVPFLDKAFIDTAMRINPEAKM
SKDGRIEKHILRQAFEHKLPQEVAWRQKEQFSDGVGYSWIDGLKEHAAAQVDDLQLANAK
FRFPYNTPETKEAYFYRCFFEEHFPLPSAAETVPGGKSVACSTPEALAWDESLQGIIDPS
GRAVQSVHESAY
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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