SitesBLAST
Comparing 7025394 FitnessBrowser__ANA3:7025394 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)
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
71% identity, 100% coverage: 1:554/554 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 (= E349) 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)
70% identity, 93% coverage: 3:517/554 of query aligns to 2:497/497 of 1ct9A
- active site: L50 (= L51), N74 (= N75), G75 (= G76), T305 (= T322), R308 (= R325), E332 (= E349), M366 (≠ L383)
- binding adenosine monophosphate: L232 (= L233), L233 (= L234), S234 (= S235), S239 (= S240), A255 (= A272), V256 (= V273), D263 (= D280), M316 (= M333), S330 (= S347), G331 (= G348), E332 (= E349)
- 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)
51% identity, 98% coverage: 1:544/554 of query aligns to 1:547/557 of P78753
- S391 (≠ F384) modified: Phosphoserine
- S489 (≠ D474) 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)
41% identity, 92% coverage: 1:507/554 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 (≠ S6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ Q197) 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: 30:507/554 of query aligns to 25:501/509 of 6gq3A
- active site: L49 (= L51), N74 (= N75), G75 (= G76), T324 (= T322), R327 (= R325)
- 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, 68% coverage: 76:454/554 of query aligns to 71:435/485 of 1mb9A
- active site: G71 (= G76), D310 (≠ T322), Y336 (≠ E349), E370 (≠ L383), K431 (= K450)
- binding adenosine monophosphate: V235 (≠ L233), L236 (= L234), S242 (= S240), S260 (≠ A272), M261 (≠ V273), Y314 (≠ A326), L318 (≠ M330), G335 (= G348), Y336 (≠ E349)
- binding adenosine-5'-triphosphate: V235 (≠ L233), L236 (= L234), S237 (= S235), G239 (= G237), D241 (= D239), S242 (= S240), S260 (≠ A272), M261 (≠ V273), L318 (≠ M330), G335 (= G348), D339 (= D352), K411 (= K430), K431 (= K450)
- binding magnesium ion: D241 (= D239), D339 (= D352)
- binding pyrophosphate 2-: S237 (= S235), G239 (= G237), D241 (= D239), S242 (= S240), D339 (= D352), K411 (= K430), K431 (= K450)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 69% coverage: 76:460/554 of query aligns to 66:437/491 of 1mc1A
- active site: G66 (= G76), D306 (≠ T322), Y332 (≠ E349), E366 (≠ L383), K427 (= K450)
- binding adenosine monophosphate: V231 (≠ L233), S233 (= S235), S238 (= S240), S256 (≠ A272), M257 (≠ V273), G331 (= G348), K427 (= K450), V430 (≠ F453)
- binding magnesium ion: D237 (= D239), D335 (= D352)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A326), Y332 (≠ E349), G333 (= G350), I336 (≠ E353), D357 (≠ L374), E366 (≠ L383), K427 (= K450)
- binding pyrophosphate 2-: S233 (= S235), G235 (= G237), D237 (= D239), S238 (= S240), D335 (= D352), K407 (= K430), K427 (= K450), L428 (≠ E451)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 69% coverage: 76:460/554 of query aligns to 70:442/496 of 1mbzA
- active site: G70 (= G76), D311 (≠ T322), Y337 (≠ E349), E371 (≠ L383), K432 (= K450)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L233), L237 (= L234), S238 (= S235), S243 (= S240), S261 (≠ A272), M262 (≠ V273), Y315 (≠ A326), L319 (≠ M330), G336 (= G348), Y337 (≠ E349), G338 (= G350), D340 (= D352), I341 (≠ E353), D362 (≠ L374), E371 (≠ L383), K432 (= K450), G434 (≠ Q452), V435 (≠ F453)
- binding magnesium ion: D242 (= D239), D340 (= D352)
- binding pyrophosphate 2-: S238 (= S235), G240 (= G237), D242 (= D239), S243 (= S240), D340 (= D352), K412 (= K430), K432 (= K450), L433 (≠ E451)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
26% identity, 68% coverage: 76:450/554 of query aligns to 74:440/500 of 1jgtB
- active site: G74 (= G76), D319 (≠ T322), Y345 (≠ E349), E379 (≠ L383), K440 (= K450)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L233), L245 (= L234), S246 (= S235), G248 (= G237), I249 (≠ L238), D250 (= D239), S251 (= S240), S269 (≠ A272), M270 (≠ V273), L327 (≠ M330), G344 (= G348), Y345 (≠ E349), D348 (= D352), K420 (= K430), K440 (= K450)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A326), Y345 (≠ E349), G346 (= G350), D348 (= D352), I349 (≠ E353), M354 (≠ Y358), D370 (≠ L374), E379 (≠ L383)
- binding magnesium ion: D250 (= D239), D348 (= D352)
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)
27% identity, 46% coverage: 231:487/554 of query aligns to 242:475/503 of Q9XB61
- 244:251 (vs. 233:240, 88% identical) binding
- I270 (≠ V273) binding
- GYGSD 344:348 (≠ GEGAD 348:352) binding
- Y345 (≠ E349) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G350) binding
- Q371 (≠ E373) binding
- R374 (= R376) binding
- E380 (≠ L387) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K430) binding
- K443 (= K450) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ EQF 451:453) binding
1q19A Carbapenam synthetase (see paper)
27% identity, 46% coverage: 231:487/554 of query aligns to 241:474/500 of 1q19A
- active site: L318 (≠ T322), E321 (≠ R325), Y344 (≠ E349), E379 (≠ L387), K442 (= K450)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L233), L244 (= L234), S245 (= S235), D249 (= D239), S250 (= S240), S268 (≠ A272), I269 (≠ V273), T342 (≠ S347), G343 (= G348), D347 (= D352), K442 (= K450), I443 (≠ E451), G444 (≠ Q452), I445 (≠ F453)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E349), G345 (= G350), L348 (≠ E353), R373 (= R376), E379 (≠ L387)
Sites not aligning to the query:
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
31% identity, 28% coverage: 28:181/554 of query aligns to 23:211/455 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
30% identity, 28% coverage: 28:181/554 of query aligns to 34:226/476 of P00497
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 247 binding
- 294 binding
- 356 binding
- 357 binding
- 393 binding
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding ; C→S: Loss of activity.
- 451 binding ; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
30% identity, 28% coverage: 28:181/554 of query aligns to 23:215/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440
Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
33% identity, 21% coverage: 68:181/554 of query aligns to 181:302/561 of Q9STG9
- H187 (≠ V74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ I144) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P145) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
Sites not aligning to the query:
- 371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
- 476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
- 494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
33% identity, 21% coverage: 68:181/554 of query aligns to 95:216/460 of 6lbpA
Sites not aligning to the query:
- active site: 1, 27, 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
Query Sequence
>7025394 FitnessBrowser__ANA3:7025394
MCSIFSILDIQSDAKELRQVALEMSKLMRHRGPDWSGIYASDKAILAHERLAIVDIEHGA
QPLLTEDGSLILAVNGEIYNHKELKAQLGDKYSYQTNSDCEVILALYQEYGTEFLDKLNG
IFAFVLYDKAKDAYLIGRDHMGIIPLYTGRDAAGNFYVASEMKALMPVCKTVAEFQPGQY
LYSSIGEPVQYYTRDWQSFDAVKDNGASQEELRDALEAAVKRQLMSDVPYGVLLSGGLDS
SVISAITQTFAKRRIEDDDQSGAWWPQLHSFAVGLKGAPDLAAAKKVADAIGTIHHEINF
TFQEGLDAIKEVIYHLETYDVTTIRAATPMYLMARKIKAMGIKMVLSGEGADELFGGYLY
FHKAPNAQAFHEELVRKLDKLHLFDCLRANKAMAAWGLEARVPFLDKEFMDVAMRINPEA
KMSKDGRIEKHILRQAFEHKLPKEVAWRQKEQFSDGVGYSWIDGLKAHAAEQVDDLQLAN
AKFRFPYNTPETKEAYFYRCFFEEHYPLPSAAETVPGGKSVACSTPEALAWDESLRGIID
PSGRAVRSVHAASY
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