SitesBLAST
Comparing WP_011383678.1 NCBI__GCF_000009985.1:WP_011383678.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
29% identity, 87% coverage: 21:527/585 of query aligns to 22:456/497 of 1ct9A
- active site: L50 (= L49), N74 (= N72), G75 (= G73), T305 (≠ A334), R308 (≠ Y337), E332 (= E360), M366 (≠ A429)
- binding adenosine monophosphate: L232 (≠ F257), L233 (= L258), S234 (= S259), S239 (= S264), A255 (≠ T283), V256 (≠ A284), D263 (≠ E294), M316 (≠ L345), S330 (= S358), G331 (= G359), E332 (= E360)
- binding glutamine: R49 (= R48), L50 (= L49), I52 (= I51), V53 (≠ I52), N74 (= N72), G75 (= G73), E76 (= E74), D98 (= D95)
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)
29% identity, 90% coverage: 1:527/585 of query aligns to 1:476/554 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 (= H28) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D32) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y78) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H101) mutation to H: Little effect on the kinetic properties.
- E349 (= E360) 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)
28% identity, 89% coverage: 1:523/585 of query aligns to 1:486/557 of P78753
- S391 (≠ L394) 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)
27% identity, 84% coverage: 1:493/585 of query aligns to 1:455/561 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 (≠ L216) to E: in dbSNP:rs1049674
- F362 (≠ L357) 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, 84% coverage: 2:493/585 of query aligns to 1:442/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L49), N74 (= N72), G75 (= G73), T324 (≠ A334), R327 (≠ Y337)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R48), V51 (≠ I51), V52 (≠ I52), Y73 (≠ A71), N74 (= N72), G75 (= G73), E76 (= E74), V95 (≠ S94), D96 (= D95)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
30% identity, 59% coverage: 62:405/585 of query aligns to 55:378/491 of 1mc1A
- active site: A65 (≠ N72), G66 (= G73), D306 (≠ A334), Y332 (≠ E360), E366 (≠ V396)
- binding adenosine monophosphate: V231 (≠ F257), S233 (= S259), S238 (= S264), S256 (≠ A284), M257 (≠ G285), G331 (= G359)
- binding magnesium ion: D237 (= D263), D335 (= D363)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A338), Y332 (≠ E360), G333 (= G361), I336 (≠ E364), D357 (≠ R387), E366 (≠ V396)
- binding pyrophosphate 2-: S233 (= S259), G235 (= G261), D237 (= D263), S238 (= S264), D335 (= D363)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
30% identity, 59% coverage: 62:405/585 of query aligns to 59:383/496 of 1mbzA
- active site: A69 (≠ N72), G70 (= G73), D311 (≠ A334), Y337 (≠ E360), E371 (≠ V396)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F257), L237 (= L258), S238 (= S259), S243 (= S264), S261 (≠ A284), M262 (≠ G285), Y315 (≠ A338), L319 (≠ T342), G336 (= G359), Y337 (≠ E360), G338 (= G361), D340 (= D363), I341 (≠ E364), D362 (≠ R387), E371 (≠ V396)
- binding magnesium ion: D242 (= D263), D340 (= D363)
- binding pyrophosphate 2-: S238 (= S259), G240 (= G261), D242 (= D263), S243 (= S264), D340 (= D363)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
30% identity, 59% coverage: 62:405/585 of query aligns to 63:391/500 of 1jgtB
- active site: A73 (≠ N72), G74 (= G73), D319 (≠ A334), Y345 (≠ E360), E379 (≠ V396)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F257), L245 (= L258), S246 (= S259), G248 (= G261), I249 (= I262), D250 (= D263), S251 (= S264), S269 (≠ A284), M270 (≠ G285), L327 (≠ T342), G344 (= G359), Y345 (≠ E360), D348 (= D363)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A338), Y345 (≠ E360), G346 (= G361), D348 (= D363), I349 (≠ E364), M354 (≠ Y369), D370 (≠ R387), E379 (≠ V396)
- binding magnesium ion: D250 (= D263), D348 (= D363)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 76% coverage: 62:507/585 of query aligns to 60:435/485 of 1mb9A
- active site: A70 (≠ N72), G71 (= G73), D310 (≠ A334), Y336 (≠ E360), E370 (≠ V396), K431 (= K503)
- binding adenosine monophosphate: V235 (≠ F257), L236 (= L258), S242 (= S264), S260 (≠ A284), M261 (≠ G285), Y314 (≠ A338), L318 (≠ T342), G335 (= G359), Y336 (≠ E360)
- binding adenosine-5'-triphosphate: V235 (≠ F257), L236 (= L258), S237 (= S259), G239 (= G261), D241 (= D263), S242 (= S264), S260 (≠ A284), M261 (≠ G285), L318 (≠ T342), G335 (= G359), D339 (= D363), K411 (= K483), K431 (= K503)
- binding magnesium ion: D241 (= D263), D339 (= D363)
- binding pyrophosphate 2-: S237 (= S259), G239 (= G261), D241 (= D263), S242 (= S264), D339 (= D363), K411 (= K483), K431 (= K503)
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
32% identity, 27% coverage: 2:160/585 of query aligns to 1:199/460 of 6lbpA
Sites not aligning to the query:
- active site: 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
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)
32% identity, 27% coverage: 2:160/585 of query aligns to 87:285/561 of Q9STG9
- H187 (vs. gap) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K140) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P141) 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.
1q19A Carbapenam synthetase (see paper)
26% identity, 41% coverage: 130:368/585 of query aligns to 128:352/500 of 1q19A
- active site: L318 (≠ A334), E321 (≠ Y337), Y344 (≠ E360)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F257), L244 (= L258), S245 (= S259), D249 (= D263), S250 (= S264), S268 (≠ G278), I269 (≠ V279), T342 (≠ S358), G343 (= G359), D347 (= D363)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E360), G345 (= G361), L348 (≠ E364)
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)
26% identity, 41% coverage: 130:368/585 of query aligns to 129:353/503 of Q9XB61
- 244:251 (vs. 257:264, 75% identical) binding
- I270 (≠ V279) binding
- GYGSD 344:348 (≠ GEGGD 359:363) binding
- Y345 (≠ E360) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G361) 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
Query Sequence
>WP_011383678.1 NCBI__GCF_000009985.1:WP_011383678.1
MCGIAGVMTANGPPDGQVLDKLADALAHRGPDGRGRHVSGNVGLVQNRLSIIDLEGGRQP
ILDGAGNAIVANGEIYNYLELKSDMAGQVFATGSDCEPPLHLYRHQGPAFARSLRGMYAF
AIHDGGAQKLVLGRDPFGIKPLYLTETAPGLAFASEPQALIAAGLVKPELDPAALAELLQ
LQFTTGTRTIFKGIRRLGAGETVVAEGGCVTEGRRLPALPAGGPVDGGLDQMLDQLDDTL
TESVELHQRSDVPYGMFLSGGIDSSVVLALMARLNPKGVLAFTAGFPGTRVHDERQHARD
LARAVGARHVEVEFTESDFWELLPLVAAAMDDPAADYACLPTFKLAREARKEVKVILSGE
GGDELFGGYGRYRHAMRPWPLTKSMRRKGTFDGLDVLRDGITSHWRHGMKLAERAEALPG
RTRLQVAQAVDCTDWLPNDLLTKADRCLMANGIEGRVPFLDPVVAAFAFRLPDHLKVRKG
LGKWILRRWLETALPAARPFDKKRGFTVPVAEWIAAKPQIGQLVARQPGIAEICHPGAVE
ALFRTCAKDTGFACWTLLFYALWHQRHVLGKIPAGDAFSELADRI
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