SitesBLAST
Comparing WP_036374485.1 NCBI__GCF_000015305.1:WP_036374485.1 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)
33% identity, 56% coverage: 30:389/643 of query aligns to 27:346/497 of 1ct9A
- active site: L50 (= L53), N74 (= N81), G75 (= G82), T305 (≠ V349), R308 (≠ P352), E332 (= E375)
- binding adenosine monophosphate: L232 (≠ F274), L233 (= L275), S234 (= S276), S239 (= S281), A255 (≠ T299), V256 (≠ T300), D263 (≠ E309), M316 (≠ I360), S330 (= S373), G331 (= G374), E332 (= E375)
- binding glutamine: R49 (= R52), L50 (= L53), I52 (= I55), V53 (≠ I56), N74 (= N81), G75 (= G82), E76 (= E83), D98 (= D107)
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)
31% identity, 61% coverage: 1:394/643 of query aligns to 1:368/554 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 (≠ Y87) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A113) mutation to H: Little effect on the kinetic properties.
- E349 (= E375) 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)
29% identity, 62% coverage: 1:396/643 of query aligns to 1:377/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 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)
29% identity, 60% coverage: 1:389/643 of query aligns to 1:379/561 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 (vs. gap) to E: in dbSNP:rs1049674
- F362 (≠ L372) 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)
28% identity, 60% coverage: 2:389/643 of query aligns to 1:366/509 of 6gq3A
- active site: W4 (≠ L5), L49 (= L53), N74 (= N81), G75 (= G82), T324 (≠ V349), R327 (≠ P352)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R52), V51 (≠ I55), V52 (≠ I56), Y73 (≠ F80), N74 (= N81), G75 (= G82), E76 (= E83), V95 (≠ G106), D96 (= D107)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
30% identity, 49% coverage: 77:389/643 of query aligns to 69:357/500 of 1jgtB
- active site: A73 (≠ N81), G74 (= G82), D319 (≠ V349), Y345 (≠ E375)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F274), L245 (= L275), S246 (= S276), G248 (= G278), I249 (= I279), D250 (= D280), S251 (= S281), S269 (≠ T299), M270 (≠ T300), L327 (= L357), G344 (= G374), Y345 (≠ E375), D348 (= D378)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A353), Y345 (≠ E375), G346 (= G376), D348 (= D378), I349 (≠ E379), M354 (≠ I386)
- binding magnesium ion: D250 (= D280), D348 (= D378)
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
28% identity, 48% coverage: 75:383/643 of query aligns to 49:352/500 of 1q19A
- active site: G56 (= G82), L318 (≠ V349), E321 (≠ P352), Y344 (≠ E375)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F274), L244 (= L275), S245 (= S276), D249 (= D280), S250 (= S281), S268 (≠ T299), I269 (≠ T300), T342 (≠ S373), G343 (= G374), D347 (= D378)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E375), G345 (= G376), L348 (≠ E379)
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)
28% identity, 48% coverage: 75:383/643 of query aligns to 50:353/503 of Q9XB61
- 244:251 (vs. 274:281, 75% identical) binding ATP
- I270 (≠ T300) binding ATP
- GYGSD 344:348 (≠ GEGAD 374:378) binding ATP
- Y345 (≠ E375) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G376) binding substrate
Sites not aligning to the query:
- 371 binding substrate
- 374 binding substrate
- 380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
- 421 binding ATP
- 443 mutation K->A,M: Loss of activity.
- 444:446 binding ATP
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
30% identity, 49% coverage: 77:389/643 of query aligns to 61:344/491 of 1mc1A
- active site: A65 (≠ N81), G66 (= G82), D306 (≠ V349), Y332 (≠ E375)
- binding adenosine monophosphate: V231 (≠ F274), S233 (= S276), S238 (= S281), S256 (≠ T299), M257 (≠ T300), G331 (= G374)
- binding magnesium ion: D237 (= D280), D335 (= D378)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A353), Y332 (≠ E375), G333 (= G376), I336 (≠ E379)
- binding pyrophosphate 2-: S233 (= S276), G235 (= G278), D237 (= D280), S238 (= S281), D335 (= D378)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
30% identity, 49% coverage: 77:389/643 of query aligns to 65:349/496 of 1mbzA
- active site: A69 (≠ N81), G70 (= G82), D311 (≠ V349), Y337 (≠ E375)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F274), L237 (= L275), S238 (= S276), S243 (= S281), S261 (≠ T299), M262 (≠ T300), Y315 (≠ A353), L319 (= L357), G336 (= G374), Y337 (≠ E375), G338 (= G376), D340 (= D378), I341 (≠ E379)
- binding magnesium ion: D242 (= D280), D340 (= D378)
- binding pyrophosphate 2-: S238 (= S276), G240 (= G278), D242 (= D280), S243 (= S281), D340 (= D378)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
30% identity, 49% coverage: 77:389/643 of query aligns to 66:348/485 of 1mb9A
- active site: A70 (≠ N81), G71 (= G82), D310 (≠ V349), Y336 (≠ E375)
- binding adenosine monophosphate: V235 (≠ F274), L236 (= L275), S242 (= S281), S260 (≠ T299), M261 (≠ T300), Y314 (≠ A353), L318 (= L357), G335 (= G374), Y336 (≠ E375)
- binding adenosine-5'-triphosphate: V235 (≠ F274), L236 (= L275), S237 (= S276), G239 (= G278), D241 (= D280), S242 (= S281), S260 (≠ T299), M261 (≠ T300), L318 (= L357), G335 (= G374), D339 (= D378)
- binding magnesium ion: D241 (= D280), D339 (= D378)
- binding pyrophosphate 2-: S237 (= S276), G239 (= G278), D241 (= D280), S242 (= S281), D339 (= D378)
Sites not aligning to the query:
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)
28% identity, 20% coverage: 74:203/643 of query aligns to 181:321/561 of Q9STG9
- H187 (≠ F80) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K152) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P153) 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)
28% identity, 20% coverage: 74:203/643 of query aligns to 95:235/460 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
>WP_036374485.1 NCBI__GCF_000015305.1:WP_036374485.1
MCGLLALVIDPSSEVSPTTVDAVSAASAQMRHRGPDEPGTWNDTRVVLGFNRLSIIDIAH
SHQPLRWGPPEAPGRYTLVFNGEIYNYLELRDALRSEFGAEFHTDGDGEAIVAAYHHWGA
DALTRLRGMFAFALWDSVAQELFCARDPFGIKPLYLATGTGGTAVGSEKKCLLDIADRLG
FDLGVDERAVQHYTVLQYVPEPETLHRGIRRLESGSYARVRPGAQPEVTRYFRPRFDAVA
FRAGAEQARYDEITAALEDSVAKHMRADVTVGAFLSGGIDSTAIAALAMRHNPRLITFTT
GFEREGFSEVDVAVASAEAIGARHVTKVVSQQEFVAALPEIVWYLDEPVADPALVPLYFI
AREARKHVKVVLSGEGADELFGGYTIYREPLSLKPFDYLPRGLRKSVGRMAGPLPEGMRG
KSLLHRGSLTLEERYYGNARSFSDAQLRAVLPRFRPEWVHTDVTAPVYAQSQDWDPVARM
QHIDLFTWLRGDILVKADKMTMANSLELRVPFLDPEVFAVASRLPYDQKITRSTTKYALR
RALEPIVPAHVLNRPKLGFPVPIRHWLRSGELLDWAYGMVGTSGAGDLVELAAVRAMLDE
HRSGTTDHSRRLWTVLIFMLWYAIFVDKTVTPQISEPTYPVQL
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