SitesBLAST
Comparing WP_006748146.1 NCBI__GCF_000227685.2:WP_006748146.1 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 15 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)
29% identity, 88% coverage: 1:523/595 of query aligns to 1:453/554 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 (vs. gap) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ F81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K106) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q370) 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)
30% identity, 84% coverage: 27:523/595 of query aligns to 27:433/497 of 1ct9A
- active site: L50 (= L50), N74 (= N75), G75 (= G76), T305 (≠ M344), R308 (≠ Q347), E332 (≠ Q370), M366 (≠ E434)
- binding adenosine monophosphate: L232 (= L265), L233 (= L266), S234 (= S267), S239 (= S272), A255 (≠ T291), V256 (= V292), D263 (≠ E299), M316 (≠ L355), S330 (= S368), G331 (= G369), E332 (≠ Q370)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ L53), N74 (= N75), G75 (= G76), E76 (≠ A77), D98 (= D100)
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)
29% identity, 84% coverage: 1:501/595 of query aligns to 1:435/557 of P78753
- S391 (≠ D456) 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)
25% identity, 92% coverage: 1:547/595 of query aligns to 1:493/561 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 (≠ R229) to E: in dbSNP:rs1049674
- F362 (≠ Q367) 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)
25% identity, 87% coverage: 2:519/595 of query aligns to 1:453/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L50), N74 (= N75), G75 (= G76), T324 (≠ M344), R327 (≠ Q347)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R49), V51 (≠ I52), V52 (≠ L53), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (≠ A77), V95 (≠ G99), D96 (= D100)
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, 55% coverage: 53:378/595 of query aligns to 35:353/503 of Q9XB61
- 244:251 (vs. 265:272, 88% identical) binding ATP
- I270 (≠ V292) binding ATP
- GYGSD 344:348 (≠ GQGAD 369:373) binding ATP
- Y345 (≠ Q370) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G371) 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
1q19A Carbapenam synthetase (see paper)
26% identity, 55% coverage: 53:378/595 of query aligns to 34:352/500 of 1q19A
- active site: G56 (= G76), L318 (≠ M344), E321 (≠ Q347), Y344 (≠ Q370)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L265), L244 (= L266), S245 (= S267), D249 (= D271), S250 (= S272), S268 (≠ T291), I269 (≠ V292), T342 (≠ S368), G343 (= G369), D347 (= D373)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q370), G345 (= G371), L348 (≠ E374)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
26% identity, 54% coverage: 60:378/595 of query aligns to 49:353/500 of 1jgtB
- active site: A73 (vs. gap), G74 (vs. gap), D319 (≠ M344), Y345 (≠ Q370)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L265), L245 (= L266), S246 (= S267), G248 (= G269), I249 (≠ L270), D250 (= D271), S251 (= S272), S269 (≠ T291), M270 (≠ V292), L327 (≠ F352), G344 (= G369), Y345 (≠ Q370), D348 (= D373)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ D348), Y345 (≠ Q370), G346 (= G371), D348 (= D373), I349 (≠ E374)
- binding magnesium ion: D250 (= D271), D348 (= D373)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 54% coverage: 60:378/595 of query aligns to 45:345/496 of 1mbzA
- active site: A69 (vs. gap), G70 (vs. gap), D311 (≠ M344), Y337 (≠ Q370)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L265), L237 (= L266), S238 (= S267), S243 (= S272), S261 (≠ T291), M262 (≠ V292), Y315 (≠ D348), L319 (≠ F352), G336 (= G369), Y337 (≠ Q370), G338 (= G371), D340 (= D373), I341 (≠ E374)
- binding magnesium ion: D242 (= D271), D340 (= D373)
- binding pyrophosphate 2-: S238 (= S267), G240 (= G269), D242 (= D271), S243 (= S272), D340 (= D373)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 54% coverage: 60:378/595 of query aligns to 46:344/485 of 1mb9A
- active site: A70 (vs. gap), G71 (vs. gap), D310 (≠ M344), Y336 (≠ Q370)
- binding adenosine monophosphate: V235 (≠ L265), L236 (= L266), S242 (= S272), S260 (≠ T291), M261 (≠ V292), Y314 (≠ D348), L318 (≠ F352), G335 (= G369), Y336 (≠ Q370)
- binding adenosine-5'-triphosphate: V235 (≠ L265), L236 (= L266), S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), S260 (≠ T291), M261 (≠ V292), L318 (≠ F352), G335 (= G369), D339 (= D373)
- binding magnesium ion: D241 (= D271), D339 (= D373)
- binding pyrophosphate 2-: S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), D339 (= D373)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 58% coverage: 32:378/595 of query aligns to 3:340/491 of 1mc1A
- active site: A65 (vs. gap), G66 (vs. gap), D306 (≠ M344), Y332 (≠ Q370)
- binding adenosine monophosphate: V231 (≠ L265), S233 (= S267), S238 (= S272), S256 (≠ T291), M257 (≠ V292), G331 (= G369)
- binding magnesium ion: D237 (= D271), D335 (= D373)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ D348), Y332 (≠ Q370), G333 (= G371), I336 (≠ E374)
- binding pyrophosphate 2-: S233 (= S267), G235 (= G269), D237 (= D271), S238 (= S272), D335 (= D373)
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)
31% identity, 21% coverage: 41:165/595 of query aligns to 151:285/561 of Q9STG9
- H187 (≠ F74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K145) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P146) 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)
31% identity, 21% coverage: 41:165/595 of query aligns to 65:199/460 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
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
24% identity, 47% coverage: 2:282/595 of query aligns to 1:289/455 of 1ao0A
- active site: C1 (= C2), G27 (= G31), N98 (= N75), G99 (= G76), Y238 (vs. gap)
- binding guanosine-5'-monophosphate: M234 (vs. gap), Y238 (vs. gap), S279 (= S272)
- binding adenosine-5'-diphosphate: H25 (≠ R29), Y238 (vs. gap), S240 (≠ R228), R241 (= R229), P242 (= P230), P277 (≠ L270), D278 (= D271), S279 (= S272)
- binding magnesium ion: S279 (= S272)
- binding iron/sulfur cluster: C232 (= C226), S233 (≠ A227), M234 (vs. gap)
Sites not aligning to the query:
- active site: 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 300, 301, 301, 303
- binding magnesium ion: 341, 342
- binding iron/sulfur cluster: 378, 380, 433, 436
P14742 Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; GFAT; D-fructose-6-phosphate amidotransferase; Hexosephosphate aminotransferase; EC 2.6.1.16 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 15% coverage: 17:108/595 of query aligns to 56:148/717 of P14742
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 active site, For GATase activity
Query Sequence
>WP_006748146.1 NCBI__GCF_000227685.2:WP_006748146.1
MCGIAGEFVWGDRRADVDAVARMLPALARRGPDADGVWASGRAALGHRRLSILDLSQRAH
QPMFDPETGLALVFNGAIYNFRTLRAELERRGHRFFSSGDTEVILKGYAEWGEGVVARLH
GMFAFALFDSRTQKILLARDRMGIKPLYLARSGHGIRFASNTQALLDSGGVDPALDPEAL
HLLFSLHAVVPAPRTVLRGIRKLQPGHYLLIEADGHEHLERYWQLCARRPEQAIDDDEWR
ERIEAGLRRAVRRRLEVADVPVGVLLSGGLDSSLLVALAVEEGAQDLRTFTVGFEDQPEE
KGSEFEFSDPVAERYATDHQRTLIPNSEVLRRLPEAVAAMAEPMFGQDAVAFYLLAEQVS
QHVKVVQSGQGADEVFGGYFWYPKMAEERSGDWAERFRKHYFDRDDPEMRELLAAPPPND
LAGEWLRAELAMLETDRADSFIDAVLALDVTTLIVDDPVKRVDNMTMAFGLEARVPFLDH
ELVETAAAMPPHLKLGDGGKKVLKQIARGRLPDAVLDRPKGYFPVPALKYVRGDFLEFMR
DILGSQAARERGIYRPEYVQRLLDAPDQYFTRIQGSKLWHLALLEFWLQTHVDRA
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