SitesBLAST
Comparing WP_009543906.1 NCBI__GCF_000017845.1:WP_009543906.1 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)
38% identity, 97% coverage: 1:486/501 of query aligns to 1:511/554 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 (= H25) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D29) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y77) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H101) mutation to H: Little effect on the kinetic properties.
- E349 (= E326) 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)
38% identity, 99% coverage: 1:497/501 of query aligns to 1:535/557 of P78753
- S391 (≠ I361) modified: Phosphoserine
- S489 (= S449) modified: Phosphoserine
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
40% identity, 92% coverage: 25:486/501 of query aligns to 29:491/497 of 1ct9A
- active site: L50 (= L48), N74 (= N71), G75 (= G72), T305 (≠ D300), R308 (= R303), E332 (= E326), M366 (≠ N360)
- binding adenosine monophosphate: L232 (≠ F225), L233 (= L226), S234 (= S227), S239 (= S232), A255 (≠ S250), V256 (= V251), D263 (= D258), M316 (≠ T311), S330 (≠ T324), G331 (= G325), E332 (= E326)
- binding glutamine: R49 (= R47), L50 (= L48), I52 (= I50), V53 (≠ M51), N74 (= N71), G75 (= G72), E76 (= E73), D98 (= D95)
Sites not aligning to the query:
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)
33% identity, 95% coverage: 1:477/501 of query aligns to 1:522/561 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 (vs. gap) to E: in dbSNP:rs1049674
- F362 (≠ L323) 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)
34% identity, 95% coverage: 2:477/501 of query aligns to 1:496/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L48), N74 (= N71), G75 (= G72), T324 (≠ D300), R327 (= R303)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R47), V51 (≠ I50), V52 (≠ M51), Y73 (≠ G70), N74 (= N71), G75 (= G72), E76 (= E73), V95 (≠ S94), D96 (= D95)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 77% coverage: 72:459/501 of query aligns to 70:465/496 of 1mbzA
- active site: G70 (= G72), D311 (= D300), Y337 (≠ E326), E371 (≠ L363), K432 (= K427)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F225), L237 (= L226), S238 (= S227), S243 (= S232), S261 (= S250), M262 (≠ V251), Y315 (≠ S304), L319 (≠ C308), G336 (= G325), Y337 (≠ E326), G338 (= G327), D340 (= D329), I341 (≠ E330), D362 (≠ S354), E371 (≠ L363), K432 (= K427), G434 (≠ Q429), V435 (≠ F430)
- binding magnesium ion: D242 (= D231), D340 (= D329)
- binding pyrophosphate 2-: S238 (= S227), G240 (= G229), D242 (= D231), S243 (= S232), D340 (= D329), K412 (= K407), K432 (= K427), L433 (≠ E428)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 77% coverage: 72:459/501 of query aligns to 66:460/491 of 1mc1A
- active site: G66 (= G72), D306 (= D300), Y332 (≠ E326), E366 (≠ L363), K427 (= K427)
- binding adenosine monophosphate: V231 (≠ F225), S233 (= S227), S238 (= S232), S256 (= S250), M257 (≠ V251), G331 (= G325), K427 (= K427), V430 (≠ F430)
- binding magnesium ion: D237 (= D231), D335 (= D329)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ S304), Y332 (≠ E326), G333 (= G327), I336 (≠ E330), D357 (≠ S354), E366 (≠ L363), K427 (= K427)
- binding pyrophosphate 2-: S233 (= S227), G235 (= G229), D237 (= D231), S238 (= S232), D335 (= D329), K407 (= K407), K427 (= K427), L428 (≠ E428)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 72% coverage: 72:430/501 of query aligns to 71:434/485 of 1mb9A
- active site: G71 (= G72), D310 (= D300), Y336 (≠ E326), E370 (≠ L363), K431 (= K427)
- binding adenosine monophosphate: V235 (≠ F225), L236 (= L226), S242 (= S232), S260 (= S250), M261 (≠ V251), Y314 (≠ S304), L318 (≠ C308), G335 (= G325), Y336 (≠ E326)
- binding adenosine-5'-triphosphate: V235 (≠ F225), L236 (= L226), S237 (= S227), G239 (= G229), D241 (= D231), S242 (= S232), S260 (= S250), M261 (≠ V251), L318 (≠ C308), G335 (= G325), D339 (= D329), K411 (= K407), K431 (= K427)
- binding magnesium ion: D241 (= D231), D339 (= D329)
- binding pyrophosphate 2-: S237 (= S227), G239 (= G229), D241 (= D231), S242 (= S232), D339 (= D329), K411 (= K407), K431 (= K427)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
28% identity, 71% coverage: 72:427/501 of query aligns to 74:440/500 of 1jgtB
- active site: G74 (= G72), D319 (= D300), Y345 (≠ E326), E379 (≠ L363), K440 (= K427)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F225), L245 (= L226), S246 (= S227), G248 (= G229), I249 (≠ L230), D250 (= D231), S251 (= S232), S269 (= S250), M270 (≠ V251), L327 (≠ C308), G344 (= G325), Y345 (≠ E326), D348 (= D329), K420 (= K407), K440 (= K427)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ S304), Y345 (≠ E326), G346 (= G327), D348 (= D329), I349 (≠ E330), M354 (≠ Y335), D370 (≠ S354), E379 (≠ L363)
- binding magnesium ion: D250 (= D231), D348 (= D329)
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
29% identity, 47% coverage: 222:455/501 of query aligns to 240:470/500 of 1q19A
- active site: L318 (≠ D300), E321 (≠ R303), Y344 (≠ E326), E379 (≠ S354), K442 (= K427)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F225), L244 (= L226), S245 (= S227), D249 (= D231), S250 (= S232), S268 (= S250), I269 (≠ V251), T342 (= T324), G343 (= G325), D347 (= D329), K442 (= K427), I443 (≠ E428), G444 (≠ Q429), I445 (≠ F430)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E326), G345 (= G327), L348 (≠ E330), R373 (≠ H348), E379 (≠ S354)
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)
29% identity, 47% coverage: 222:455/501 of query aligns to 241:471/503 of Q9XB61
- 244:251 (vs. 225:232, 88% identical) binding ATP
- I270 (≠ V251) binding ATP
- GYGSD 344:348 (≠ GEGAD 325:329) binding ATP
- Y345 (≠ E326) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G327) binding substrate
- Q371 (≠ A345) binding substrate
- R374 (≠ H348) binding substrate
- E380 (≠ S354) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K407) binding ATP
- K443 (= K427) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ EQF 428:430) binding ATP
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
29% identity, 31% coverage: 2:158/501 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)
29% identity, 31% coverage: 2:158/501 of query aligns to 87:285/561 of Q9STG9
- H187 (≠ G70) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K138) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P139) 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.
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
27% identity, 48% coverage: 2:239/501 of query aligns to 12:301/476 of P00497
- C12 (= C2) active site, Nucleophile; mutation to F: Loss of enzyme activity and N-terminal processing.
- C247 (vs. gap) binding [4Fe-4S] cluster
- S294 (= S232) binding Mg(2+)
Sites not aligning to the query:
- 1:11 modified: propeptide
- 356 binding Mg(2+)
- 357 binding Mg(2+)
- 393 binding [4Fe-4S] cluster
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding [4Fe-4S] cluster; C→S: Loss of activity.
- 451 binding [4Fe-4S] cluster; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
27% identity, 48% coverage: 2:239/501 of query aligns to 1:290/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 382, 384, 388, 437, 440
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
28% identity, 48% coverage: 2:239/501 of query aligns to 1:286/455 of 1ao0A
- active site: C1 (= C2), G27 (= G27), N98 (= N71), G99 (= G72), Y238 (= Y183)
- binding guanosine-5'-monophosphate: M234 (vs. gap), Y238 (= Y183), S279 (= S232)
- binding adenosine-5'-diphosphate: H25 (= H25), Y238 (= Y183), S240 (≠ N185), R241 (≠ L186), P242 (= P187), P277 (≠ L230), D278 (= D231), S279 (= S232)
- binding magnesium ion: S279 (= S232)
- binding iron/sulfur cluster: C232 (vs. gap), S233 (vs. gap), 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
Query Sequence
>WP_009543906.1 NCBI__GCF_000017845.1:WP_009543906.1
MCGIAGIWGKTSQSNIEAMMESIVHRGPDANGIFVVPDGSGILGHQRLSIMDVEGGDQPI
YGDGKKAIIGNGEIYNYPQLFSDLESKYQFVTKSDTEAILHLYDDKNITAIPELDGMFSF
AIIDNNKFIAARDPIGIKPLYYSEKDGNFWFASELKAITQFCEDVKEFPPGTFFSSETGF
STYYNLPDISPDIDANVDDIVKEIQETVQASVVKRLMADVPLGAFLSGGLDSSIIAAIAK
KHKSELHTFSVGVEGSKDINAARLVSDYLGTIHHEYLITPKEAIAKLPEIIYALESFDQD
LVRSAIPCYFTSRLAAQYVKVILTGEGADELFAGYTYYKDITSDAILHTELRRSVSSLHN
INLQRVDRLTMAHSIEGRVPFLDLKMIELGQKIPAHLKLRGNPPVEKWILRKAFEDILPD
EIVWRKKEQFDEGSGTVDLLVDTLKDIMSEEQAQTYQKQHSHINLRSAEECYYHQIFMDV
FDNPTAILNNVARWADRPVLV
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