SitesBLAST
Comparing WP_012281454.1 NCBI__GCF_000019165.1:WP_012281454.1 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 13 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, 87% coverage: 1:534/614 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 (= H30) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ T83) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ L108) mutation to H: Little effect on the kinetic properties.
- E349 (= E379) 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)
29% identity, 87% coverage: 2:534/614 of query aligns to 1:433/497 of 1ct9A
- active site: A1 (≠ C2), L50 (= L51), N74 (= N77), G75 (= G78), T305 (≠ A355), R308 (≠ E358), E332 (= E379), M366 (≠ W463)
- binding adenosine monophosphate: L232 (= L263), L233 (= L264), S234 (= S265), S239 (= S270), A255 (≠ S293), V256 (≠ I294), D263 (= D313), M316 (≠ F364), S330 (= S377), G331 (= G378), E332 (= E379)
- binding glutamine: A1 (≠ C2), R49 (= R50), L50 (= L51), I52 (≠ V53), V53 (= V54), N74 (= N77), G75 (= G78), E76 (= E79), D98 (= D102)
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)
30% identity, 87% coverage: 1:534/614 of query aligns to 1:468/557 of P78753
- S391 (≠ A466) 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)
28% identity, 64% coverage: 1:393/614 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 (≠ V8) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ T193) to E: in dbSNP:rs1049674
- F362 (≠ L376) 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, 64% coverage: 2:393/614 of query aligns to 1:366/509 of 6gq3A
- active site: W4 (= W7), L49 (= L51), N74 (= N77), G75 (= G78), T324 (≠ A355), R327 (≠ E358)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (= V53), V52 (= V54), Y73 (= Y76), N74 (= N77), G75 (= G78), E76 (= E79), V95 (≠ S101), D96 (= D102)
1q19A Carbapenam synthetase (see paper)
24% identity, 70% coverage: 101:531/614 of query aligns to 79:442/500 of 1q19A
- active site: L318 (≠ M354), E321 (≠ D356), Y344 (≠ E379), E379 (= E446), K442 (= K531)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (vs. gap), L244 (= L264), S245 (= S265), D249 (= D269), S250 (= S270), S268 (= S293), I269 (= I294), T342 (≠ S377), G343 (= G378), D347 (= D382), K442 (= K531)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E379), G345 (≠ C380), L348 (≠ E383), R373 (≠ E435), E379 (= E446)
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)
24% identity, 70% coverage: 101:531/614 of query aligns to 80:443/503 of Q9XB61
- 244:251 (vs. 264:270, 88% identical) binding ATP
- I270 (= I294) binding ATP
- GYGSD 344:348 (≠ GECAD 378:382) binding ATP
- Y345 (≠ E379) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (≠ C380) binding substrate
- Q371 (≠ R432) binding substrate
- R374 (≠ E435) binding substrate
- E380 (= E446) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K511) binding ATP
- K443 (= K531) mutation K->A,M: Loss of activity.
Sites not aligning to the query:
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
26% identity, 36% coverage: 38:259/614 of query aligns to 60:281/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 382, 384, 388, 437, 440
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
26% identity, 36% coverage: 38:259/614 of query aligns to 71:292/476 of P00497
- C247 (vs. gap) binding [4Fe-4S] cluster
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 294 binding Mg(2+)
- 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.
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
26% identity, 36% coverage: 38:259/614 of query aligns to 60:277/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 27, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 25, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 378, 380, 433, 436
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)
37% identity, 20% coverage: 46:167/614 of query aligns to 155:285/561 of Q9STG9
- H187 (≠ Y76) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K147) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P148) 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)
37% identity, 20% coverage: 46:167/614 of query aligns to 69:199/460 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
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 55% coverage: 63:397/614 of query aligns to 59:360/500 of 1jgtB
- active site: A73 (≠ N77), G74 (= G78), D319 (≠ G353), Y345 (≠ E379)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L263), L245 (= L264), S246 (= S265), G248 (= G267), I249 (≠ L268), D250 (= D269), S251 (= S270), S269 (= S293), M270 (≠ I294), L327 (= L361), G344 (= G378), Y345 (≠ E379), D348 (= D382)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ V357), Y345 (≠ E379), G346 (≠ C380), D348 (= D382), I349 (≠ E383), M354 (≠ F391)
- binding magnesium ion: D250 (= D269), D348 (= D382)
Sites not aligning to the query:
Query Sequence
>WP_012281454.1 NCBI__GCF_000019165.1:WP_012281454.1
MCGIVGWVDWEADLSQQGTILDAMVETLTHRGPDASGTWISPQALIGHRRLSVVDRIGGV
QPMIREVGGRRYVLTYNGELYNTPELRQELEVRGHRFRTRSDTEALLLAFIEWGEDCVQK
LNGIFAFGVWDETERRLFLARDRMGVKPLFYVRRGSALLFASELKALLAHPDIRPELDAE
GLAEVFAIAPARTPGHGVFKGIQEVRPGYTLTIDAASMRKKPYWTLKSRPHEDNLEQTTE
RLRELLLDAIERQLVSDVPVCTLLSGGLDSSTLTAVAAHVYARDGLGPLNTYSIDYRDND
IYFKPSAFQPNADAPWIKRVSAHLGTVHHDVIIDTPELVDALRPALWARDLPGMADVESS
LYLFCREIKKGATVALSGECADEVFGGYPWFHRPELLNVGTFPWSRRLAERADLLAPEMR
QYIQPEAYVARRYEETLAEVPRLPGEDAEEARRREMFYLNIHWFMATLLDRKDRMSMAHG
LEVRVPFCDHRIVEYVWNIPWAMKTCEGREKGLLRRALRGILPEDVLWRKKSPYPKTHHP
AYTAAVRQWLTEILHDPASPLLPIIDVEKVRALAAADAVTTDLPWFGQLMGLPQLYAYLA
QVDLWLRTMQISIR
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