SitesBLAST
Comparing WP_011382566.1 NCBI__GCF_000009985.1:WP_011382566.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
33% identity, 58% coverage: 1:373/639 of query aligns to 1:358/554 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 (= H29) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H80) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A105) mutation to H: Little effect on the kinetic properties.
- E349 (≠ W364) 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)
33% identity, 58% coverage: 3:373/639 of query aligns to 2:341/497 of 1ct9A
- active site: L50 (= L50), N74 (= N74), G75 (= G75), T305 (≠ S341), R308 (vs. gap), E332 (≠ W364)
- binding adenosine monophosphate: L232 (≠ F262), L233 (= L263), S234 (= S264), S239 (= S269), A255 (≠ G288), V256 (≠ L289), D263 (≠ E298), M316 (≠ L349), S330 (≠ T362), G331 (= G363), E332 (≠ W364)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (≠ V52), V53 (= V53), N74 (= N74), G75 (= G75), E76 (= E76), D98 (= D99)
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)
30% identity, 58% coverage: 1:373/639 of query aligns to 1:374/561 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 (≠ A230) to E: in dbSNP:rs1049674
- F362 (≠ L361) 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)
30% identity, 58% coverage: 2:373/639 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ F5), L49 (= L50), N74 (= N74), G75 (= G75), T324 (≠ S341), R327 (vs. gap)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R49), V51 (= V52), V52 (= V53), Y73 (= Y73), N74 (= N74), G75 (= G75), E76 (= E76), V95 (≠ S98), D96 (= D99)
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, 58% coverage: 1:373/639 of query aligns to 1:365/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 489 modified: Phosphoserine
1jgtB Crystal structure of beta-lactam synthetase (see paper)
30% identity, 47% coverage: 72:372/639 of query aligns to 71:353/500 of 1jgtB
- active site: A73 (≠ N74), G74 (= G75), D319 (≠ F338), Y345 (≠ W364)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F262), L245 (= L263), S246 (= S264), G248 (= G266), I249 (≠ L267), D250 (= D268), S251 (= S269), S269 (≠ A290), M270 (≠ F291), L327 (= L346), G344 (= G363), Y345 (≠ W364), D348 (= D367)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ T342), Y345 (≠ W364), G346 (= G365), D348 (= D367), I349 (≠ E368)
- binding magnesium ion: D250 (= D268), D348 (= D367)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
29% identity, 47% coverage: 72:372/639 of query aligns to 67:345/496 of 1mbzA
- active site: A69 (≠ N74), G70 (= G75), D311 (≠ F338), Y337 (≠ W364)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F262), L237 (= L263), S238 (= S264), S243 (= S269), S261 (≠ A290), M262 (≠ F291), Y315 (≠ T342), L319 (= L346), G336 (= G363), Y337 (≠ W364), G338 (= G365), D340 (= D367), I341 (≠ E368)
- binding magnesium ion: D242 (= D268), D340 (= D367)
- binding pyrophosphate 2-: S238 (= S264), G240 (= G266), D242 (= D268), S243 (= S269), D340 (= D367)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
29% identity, 47% coverage: 72:372/639 of query aligns to 63:340/491 of 1mc1A
- active site: A65 (≠ N74), G66 (= G75), D306 (≠ F338), Y332 (≠ W364)
- binding adenosine monophosphate: V231 (≠ F262), S233 (= S264), S238 (= S269), S256 (≠ A290), M257 (≠ F291), G331 (= G363)
- binding magnesium ion: D237 (= D268), D335 (= D367)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ T342), Y332 (≠ W364), G333 (= G365), I336 (≠ E368)
- binding pyrophosphate 2-: S233 (= S264), G235 (= G266), D237 (= D268), S238 (= S269), D335 (= D367)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 47% coverage: 72:372/639 of query aligns to 68:344/485 of 1mb9A
- active site: A70 (≠ N74), G71 (= G75), D310 (≠ F338), Y336 (≠ W364)
- binding adenosine monophosphate: V235 (≠ F262), L236 (= L263), S242 (= S269), S260 (≠ A290), M261 (≠ F291), Y314 (≠ T342), L318 (= L346), G335 (= G363), Y336 (≠ W364)
- binding adenosine-5'-triphosphate: V235 (≠ F262), L236 (= L263), S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), S260 (≠ A290), M261 (≠ F291), L318 (= L346), G335 (= G363), D339 (= D367)
- binding magnesium ion: D241 (= D268), D339 (= D367)
- binding pyrophosphate 2-: S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), D339 (= D367)
Sites not aligning to the query:
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
30% identity, 26% coverage: 2:164/639 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)
30% identity, 26% coverage: 2:164/639 of query aligns to 87:285/561 of Q9STG9
- H187 (≠ Y73) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K144) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P145) 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.
Q27601 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPAT; Phosphoribosylamidotransferase; PRAT; EC 2.4.2.14 from Drosophila melanogaster (Fruit fly) (see paper)
27% identity, 26% coverage: 2:170/639 of query aligns to 54:286/546 of Q27601
- S113 (vs. gap) modified: Phosphoserine
- T114 (vs. gap) modified: Phosphothreonine
- S120 (vs. gap) modified: Phosphoserine
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
27% identity, 26% coverage: 2:164/639 of query aligns to 12:209/476 of P00497
- C12 (= C2) active site, Nucleophile; mutation to F: Loss of enzyme activity and N-terminal processing.
Sites not aligning to the query:
- 1:11 modified: propeptide
- 247 binding [4Fe-4S] cluster
- 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.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
27% identity, 26% coverage: 2:164/639 of query aligns to 1:198/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
26% identity, 26% coverage: 2:164/639 of query aligns to 1:194/455 of 1ao0A
Sites not aligning to the query:
- active site: 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436
Query Sequence
>WP_011382566.1 NCBI__GCF_000009985.1:WP_011382566.1
MCGIFGMVRGGGRPVESNVLAAMKTALHHRGPDGNGIFAEGPVGLGNTRLAVVDTAGGSQ
PVIDPSSGAAIVYNGELFNHLELRAELESVGWCFRTHSDTEVVLAAFCVWGEDCVLRFNG
MYAFAVFDPKARRVFIARDPAGIKPLYLTETADGLAFASEAKALLPIAGRRPDWQALWGY
LTYGYMAPDCSPFAGITKFPAGSLAWIDLELPAARLAVRPYWQPRFGCGAPLAEGEAVDR
LDALLSQAVKHELMSDVPVGLFLSGGLDSSAVAYYAARRHGQAISSFGLAFEETTHDESN
DARTVARHLGIEHKELMFSPALVREGLRRVTETMDEPFGDSTVVPLLMLSRFAREHVTVV
LTGWGGDEVLAGYPTLTAHRVASLYRRLPGMLAHGLVPALVDRLPVSDKYLSFEFKARRF
LRGMKLTPEQQHFLWMGYFDDAFKHALLTPDVTAQVAQQDSLAHFAGMAAGMAEPTLTDR
IMHLDFRYFLHGNGLFQADRMTMAASLEARVPLLNKQMLDFALPLPAGLKMAGGTPKGLL
KKALAPHLPPAILSKPKKGFGPPSGHWVRSVFGPLLDHLFSRERIEAQGILNHATVARLL
AEHRELKADHGRTLWALMSLQLWYDRFILDQASPLERAA
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