SitesBLAST
Comparing WP_007475570.1 NCBI__GCF_000170735.1:WP_007475570.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
26% identity, 72% coverage: 23:473/630 of query aligns to 26:463/497 of 1ct9A
- active site: L50 (= L47), N74 (= N72), G75 (= G73), T305 (≠ P337), R308 (≠ D340), E332 (≠ D364), M366 (≠ K381)
- binding adenosine monophosphate: L232 (≠ F264), L233 (= L265), S234 (= S266), S239 (= S271), A255 (≠ T288), V256 (≠ I289), D263 (≠ E298), M316 (≠ L348), S330 (= S362), G331 (≠ A363), E332 (≠ D364)
- binding glutamine: R49 (= R46), L50 (= L47), I52 (= I49), V53 (≠ L50), N74 (= N72), G75 (= G73), E76 (= E74), D98 (= D97)
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)
29% identity, 62% coverage: 1:392/630 of query aligns to 1:377/554 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 (≠ Y26) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D30) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ F78) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K103) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D364) 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, 59% coverage: 1:373/630 of query aligns to 1:365/557 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)
28% identity, 59% coverage: 1:373/630 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 (≠ C226) 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)
28% identity, 59% coverage: 2:373/630 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ V5), L49 (= L47), N74 (= N72), G75 (= G73), T324 (≠ F338), R327 (≠ S341)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R46), V51 (≠ I49), V52 (≠ L50), Y73 (= Y71), N74 (= N72), G75 (= G73), E76 (= E74), V95 (≠ S96), D96 (= D97)
1mb9A Beta-lactam synthetase complexed with atp (see paper)
24% identity, 44% coverage: 57:332/630 of query aligns to 46:299/485 of 1mb9A
- active site: A70 (≠ N72), G71 (= G73)
- binding adenosine monophosphate: V235 (≠ F264), L236 (= L265), S242 (= S271), S260 (≠ T288), M261 (≠ I289)
- binding adenosine-5'-triphosphate: V235 (≠ F264), L236 (= L265), S237 (= S266), G239 (= G268), D241 (= D270), S242 (= S271), S260 (≠ T288), M261 (≠ I289)
- binding magnesium ion: D241 (= D270)
- binding pyrophosphate 2-: S237 (= S266), G239 (= G268), D241 (= D270), S242 (= S271)
Sites not aligning to the query:
- active site: 310, 336, 370, 431
- binding adenosine monophosphate: 314, 318, 335, 336
- binding adenosine-5'-triphosphate: 318, 335, 339, 411, 431
- binding magnesium ion: 339
- binding pyrophosphate 2-: 339, 411, 431
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
24% identity, 44% coverage: 57:332/630 of query aligns to 45:300/496 of 1mbzA
Sites not aligning to the query:
- active site: 311, 337, 371, 432
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: 315, 319, 336, 337, 338, 340, 341, 362, 371, 432, 434, 435
- binding magnesium ion: 340
- binding pyrophosphate 2-: 340, 412, 432, 433
1q19A Carbapenam synthetase (see paper)
39% identity, 18% coverage: 261:372/630 of query aligns to 240:352/500 of 1q19A
- active site: L318 (≠ D340), E321 (≠ S343), Y344 (≠ D364)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F264), L244 (= L265), S245 (= S266), D249 (= D270), S250 (= S271), S268 (≠ T288), I269 (= I289), T342 (≠ S362), G343 (≠ A363), D347 (= D367)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D364), G345 (= G365), L348 (≠ E368)
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)
26% identity, 45% coverage: 89:372/630 of query aligns to 74:353/503 of Q9XB61
- 244:251 (vs. 264:271, 75% identical) binding ATP
- I270 (= I289) binding ATP
- GYGSD 344:348 (≠ ADGGD 363:367) binding ATP
- Y345 (≠ D364) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G365) 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
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
26% identity, 25% coverage: 2:159/630 of query aligns to 1:190/455 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
30% identity, 16% coverage: 58:159/630 of query aligns to 96:205/476 of P00497
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 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)
30% identity, 16% coverage: 58:159/630 of query aligns to 85:194/465 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
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, 22% coverage: 40:179/630 of query aligns to 153:298/561 of Q9STG9
- H187 (≠ Y71) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K143) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P144) 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)
29% identity, 22% coverage: 40:179/630 of query aligns to 67:212/460 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_007475570.1 NCBI__GCF_000170735.1:WP_007475570.1
MCGIVGFINKEKRFDVLNNMLLIQNYRGPDDYGLYFDNGVHLGHNRLSILDLSDAGHQPF
ISEDENYVIVYNGEVYNFKQIRKELEKLGERFKSNSDTEVILKSYIHWGIEKSIEKFRGM
FAFAIYDKLNKKIILVRDRAGVKPLYYYIDGNEFVFASELKSICQYPFFKKELNKNILPY
YFQFGYIPAPFSIYKNCYKLEPGHYLEYDLNNNRYHITKYWDIDNCYLQEKIDANEKEIL
NDLENILEESFNLRMIADVPVGVFLSGGIDSSLVTAILSKKYKLNTFTIGFDDKRYDEAS
HAKIVANYFKTNHNELYINETMMLKKIEKLPYYYDEPFGDSSSIPTMLVSELAKKQVTVS
LSADGGDEIFCGYSKYFALNKINRLFSNKLKKKFIKLSVNLLEENIVEKLNELLPSKIKQ
RNIKDKFNKFKRAINSNSFEDMFLEATSYSDKNIVRSILNIDINKKAFNKFKFLPQLSLL
ENLMRIDYKTFLVDDVLVKVDRATMSVSLEGREPLLDHKISEYLGKIPIELKYKNNQGKY
LAKQILYKYIPKEIIDKPKSGFQIPLEKWIKEDLKLLVNHYISKEKIDKEIFNIDEILQI
KKEVFNGKVKNLSLLWFVLMYQMWKEKWFE
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