SitesBLAST
Comparing WP_012976121.1 NCBI__GCF_000010725.1:WP_012976121.1 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)
36% identity, 53% coverage: 20:380/684 of query aligns to 22:344/497 of 1ct9A
- active site: L50 (= L51), N74 (= N75), G75 (= G76), T305 (≠ R343), R308 (vs. gap), E332 (= E368)
- binding adenosine monophosphate: L232 (≠ Y265), L233 (≠ I266), S234 (= S267), S239 (= S272), A255 (≠ G291), V256 (= V292), D263 (≠ E301), M316 (≠ L352), S330 (= S366), G331 (= G367), E332 (= E368)
- binding glutamine: R49 (= R50), L50 (= L51), I52 (= I53), V53 (= V54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D100)
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)
33% identity, 56% coverage: 1:380/684 of query aligns to 1:361/554 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 (= H81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H106) mutation to H: Little effect on the kinetic properties.
- E349 (= E368) 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)
33% identity, 56% coverage: 1:380/684 of query aligns to 1:368/557 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)
29% identity, 56% coverage: 1:380/684 of query aligns to 1:377/561 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 (= V210) to E: in dbSNP:rs1049674
- F362 (vs. gap) 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)
29% identity, 52% coverage: 28:380/684 of query aligns to 23:364/509 of 6gq3A
- active site: L49 (= L51), N74 (= N75), G75 (= G76), T324 (≠ R343), R327 (vs. gap)
- binding 5-oxo-l-norleucine: R48 (= R50), V51 (≠ I53), V52 (= V54), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ T99), D96 (= D100)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
30% identity, 46% coverage: 74:385/684 of query aligns to 64:347/491 of 1mc1A
- active site: A65 (≠ N75), G66 (= G76), D306 (≠ L341), Y332 (≠ E368)
- binding adenosine monophosphate: V231 (≠ Y265), S233 (= S267), S238 (= S272), S256 (= S286), M257 (= M287), G331 (= G367)
- binding magnesium ion: D237 (= D271), D335 (= D371)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A345), Y332 (≠ E368), G333 (= G369), I336 (≠ E372)
- binding pyrophosphate 2-: S233 (= S267), G235 (= G269), D237 (= D271), S238 (= S272), D335 (= D371)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
30% identity, 46% coverage: 74:385/684 of query aligns to 68:352/496 of 1mbzA
- active site: A69 (≠ N75), G70 (= G76), D311 (≠ L341), Y337 (≠ E368)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ Y265), L237 (≠ I266), S238 (= S267), S243 (= S272), S261 (= S286), M262 (= M287), Y315 (≠ A345), L319 (= L349), G336 (= G367), Y337 (≠ E368), G338 (= G369), D340 (= D371), I341 (≠ E372)
- binding magnesium ion: D242 (= D271), D340 (= D371)
- binding pyrophosphate 2-: S238 (= S267), G240 (= G269), D242 (= D271), S243 (= S272), D340 (= D371)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 46% coverage: 74:385/684 of query aligns to 69:351/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (≠ L341), Y336 (≠ E368)
- binding adenosine monophosphate: V235 (≠ Y265), L236 (≠ I266), S242 (= S272), S260 (= S286), M261 (= M287), Y314 (≠ A345), L318 (= L349), G335 (= G367), Y336 (≠ E368)
- binding adenosine-5'-triphosphate: V235 (≠ Y265), L236 (≠ I266), S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), S260 (= S286), M261 (= M287), L318 (= L349), G335 (= G367), D339 (= D371)
- binding magnesium ion: D241 (= D271), D339 (= D371)
- binding pyrophosphate 2-: S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), D339 (= D371)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
29% identity, 46% coverage: 74:385/684 of query aligns to 72:360/500 of 1jgtB
- active site: A73 (≠ N75), G74 (= G76), D319 (≠ L341), Y345 (≠ E368)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ Y265), L245 (≠ I266), S246 (= S267), G248 (= G269), I249 (≠ L270), D250 (= D271), S251 (= S272), S269 (= S286), M270 (= M287), L327 (= L349), G344 (= G367), Y345 (≠ E368), D348 (= D371)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A345), Y345 (≠ E368), G346 (= G369), D348 (= D371), I349 (≠ E372), M354 (≠ L379)
- binding magnesium ion: D250 (= D271), D348 (= D371)
Sites not aligning to the query:
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
34% identity, 18% coverage: 44:165/684 of query aligns to 67:199/460 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
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)
34% identity, 18% coverage: 44:165/684 of query aligns to 153:285/561 of Q9STG9
- H187 (≠ F74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ L145) 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.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
29% identity, 18% coverage: 46:165/684 of query aligns to 68:198/465 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
29% identity, 18% coverage: 46:165/684 of query aligns to 79:209/476 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.
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
31% identity, 15% coverage: 66:165/684 of query aligns to 89:194/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 27, 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 25, 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_012976121.1 NCBI__GCF_000010725.1:WP_012976121.1
MCGVAGVLAGSRAEPAGLDELKRMIAMLSHRGPDGYGFYRDDRIGLAHARLSIVGLAGGF
QPIHNEDRSLWISFNGEIFNHVELRRDLEARGHRFYTRTDTEVIVHAFEEYGPATWARLN
GQFAICLWDATRRELWLVRDRLGILPLFYARRGDHLVFASEAKALFGGGRVAPAFDHARL
AQVFTHWSAAPHGSVFERVESVPAATAIRVDSTLALHVDRYWQPDFTADPALAKLSLDEA
ADRLEEKLLDAIRLRLRADVPVGVYISGGLDSSVIAALARKLDTTSMHSFGVRFTDAGFD
ETPQQRLVAGHVGTGHHDILCGPRDIQAALPDVVRHSETPLVRTAPAPLFLLSRLVRESG
IRVVLSGEGADEWLAGYDLFKEDKVRRFWARQPGSKVRPKLLGRVHPFAAVNGQKDSPLW
QAFFKRGMMETDEAFYAHRTRWRNTAWAQRLLSADVQATADDAAFEAHVAAHLPDGWSRW
SPLARSQWAEISSFMTPYLLSTQGDRVAMANGIEVRYPFLDPAVDDLCAALPDRVKMLGL
RDKLALRRLAARHLPAEIVQRPKRPYRAPMTSALFGDAAPDHVRDLLSPDALVRYGLTDA
TAVLALADKAHRRNGHMAGEREEMALVGALTLQMLAHYIQDDLPQRIRDQRAALDRAEIH
VLEDQALKDRAAGSRTATPQPTAA
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