SitesBLAST
Comparing WP_012971900.1 NCBI__GCF_000025485.1:WP_012971900.1 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 11 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)
27% identity, 88% coverage: 1:530/605 of query aligns to 1:462/554 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 (≠ Y80) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ N105) mutation to H: Little effect on the kinetic properties.
- E349 (= E364) 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)
27% identity, 84% coverage: 29:539/605 of query aligns to 29:454/497 of 1ct9A
- active site: L50 (= L50), N74 (= N74), G75 (= G75), T305 (≠ M338), R308 (≠ Y341), E332 (= E364), M366 (≠ L415)
- binding adenosine monophosphate: L232 (≠ F261), L233 (= L262), S234 (= S263), S239 (= S268), A255 (≠ S287), V256 (= V288), D263 (≠ E298), M316 (≠ L349), S330 (= S362), G331 (= G363), E332 (= E364)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ I53), N74 (= N74), G75 (= G75), E76 (= E76), D98 (= D99)
Sites not aligning to the query:
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)
26% identity, 84% coverage: 22:527/605 of query aligns to 23:473/557 of P78753
- S391 (≠ N455) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
28% identity, 58% coverage: 24:373/605 of query aligns to 20:361/509 of 6gq3A
- active site: L49 (= L50), N74 (= N74), G75 (= G75), T324 (≠ S347), R327 (≠ A350)
- binding 5-oxo-l-norleucine: R48 (= R49), V51 (≠ I52), V52 (≠ I53), Y73 (≠ A73), N74 (= N74), G75 (= G75), E76 (= E76), V95 (≠ S98), D96 (= 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)
27% identity, 58% coverage: 24:373/605 of query aligns to 21:374/561 of P08243
- V210 (vs. gap) to E: in dbSNP:rs1049674
- F362 (= F361) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
Sites not aligning to the query:
- 2 active site, For GATase activity; C→A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- 6 A → E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- 550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974
1jgtB Crystal structure of beta-lactam synthetase (see paper)
28% identity, 50% coverage: 72:375/605 of query aligns to 71:356/500 of 1jgtB
- active site: A73 (≠ N74), G74 (= G75), D319 (= D340), Y345 (≠ E364)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F261), L245 (= L262), S246 (= S263), G248 (= G265), I249 (≠ L266), D250 (= D267), S251 (= S268), S269 (= S287), M270 (≠ V288), L327 (≠ T346), G344 (= G363), Y345 (≠ E364), D348 (= D367)
- binding n2-(carboxyethyl)-l-arginine: Y323 (vs. gap), Y345 (≠ E364), G346 (= G365), D348 (= D367), I349 (≠ E368), M354 (≠ Y373)
- binding magnesium ion: D250 (= D267), D348 (= D367)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 50% coverage: 72:375/605 of query aligns to 63:343/491 of 1mc1A
- active site: A65 (≠ N74), G66 (= G75), D306 (= D340), Y332 (≠ E364)
- binding adenosine monophosphate: V231 (≠ F261), S233 (= S263), S238 (= S268), S256 (= S287), M257 (≠ V288), G331 (= G363)
- binding magnesium ion: D237 (= D267), D335 (= D367)
- binding deoxyguanidinoproclavaminic acid: Y310 (vs. gap), Y332 (≠ E364), G333 (= G365), I336 (≠ E368)
- binding pyrophosphate 2-: S233 (= S263), G235 (= G265), D237 (= D267), S238 (= S268), D335 (= D367)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 50% coverage: 72:375/605 of query aligns to 68:347/485 of 1mb9A
- active site: A70 (≠ N74), G71 (= G75), D310 (= D340), Y336 (≠ E364)
- binding adenosine monophosphate: V235 (≠ F261), L236 (= L262), S242 (= S268), S260 (= S287), M261 (≠ V288), Y314 (vs. gap), L318 (≠ T346), G335 (= G363), Y336 (≠ E364)
- binding adenosine-5'-triphosphate: V235 (≠ F261), L236 (= L262), S237 (= S263), G239 (= G265), D241 (= D267), S242 (= S268), S260 (= S287), M261 (≠ V288), L318 (≠ T346), G335 (= G363), D339 (= D367)
- binding magnesium ion: D241 (= D267), D339 (= D367)
- binding pyrophosphate 2-: S237 (= S263), G239 (= G265), D241 (= D267), S242 (= S268), D339 (= D367)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 50% coverage: 72:375/605 of query aligns to 67:348/496 of 1mbzA
- active site: A69 (≠ N74), G70 (= G75), D311 (= D340), Y337 (≠ E364)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F261), L237 (= L262), S238 (= S263), S243 (= S268), S261 (= S287), M262 (≠ V288), Y315 (vs. gap), L319 (≠ T346), G336 (= G363), Y337 (≠ E364), G338 (= G365), D340 (= D367), I341 (≠ E368)
- binding magnesium ion: D242 (= D267), D340 (= D367)
- binding pyrophosphate 2-: S238 (= S263), G240 (= G265), D242 (= D267), S243 (= S268), D340 (= D367)
Sites not aligning to the query:
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)
28% identity, 20% coverage: 41:164/605 of query aligns to 151:285/561 of Q9STG9
- H187 (≠ A73) 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.
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
31% identity, 16% coverage: 67:164/605 of query aligns to 95:199/460 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
Query Sequence
>WP_012971900.1 NCBI__GCF_000025485.1:WP_012971900.1
MCGIAGFMLARGRRPEPEWLDRMAERLAHRGPDDRGRYCAGPVGLVQTRLSIIGLESGHQ
PLLSADGQLALVANGEVYNYIELNAELRALGQPPRTGSDSETILNAYAAHGLDALDRLRG
MYAFALHDARAGRLILGRDRLGIKPLFYVRLPDRIAFASEIKALLALLPESPRIQPSALR
QFLQNQFAGGEETLIDGIRRVPPGTALLIDADLNIRPHRYWLALDVEPRRIGFEEARAEL
DALMDDAMREHQRSDVPFGLFLSGGLDSAVLAAKLAEQGAGRIKSYSVGYRGTAMAHELD
EAARVATHFGFDHRPLELELPRVFGRLPHTVWCADELMRDYACLPTSILAETAGAELKVV
FSGEGGDEAFAGYGRYRPPLAERLLKSLLHPGSGGFRTRGQWAGRWTRRLMGPALRAVAD
ADRAPVRRAWSETPRHWSDMQRRQYTDLVTALPDNLLVKTDRLLMGFGLEGRVPFLDHRI
VEFGLSLPDALKVQGHQGKWLVRRWAEPKLPPGHLERPKRGFHVPVGDWLRGSLATEVGR
RLALNPGVRDWFEVTAIPELVAARQAGRGGGRELFGLMQFAIWHRLFIERPGLRPTPDED
PLDWI
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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