SitesBLAST
Comparing YP_004144523.1 NCBI__GCF_000185905.1:YP_004144523.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
31% identity, 58% coverage: 1:388/673 of query aligns to 1:363/554 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 (= H31) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D35) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y82) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H107) mutation to H: Little effect on the kinetic properties.
- E349 (= E374) 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)
32% identity, 55% coverage: 19:389/673 of query aligns to 17:347/497 of 1ct9A
- active site: L50 (= L52), N74 (= N76), G75 (= G77), T305 (≠ R349), R308 (vs. gap), E332 (= E374)
- binding adenosine monophosphate: L232 (≠ Y271), L233 (= L272), S234 (= S273), S239 (= S278), A255 (≠ S297), V256 (≠ L298), D263 (≠ E307), M316 (≠ L358), S330 (≠ T372), G331 (= G373), E332 (= E374)
- binding glutamine: R49 (= R51), L50 (= L52), I52 (≠ V54), V53 (≠ I55), N74 (= N76), G75 (= G77), E76 (= E78), D98 (= D101)
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)
30% identity, 57% coverage: 1:386/673 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)
27% identity, 58% coverage: 1:389/673 of query aligns to 1:380/561 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 (vs. gap) 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, 57% coverage: 5:388/673 of query aligns to 1:366/509 of 6gq3A
- active site: W4 (≠ V8), L49 (= L52), N74 (= N76), G75 (= G77), T324 (≠ R349), R327 (vs. gap)
- binding 5-oxo-l-norleucine: C1 (≠ A5), R48 (= R51), V51 (= V54), V52 (≠ I55), Y73 (≠ F75), N74 (= N76), G75 (= G77), E76 (= E78), V95 (≠ S100), D96 (= D101)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
28% identity, 48% coverage: 67:391/673 of query aligns to 64:360/500 of 1jgtB
- active site: A73 (≠ N76), G74 (= G77), D319 (≠ I347), Y345 (≠ E374)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ Y271), L245 (= L272), S246 (= S273), G248 (= G275), I249 (≠ L276), D250 (= D277), S251 (= S278), S269 (≠ R299), M270 (≠ F300), L327 (= L355), G344 (= G373), Y345 (≠ E374), D348 (= D377)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A351), Y345 (≠ E374), G346 (= G375), D348 (= D377), I349 (≠ E378), M354 (≠ L385)
- binding magnesium ion: D250 (= D277), D348 (= D377)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 48% coverage: 67:391/673 of query aligns to 56:347/491 of 1mc1A
- active site: A65 (≠ N76), G66 (= G77), D306 (≠ I347), Y332 (≠ E374)
- binding adenosine monophosphate: V231 (≠ Y271), S233 (= S273), S238 (= S278), S256 (≠ R299), M257 (≠ F300), G331 (= G373)
- binding magnesium ion: D237 (= D277), D335 (= D377)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ A351), Y332 (≠ E374), G333 (= G375), I336 (≠ E378)
- binding pyrophosphate 2-: S233 (= S273), G235 (= G275), D237 (= D277), S238 (= S278), D335 (= D377)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 48% coverage: 67:391/673 of query aligns to 60:352/496 of 1mbzA
- active site: A69 (≠ N76), G70 (= G77), D311 (≠ I347), Y337 (≠ E374)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ Y271), L237 (= L272), S238 (= S273), S243 (= S278), S261 (≠ R299), M262 (≠ F300), Y315 (≠ A351), L319 (= L355), G336 (= G373), Y337 (≠ E374), G338 (= G375), D340 (= D377), I341 (≠ E378)
- binding magnesium ion: D242 (= D277), D340 (= D377)
- binding pyrophosphate 2-: S238 (= S273), G240 (= G275), D242 (= D277), S243 (= S278), D340 (= D377)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 48% coverage: 67:391/673 of query aligns to 61:351/485 of 1mb9A
- active site: A70 (≠ N76), G71 (= G77), D310 (≠ I347), Y336 (≠ E374)
- binding adenosine monophosphate: V235 (≠ Y271), L236 (= L272), S242 (= S278), S260 (≠ R299), M261 (≠ F300), Y314 (≠ A351), L318 (= L355), G335 (= G373), Y336 (≠ E374)
- binding adenosine-5'-triphosphate: V235 (≠ Y271), L236 (= L272), S237 (= S273), G239 (= G275), D241 (= D277), S242 (= S278), S260 (≠ R299), M261 (≠ F300), L318 (= L355), G335 (= G373), D339 (= D377)
- binding magnesium ion: D241 (= D277), D339 (= D377)
- binding pyrophosphate 2-: S237 (= S273), G239 (= G275), D241 (= D277), S242 (= S278), D339 (= D377)
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)
26% identity, 34% coverage: 70:299/673 of query aligns to 182:392/561 of Q9STG9
- H187 (≠ F75) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ C146) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P147) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
- G371 (≠ S279) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734.
Sites not aligning to the query:
- 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)
26% identity, 34% coverage: 70:299/673 of query aligns to 96:306/460 of 6lbpA
Sites not aligning to the query:
Query Sequence
>YP_004144523.1 NCBI__GCF_000185905.1:YP_004144523.1
MCGIAGIVALNAAAEPPSRAALLRMAAALSHRGPDESGVYRDRRAGLAHTRLSVIDLSTG
QQPLADTGDTTWIVFNGEIFNYVELREQLMALGHRFRTRSDTEVIVHAYRAWGVAAFERL
NGQWALAIWDSLTGRLVLSRDRFGICPLHLCEHAGRLHFASEVKAIFAADPAIPRAFDPA
GIDQTFTLWTVVPPQGVFQGVKELTPGHVRIYDNGSVREHAFWKPCYPEIADQAHGTFTG
SLDDAVDEVRSALQAATALRMVKADVPVGCYLSGGLDSSLVAMLGRRFAGAPFQTFSLRF
ADAEYDETRYQRLVASASGGEHHEVMVSRGDIAEVFPDVIRHAERPILRTAPAPLFLLSR
LVREHGIKVVLTGEGADEMFAGYDLFREGKVRRFWGRQPASARRARLLERLYPYLSRSPV
KQQAMARQFFGLGIHAFGAPGFAHDTRWRTTSAIKRLFSAGMHAEAARHDVVADLLGRLP
EEFPRWGPLAQDQYLEIRTLMSGYLLSSQGDRMLMAHSVEGRFPFLDDRLVALANSLPPD
YKLRILDEKHVLKRVAKSIVPAEVVARKKQPYRAPNALCFTGDGAPAYVREALSETALRA
ANVFDPNSVARLLDKCAAKTGDGDLSNSDNMALVGVLSTQLLHQQFVASRPSSAHAVDLR
IDVDHLHREEVLV
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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