SitesBLAST
Comparing PP_1750 FitnessBrowser__Putida:PP_1750 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)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
26% identity, 86% coverage: 35:545/595 of query aligns to 30:445/497 of 1ct9A
- active site: L50 (= L55), N74 (= N80), G75 (= G81), T305 (≠ I356), R308 (vs. gap), E332 (≠ Q376), M366 (≠ L457)
- binding adenosine monophosphate: L232 (= L271), L233 (= L272), S234 (= S273), S239 (= S278), A255 (≠ S297), V256 (≠ I298), D263 (≠ E310), M316 (≠ L361), S330 (= S374), G331 (= G375), E332 (≠ Q376)
- binding glutamine: R49 (= R54), L50 (= L55), I52 (= I57), V53 (≠ M58), N74 (= N80), G75 (= G81), E76 (≠ A82), D98 (= D105)
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)
25% identity, 92% coverage: 1:545/595 of query aligns to 1:465/554 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 (= D38) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ F86) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K111) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q376) 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)
27% identity, 92% coverage: 1:545/595 of query aligns to 1:480/557 of P78753
- S391 (≠ D452) modified: Phosphoserine
Sites not aligning to the query:
- 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)
25% identity, 83% coverage: 32:526/595 of query aligns to 24:470/561 of P08243
- V210 (≠ A197) 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:
- 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
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
26% identity, 62% coverage: 32:397/595 of query aligns to 23:373/509 of 6gq3A
- active site: L49 (= L55), N74 (= N80), G75 (= G81), T324 (≠ S352), R327 (≠ H353)
- binding 5-oxo-l-norleucine: R48 (= R54), V51 (≠ I57), V52 (≠ M58), Y73 (≠ F79), N74 (= N80), G75 (= G81), E76 (≠ A82), V95 (≠ G104), D96 (= D105)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 55% coverage: 79:407/595 of query aligns to 72:375/500 of 1jgtB
- active site: A73 (≠ N80), G74 (= G81), D319 (= D354), Y345 (≠ Q376)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L271), L245 (= L272), S246 (= S273), G248 (= G275), I249 (≠ V276), D250 (= D277), S251 (= S278), S269 (= S297), M270 (≠ I298), L327 (vs. gap), G344 (= G375), Y345 (≠ Q376), D348 (= D379)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ F358), Y345 (≠ Q376), G346 (= G377), D348 (= D379), I349 (≠ E380), M354 (≠ Y385), D370 (≠ R402)
- binding magnesium ion: D250 (= D277), D348 (= D379)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 55% coverage: 79:407/595 of query aligns to 64:362/491 of 1mc1A
- active site: A65 (≠ N80), G66 (= G81), D306 (= D354), Y332 (≠ Q376)
- binding adenosine monophosphate: V231 (≠ L271), S233 (= S273), S238 (= S278), S256 (= S297), M257 (≠ I298), G331 (= G375)
- binding magnesium ion: D237 (= D277), D335 (= D379)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ F358), Y332 (≠ Q376), G333 (= G377), I336 (≠ E380), D357 (≠ R402)
- binding pyrophosphate 2-: S233 (= S273), G235 (= G275), D237 (= D277), S238 (= S278), D335 (= D379)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 55% coverage: 79:407/595 of query aligns to 68:367/496 of 1mbzA
- active site: A69 (≠ N80), G70 (= G81), D311 (= D354), Y337 (≠ Q376)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L271), L237 (= L272), S238 (= S273), S243 (= S278), S261 (= S297), M262 (≠ I298), Y315 (≠ F358), L319 (vs. gap), G336 (= G375), Y337 (≠ Q376), G338 (= G377), D340 (= D379), I341 (≠ E380), D362 (≠ R402)
- binding magnesium ion: D242 (= D277), D340 (= D379)
- binding pyrophosphate 2-: S238 (= S273), G240 (= G275), D242 (= D277), S243 (= S278), D340 (= D379)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 55% coverage: 79:407/595 of query aligns to 69:366/485 of 1mb9A
- active site: A70 (≠ N80), G71 (= G81), D310 (= D354), Y336 (≠ Q376)
- binding adenosine monophosphate: V235 (≠ L271), L236 (= L272), S242 (= S278), S260 (= S297), M261 (≠ I298), Y314 (≠ F358), L318 (vs. gap), G335 (= G375), Y336 (≠ Q376)
- binding adenosine-5'-triphosphate: V235 (≠ L271), L236 (= L272), S237 (= S273), G239 (= G275), D241 (= D277), S242 (= S278), S260 (= S297), M261 (≠ I298), L318 (vs. gap), G335 (= G375), D339 (= D379)
- binding magnesium ion: D241 (= D277), D339 (= D379)
- binding pyrophosphate 2-: S237 (= S273), G239 (= G275), D241 (= D277), S242 (= S278), D339 (= D379)
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
31% identity, 20% coverage: 268:384/595 of query aligns to 240:352/500 of 1q19A
- active site: L318 (≠ M350), E321 (≠ H353), Y344 (≠ Q376)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L271), L244 (= L272), S245 (= S273), D249 (= D277), S250 (= S278), S268 (= S297), I269 (= I298), T342 (≠ S374), G343 (= G375), D347 (= D379)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q376), G345 (= G377), L348 (≠ E380)
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)
31% identity, 20% coverage: 268:384/595 of query aligns to 241:353/503 of Q9XB61
- 244:251 (vs. 271:278, 75% identical) binding
- I270 (= I298) binding
- GYGSD 344:348 (≠ GQGAD 375:379) binding
- Y345 (≠ Q376) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G377) binding
Sites not aligning to the query:
- 371 binding
- 374 binding
- 380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
- 421 binding
- 443 mutation K->A,M: Loss of activity.
- 444:446 binding
Query Sequence
>PP_1750 FitnessBrowser__Putida:PP_1750
MCGLAGELRFTPIDQAPRPADLAAVERITHHLAPRGPDAWGFHSQGPIALGHRRLKIMDL
SDGSAQPMVDNTLGLSLAFNGAIYNFPELREELQALGYSFWSDGDTEVLLKGYHAWGAAL
LPKLNGMFALAIWERDNQRLFLARDRLGVKPLYLSRNGERLRFASTLPALLKGGDIDPML
DPVALNHYLNFHAVVPAPRTLLANVQKLEPGTWMRIDRHGEVERQVWWQLHYGPHPDERE
LDLEGWTTRVLDATRDAVAIRQRAAVDVGVLLSGGVDSSLLVGLLREVGVDDLSTFSIGF
EDAGGERGDEFQYSDLIAKHYGTRHHQLRIAEHEIIDQLPAAFRAMSEPMVSHDCIAFYL
LSREVAKHCKGVQSGQGADELFAGYHWYPQVDGADDAYAAYREAFFDRSHAEYRDTVQAP
WLLETDAAGDFVREHFARPGAPAAVDKALRLDSTVMLVDDPVKRVDNMTMAWGLEARTPF
LDYRLVELSARIPARFKLPDGGKQVLKQAARRVIPHEVIDRKKGYFPVPGLKHLEGATLG
WVRELLTDPSQDRGLFNPTMLDRLLSNPHGQLTPLRGSKLWQLAALNLWLSEQGI
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