SitesBLAST
Comparing WP_026606747.1 NCBI__GCF_000427445.1:WP_026606747.1 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)
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, 60% coverage: 1:395/655 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 (vs. gap) to E: in dbSNP:rs1049674
- F362 (≠ L380) 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, 60% coverage: 2:395/655 of query aligns to 1:364/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L54), N74 (= N79), G75 (= G80), T324 (≠ P356), R327 (≠ D359)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R53), V51 (= V56), V52 (= V57), Y73 (≠ F78), N74 (= N79), G75 (= G80), E76 (= E81), V95 (≠ S100), D96 (= D110)
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
29% identity, 55% coverage: 31:392/655 of query aligns to 30:358/554 of P22106
- 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 (= H85) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A116) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D383) 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
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)
28% identity, 56% coverage: 25:392/655 of query aligns to 24:365/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 489 modified: Phosphoserine
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
39% identity, 22% coverage: 31:176/655 of query aligns to 29:164/497 of 1ct9A
Sites not aligning to the query:
- active site: 1, 305, 308, 332, 366
- binding adenosine monophosphate: 232, 233, 234, 239, 255, 256, 263, 316, 330, 331, 332
- binding glutamine: 1
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 41% coverage: 77:347/655 of query aligns to 71:307/500 of 1jgtB
Sites not aligning to the query:
- active site: 319, 345, 379, 440
- binding diphosphomethylphosphonic acid adenosyl ester: 327, 344, 345, 348, 420, 440
- binding n2-(carboxyethyl)-l-arginine: 323, 345, 346, 348, 349, 354, 370, 379
- binding magnesium ion: 348
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 41% coverage: 77:347/655 of query aligns to 68:298/485 of 1mb9A
- active site: A70 (≠ N79), G71 (= G80)
- binding adenosine monophosphate: V235 (≠ F281), L236 (= L282), S242 (= S288), S260 (≠ T307), M261 (≠ I308)
- binding adenosine-5'-triphosphate: V235 (≠ F281), L236 (= L282), S237 (= S283), G239 (= G285), D241 (= D287), S242 (= S288), S260 (≠ T307), M261 (≠ I308)
- binding magnesium ion: D241 (= D287)
- binding pyrophosphate 2-: S237 (= S283), G239 (= G285), D241 (= D287), S242 (= S288)
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)
27% identity, 41% coverage: 77:347/655 of query aligns to 67:299/496 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
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)
28% identity, 44% coverage: 105:391/655 of query aligns to 72:353/503 of Q9XB61
- 244:251 (vs. 281:288, 75% identical) binding
- I270 (= I308) binding
- GYGSD 344:348 (≠ GDAGD 382:386) binding
- Y345 (≠ D383) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (≠ A384) 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
1q19A Carbapenam synthetase (see paper)
28% identity, 44% coverage: 105:391/655 of query aligns to 71:352/500 of 1q19A
- active site: L318 (vs. gap), E321 (≠ Q362), Y344 (≠ D383)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F281), L244 (= L282), S245 (= S283), D249 (= D287), S250 (= S288), S268 (≠ T307), I269 (= I308), T342 (≠ S381), G343 (= G382), D347 (= D386)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D383), G345 (≠ A384), L348 (≠ E387)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 41% coverage: 77:347/655 of query aligns to 63:294/491 of 1mc1A
Sites not aligning to the query:
- active site: 306, 332, 366, 427
- binding adenosine monophosphate: 331, 427, 430
- binding magnesium ion: 335
- binding deoxyguanidinoproclavaminic acid: 310, 332, 333, 336, 357, 366, 427
- binding pyrophosphate 2-: 335, 407, 427, 428
Query Sequence
>WP_026606747.1 NCBI__GCF_000427445.1:WP_026606747.1
MCGVAGFLGSGGVGPDEWPSLLNRMGAAIAHRGPDSCGIWTDADAGIGLAHRRLAVVDLS
PAGRQPMISPSGRFVIIFNGEIYNHVELRMELDAALEKKSQSIGWRGHSDTETLLAGFDV
WGVETTLKRSVGMFAIALWDKQRRELVLARDRMGEKPLYYGWCNGVFLFGSELKVIKAHP
AFRGEIDRDAVALLLKHSYIPAPYSIYKGVRKLKPGMLLRVTASSAAFDDPVVYWSFCEA
AESALANPFTGSDSEAVEALEALLRRSVSNQMLADVPLGAFLSGGVDSSTVVALMQAQSS
QPIKTFTIGFDESAYNEAKYARAVAKHLGTQHTELYVSPKRAMEVIPLLPALYDEPFSDS
SQIPTYLVSQMARKHVTVSLSGDAGDELFGGYTRYLLARTLWAWAGKLPGPARCKVASFL
SAASPSFWDKIYEKASHILPQRFRSTHFGHKIHKLAEIFSATSADDIYDGLISHWRRPTD
TVMGATESPSLMSLLKKADSFESFEDRMMAADSLSYLPDDILVKVDRAAMGVSLETRVPF
LDHRVLEFAWRLPLRMKMRKGESKWILRQVLYKHVPPDLIERPKMGFGVPIDDWLRGPLR
DWAEGLLNEQRLRREGYFYAEPIRRKWDEHQSGQHNWQYHLWDVLMFQAWLERES
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