SitesBLAST
Comparing WP_012045542.1 NCBI__GCF_000015165.1:WP_012045542.1 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 9 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)
30% identity, 59% coverage: 1:389/656 of query aligns to 1:358/554 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 (= H85) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A112) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D380) 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)
31% identity, 56% coverage: 24:389/656 of query aligns to 22:341/497 of 1ct9A
- active site: L50 (= L54), N74 (= N79), G75 (= G80), T305 (≠ S358), R308 (vs. gap), E332 (≠ D380)
- binding adenosine monophosphate: L232 (≠ F278), L233 (= L279), S234 (= S280), S239 (= S285), A255 (≠ S304), V256 (≠ I305), D263 (≠ E314), M316 (≠ V365), S330 (= S378), G331 (= G379), E332 (≠ D380)
- binding glutamine: R49 (= R53), L50 (= L54), I52 (= I56), V53 (≠ L57), N74 (= N79), G75 (= G80), E76 (= E81), D98 (= D106)
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)
30% identity, 59% coverage: 1:389/656 of query aligns to 1:374/561 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 (≠ T238) to E: in dbSNP:rs1049674
- F362 (≠ L377) 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)
30% identity, 59% coverage: 2:389/656 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L54), N74 (= N79), G75 (= G80), T324 (≠ P353), R327 (≠ D356)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R53), V51 (≠ I56), V52 (≠ L57), Y73 (≠ F78), N74 (= N79), G75 (= G80), E76 (= E81), V95 (≠ S105), D96 (= D106)
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)
29% identity, 59% coverage: 1:389/656 of query aligns to 1:365/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 489 modified: Phosphoserine
1jgtB Crystal structure of beta-lactam synthetase (see paper)
30% identity, 42% coverage: 75:347/656 of query aligns to 69:307/500 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
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
30% identity, 42% coverage: 75:347/656 of query aligns to 65:299/496 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
1mb9A Beta-lactam synthetase complexed with atp (see paper)
31% identity, 42% coverage: 75:347/656 of query aligns to 66:298/485 of 1mb9A
- active site: A70 (≠ N79), G71 (= G80)
- binding adenosine monophosphate: V235 (≠ F278), L236 (= L279), S242 (= S285), S260 (= S304), M261 (≠ I305)
- binding adenosine-5'-triphosphate: V235 (≠ F278), L236 (= L279), S237 (= S280), G239 (= G282), D241 (= D284), S242 (= S285), S260 (= S304), M261 (≠ I305)
- binding magnesium ion: D241 (= D284)
- binding pyrophosphate 2-: S237 (= S280), G239 (= G282), D241 (= D284), S242 (= S285)
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
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
30% identity, 42% coverage: 75:347/656 of query aligns to 61:294/491 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_012045542.1 NCBI__GCF_000015165.1:WP_012045542.1
MCGIAGLFRPGGADDSALAGIVGRMTAALAHRGPDASGSWVSGRQGIALGQRRLAILDLS
EAGAQPMHSACGRYTITFNGEIYNHLDLRAELEDAAAAPNWRGHSDTETLLAAIRQWGLV
PALQRLIGMFAFALWDAETRQLILARDRFGEKPLFYGWSGADLVFGSELKALAAHPGWAP
SLDRAALTDFMRYSYVPAPATIWRDVRKLPPASFVAFVADAGPGTSPTAQSYWSLRDTVV
AAQGDRISGESEAIARLEQLLSTAVKRQCLSDVPLGAFLSGGVDSSTIVALMQAQASQPV
RTFSIGFAEGGYNEAEDARKVAQHLGTDHTELYVDARTAMEVVPKLPRIYDEPFADSSQI
PTHLVAQLARRHVTVALSGDAGDELFGGYNRHVWGSALQARLGRVPMPLRRAIGAALGAI
APEPADTLLNMLQPVLPARLRVRHAGDQVAKLARIVAADGFDGLYRTLCSIDQDPRATVV
AGEERASWAASEMKQLRGQISLLDRMTLADSLSYLSDDILQKVDRAAMAVALETRVPFLD
RDVVEFSTRVPASMKVRDGRGKWLVRQVLYRHVPADMIDRPKTGFSIPLDAWLRGPLKSW
AGDLLSPARLKRQGLFAPTRVTRMFEEHLSRRHNHAYWLWNVLMAEAWYDEWGRAG
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