SitesBLAST
Comparing WP_011371822.1 NCBI__GCF_000012965.1:WP_011371822.1 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)
33% identity, 64% coverage: 1:371/583 of query aligns to 1:366/554 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 (= H23) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D27) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y73) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ R95) mutation to H: Little effect on the kinetic properties.
- E349 (= E354) 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)
34% identity, 63% coverage: 7:371/583 of query aligns to 13:349/497 of 1ct9A
- active site: L50 (= L44), N74 (= N67), G75 (= G68), T305 (≠ M327), R308 (≠ S330), E332 (= E354)
- binding adenosine monophosphate: L232 (= L250), L233 (= L251), S234 (= S252), S239 (= S257), A255 (≠ S276), V256 (≠ I277), D263 (≠ E287), M316 (≠ L338), S330 (= S352), G331 (= G353), E332 (= E354)
- binding glutamine: R49 (= R43), L50 (= L44), I52 (= I46), V53 (≠ I47), N74 (= N67), G75 (= G68), E76 (= E69), D98 (= D89)
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, 62% coverage: 1:363/583 of query aligns to 1:365/557 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)
30% identity, 62% coverage: 1:363/583 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 (vs. gap) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ I204) to E: in dbSNP:rs1049674
- F362 (≠ L351) 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, 60% coverage: 16:363/583 of query aligns to 16:361/509 of 6gq3A
- active site: L49 (= L44), N74 (= N67), G75 (= G68), T324 (≠ M327), R327 (≠ S330)
- binding 5-oxo-l-norleucine: R48 (= R43), V51 (≠ I46), V52 (≠ I47), Y73 (≠ F66), N74 (= N67), G75 (= G68), E76 (= E69), V95 (≠ S88), D96 (= D89)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
25% identity, 53% coverage: 3:313/583 of query aligns to 10:303/500 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
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
24% identity, 50% coverage: 24:313/583 of query aligns to 20:290/491 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
1mb9A Beta-lactam synthetase complexed with atp (see paper)
25% identity, 50% coverage: 24:313/583 of query aligns to 25:294/485 of 1mb9A
- active site: A70 (≠ N67), G71 (= G68)
- binding adenosine monophosphate: V235 (≠ L250), L236 (= L251), S242 (= S257), S260 (= S276), M261 (≠ I277)
- binding adenosine-5'-triphosphate: V235 (≠ L250), L236 (= L251), S237 (= S252), G239 (= G254), D241 (= D256), S242 (= S257), S260 (= S276), M261 (≠ I277)
- binding magnesium ion: D241 (= D256)
- binding pyrophosphate 2-: S237 (= S252), G239 (= G254), D241 (= D256), S242 (= S257)
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)
24% identity, 50% coverage: 24:313/583 of query aligns to 24:295/496 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
1q19A Carbapenam synthetase (see paper)
28% identity, 52% coverage: 68:370/583 of query aligns to 56:367/500 of 1q19A
- active site: G56 (= G68), L318 (≠ D329), E321 (≠ C332), Y344 (≠ E354)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L250), L244 (= L251), S245 (= S252), D249 (= D256), S250 (= S257), S268 (= S276), I269 (= I277), T342 (≠ S352), G343 (= G353), D347 (= D357)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E354), G345 (= G355), L348 (≠ E358)
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)
28% identity, 52% coverage: 68:370/583 of query aligns to 57:368/503 of Q9XB61
- 244:251 (vs. 250:257, 88% identical) binding
- I270 (= I277) binding
- GYGSD 344:348 (≠ GEGSD 353:357) binding
- Y345 (≠ E354) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G355) 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
>WP_011371822.1 NCBI__GCF_000012965.1:WP_011371822.1
MCGIIGSTEINFNHNEVLNSLKHRGEDYQNYIIQNEMFFAHTRLSIIDLDEEANQPMIFD
EITLVFNGEIYNYKELIKEFSLECVTKSDSEVLIRLYQKFGFDFLNSLEGMFAFCIYDKE
KNLFFCARDRFGKKPLYYYCEKGKFYFASEIKAILKMLKTTPKLNEEALWQYLALQSPQG
ENTFYSGVKKLPASSYLLHQNSDIKVSTYYSLADIKITHYDEKQILKDVEKLLNDAVQKR
LVGDVEVATLLSGGLDSSFITALYAKKSKHKVHTFSIGYDEHKHYCELGFAKAASEYIGT
IHHEYKISKDEYLEAIEKVLEHLDEPMADSACIPTYILSKEIHNQGFKVCLSGEGSDESF
LGYDNYFKMLNYYHLKNPQKTPFDLTKEWEYNNRRLNNQQVYQSSGETFTYAQLQRLFSK
KIAPILHPYVSTYPPEQWLTYIDFSIWIAEVLMTKVDRMSMAHSLELRAPFLDHHLVEYL
LGVESSIKIGDTNKAILKKIARNYLPNSIIDRRKKGFSSPFIEWLYDAHSEEILNLLLDV
NKQLGIFNDDFLTFLYEEGKRGHFKQHVYSLYIFCRWYKKVYM
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