SitesBLAST
Comparing WP_019894569.1 NCBI__GCF_000384235.1:WP_019894569.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
29% identity, 82% coverage: 30:535/618 of query aligns to 30:433/497 of 1ct9A
- active site: L50 (= L50), N74 (= N73), G75 (= G74), T305 (vs. gap), R308 (≠ Q357), E332 (≠ Q380), M366 (≠ L466)
- binding adenosine monophosphate: L232 (= L275), L233 (= L276), S234 (= S277), S239 (= S282), A255 (≠ S301), V256 (≠ I302), D263 (≠ E309), M316 (≠ L365), S330 (= S378), G331 (= G379), E332 (≠ Q380)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ I53), N74 (= N73), G75 (= G74), E76 (≠ C75), D98 (= D98)
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)
29% identity, 87% coverage: 1:535/618 of query aligns to 1:453/554 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 (vs. gap) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y79) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K104) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q380) 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)
29% identity, 80% coverage: 23:516/618 of query aligns to 24:441/557 of P78753
- S391 (≠ Q443) 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)
28% identity, 63% coverage: 1:392/618 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 (≠ G229) to E: in dbSNP:rs1049674
- F362 (≠ M377) 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, 63% coverage: 2:392/618 of query aligns to 1:364/509 of 6gq3A
- active site: W4 (≠ C5), L49 (= L50), N74 (= N73), G75 (= G74), T324 (≠ M354), R327 (≠ Q357)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R49), V51 (≠ I52), V52 (≠ I53), Y73 (≠ F72), N74 (= N73), G75 (= G74), E76 (≠ C75), V95 (≠ S97), D96 (= D98)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 52% coverage: 69:388/618 of query aligns to 69:353/500 of 1jgtB
- active site: A73 (≠ N73), G74 (= G74), D319 (≠ M354), Y345 (≠ Q380)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L275), L245 (= L276), S246 (= S277), G248 (= G279), I249 (≠ L280), D250 (= D281), S251 (= S282), S269 (= S301), M270 (≠ I302), L327 (≠ F362), G344 (= G379), Y345 (≠ Q380), D348 (= D383)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ D358), Y345 (≠ Q380), G346 (= G381), D348 (= D383), I349 (≠ E384)
- binding magnesium ion: D250 (= D281), D348 (= D383)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 52% coverage: 69:388/618 of query aligns to 65:345/496 of 1mbzA
- active site: A69 (≠ N73), G70 (= G74), D311 (≠ M354), Y337 (≠ Q380)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L275), L237 (= L276), S238 (= S277), S243 (= S282), S261 (= S301), M262 (≠ I302), Y315 (≠ D358), L319 (≠ F362), G336 (= G379), Y337 (≠ Q380), G338 (= G381), D340 (= D383), I341 (≠ E384)
- binding magnesium ion: D242 (= D281), D340 (= D383)
- binding pyrophosphate 2-: S238 (= S277), G240 (= G279), D242 (= D281), S243 (= S282), D340 (= D383)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 52% coverage: 69:388/618 of query aligns to 61:340/491 of 1mc1A
- active site: A65 (≠ N73), G66 (= G74), D306 (≠ M354), Y332 (≠ Q380)
- binding adenosine monophosphate: V231 (≠ L275), S233 (= S277), S238 (= S282), S256 (= S301), M257 (≠ I302), G331 (= G379)
- binding magnesium ion: D237 (= D281), D335 (= D383)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ D358), Y332 (≠ Q380), G333 (= G381), I336 (≠ E384)
- binding pyrophosphate 2-: S233 (= S277), G235 (= G279), D237 (= D281), S238 (= S282), D335 (= D383)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 52% coverage: 69:388/618 of query aligns to 66:344/485 of 1mb9A
- active site: A70 (≠ N73), G71 (= G74), D310 (≠ M354), Y336 (≠ Q380)
- binding adenosine monophosphate: V235 (≠ L275), L236 (= L276), S242 (= S282), S260 (= S301), M261 (≠ I302), Y314 (≠ D358), L318 (≠ F362), G335 (= G379), Y336 (≠ Q380)
- binding adenosine-5'-triphosphate: V235 (≠ L275), L236 (= L276), S237 (= S277), G239 (= G279), D241 (= D281), S242 (= S282), S260 (= S301), M261 (≠ I302), L318 (≠ F362), G335 (= G379), D339 (= D383)
- binding magnesium ion: D241 (= D281), D339 (= D383)
- binding pyrophosphate 2-: S237 (= S277), G239 (= G279), D241 (= D281), S242 (= S282), D339 (= D383)
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
24% identity, 61% coverage: 60:436/618 of query aligns to 42:416/500 of 1q19A
- active site: G56 (= G74), L318 (≠ M354), E321 (≠ Q357), Y344 (≠ Q380), E379 (vs. gap)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L275), L244 (= L276), S245 (= S277), D249 (= D281), S250 (= S282), S268 (= S301), I269 (= I302), T342 (≠ S378), G343 (= G379), D347 (= D383)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q380), G345 (= G381), L348 (≠ E384), R373 (vs. gap), E379 (vs. gap)
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)
24% identity, 61% coverage: 60:436/618 of query aligns to 43:417/503 of Q9XB61
- 244:251 (vs. 275:282, 88% identical) binding ATP
- I270 (= I302) binding ATP
- GYGSD 344:348 (≠ GQGAD 379:383) binding ATP
- Y345 (≠ Q380) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G381) binding substrate
- Q371 (≠ K401) binding substrate
- R374 (vs. gap) binding substrate
- E380 (vs. gap) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
Sites not aligning to the query:
- 421 binding ATP
- 443 mutation K->A,M: Loss of activity.
- 444:446 binding ATP
2j6hA E. Coli glucosamine-6-p synthase in complex with glucose-6p and 5-oxo- l-norleucine (see paper)
27% identity, 26% coverage: 2:164/618 of query aligns to 1:197/608 of 2j6hA
- active site: C1 (= C2), R26 (= R30), G27 (= G31), W74 (≠ L50), N98 (= N73), G99 (= G74)
- binding 5-oxo-l-norleucine: C1 (= C2), R73 (= R49), W74 (≠ L50), T76 (≠ I52), H86 (≠ Q61), N98 (= N73), G99 (= G74), D123 (= D98)
Sites not aligning to the query:
- active site: 248, 481, 485, 488, 504, 603
- binding glucose-6-phosphate: 302, 347, 348, 349, 352, 399, 401, 488
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
27% identity, 26% coverage: 2:164/618 of query aligns to 1:197/608 of 4amvA
Sites not aligning to the query:
- active site: 248, 481, 485, 488, 504, 603
- binding fructose -6-phosphate: 301, 302, 303, 347, 348, 349, 352, 401, 485, 488
1jxaA Glucosamine 6-phosphate synthase with glucose 6-phosphate (see paper)
27% identity, 26% coverage: 2:164/618 of query aligns to 1:197/608 of 1jxaA
Sites not aligning to the query:
- active site: 248, 481, 485, 488, 504, 603
- binding glucose-6-phosphate: 302, 303, 347, 348, 349, 352, 401, 485, 488
1xfgA Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate (see paper)
27% identity, 26% coverage: 2:164/618 of query aligns to 1:197/238 of 1xfgA
- active site: C1 (= C2), R26 (= R30), G27 (= G31), W74 (≠ L50), N98 (= N73), G99 (= G74)
- binding glutamine hydroxamate: C1 (= C2), R73 (= R49), W74 (≠ L50), T76 (≠ I52), H86 (≠ Q61), N98 (= N73), G99 (= G74), D123 (= D98)
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
27% identity, 26% coverage: 2:164/618 of query aligns to 1:197/238 of 1xffA
- active site: C1 (= C2), R26 (= R30), G27 (= G31), W74 (≠ L50), N98 (= N73), G99 (= G74)
- binding glutamic acid: C1 (= C2), R73 (= R49), W74 (≠ L50), T76 (≠ I52), H86 (≠ Q61), N98 (= N73), G99 (= G74), D123 (= D98)
Query Sequence
>WP_019894569.1 NCBI__GCF_000384235.1:WP_019894569.1
MCGICGEIYWDGQKASEATLAPMLEKLAKRGPDDGGIWLQNQVGLGHRRLSIIDLSDAGH
QPMVDEELTLVFNGCIYNYVALREQLIELGHAFRSHSDTEVILKAYRQWGMECVTRFEGM
FAFALWDDHQHQLMLARDRFGIKPLYYAPVEGGVRFASNTQALLAAGGVNIDLDPVGLHH
QFTLHGVVPAPHTVLKGVRKLAPGQWMTVNPDGQMYQRSWWHLKAERPGPDHPSSRLQAL
SGVTDHQAWVEAVHDTLKEAVHKRLTASDVPVGVLLSGGLDSSLIVALLDEAGVEDIRTF
SIGFEDVPEEKGSEFDYSDQVVERFQTRHQKFLIPNEAVLPRLQEAVDAMSEPMFAQDAV
AFYLLSEQVSKEVKVVMSGQGADEVFGGYFWYPQMAQAAEKLGPEAQAVDAFAPFYFDRD
HAEWSEMIHPDYHIRDVTTEWVQDRLSEEDADTFIDQVLRLDASHLIVDDPVKRVDNMTM
AWGLEARVPFLDHSLVEVAMTAPPETKLQDFKYLLKAVARGRVPDSVIDRPKGYFPMPAL
KYVRGPFYDMMRSVLTSEVAQKRGLFQSDYIERLLAEPEADASFTRIQGSKLWHAALLEL
WLQTHVDPYRERNLCSAE
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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