SitesBLAST
Comparing WP_029908049.1 NCBI__GCF_000711315.1:WP_029908049.1 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)
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, 86% coverage: 23:541/601 of query aligns to 24:477/557 of P78753
- S391 (≠ H425) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
27% identity, 83% coverage: 25:525/601 of query aligns to 25:433/497 of 1ct9A
- active site: L50 (= L50), N74 (= N73), G75 (= G74), T305 (≠ M344), R308 (≠ Q347), E332 (≠ Q370), M366 (≠ V424)
- binding adenosine monophosphate: L232 (= L265), L233 (= L266), S234 (= S267), S239 (= S272), A255 (≠ S291), V256 (≠ I292), D263 (≠ E299), M316 (≠ L355), S330 (= S368), G331 (= G369), E332 (≠ Q370)
- 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)
26% identity, 87% coverage: 1:525/601 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 (≠ R29) 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 (≠ Q370) 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.
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)
26% identity, 87% coverage: 1:525/601 of query aligns to 1:470/561 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 (≠ N11) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ R227) to E: in dbSNP:rs1049674
- F362 (≠ M367) 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)
26% identity, 87% coverage: 2:521/601 of query aligns to 1:453/509 of 6gq3A
- active site: W4 (= W10), L49 (= L50), N74 (= N73), G75 (= G74), T324 (vs. gap), R327 (≠ Q347)
- 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)
26% identity, 52% coverage: 69:378/601 of query aligns to 69:353/500 of 1jgtB
- active site: A73 (≠ N73), G74 (= G74), D319 (≠ M344), Y345 (≠ Q370)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L265), L245 (= L266), S246 (= S267), G248 (= G269), I249 (≠ L270), D250 (= D271), S251 (= S272), S269 (= S291), M270 (≠ I292), L327 (≠ F352), G344 (= G369), Y345 (≠ Q370), D348 (= D373)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ D348), Y345 (≠ Q370), G346 (= G371), D348 (= D373), I349 (≠ E374)
- binding magnesium ion: D250 (= D271), D348 (= D373)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 52% coverage: 69:378/601 of query aligns to 65:345/496 of 1mbzA
- active site: A69 (≠ N73), G70 (= G74), D311 (≠ M344), Y337 (≠ Q370)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L265), L237 (= L266), S238 (= S267), S243 (= S272), S261 (= S291), M262 (≠ I292), Y315 (≠ D348), L319 (≠ F352), G336 (= G369), Y337 (≠ Q370), G338 (= G371), D340 (= D373), I341 (≠ E374)
- binding magnesium ion: D242 (= D271), D340 (= D373)
- binding pyrophosphate 2-: S238 (= S267), G240 (= G269), D242 (= D271), S243 (= S272), D340 (= D373)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
25% identity, 52% coverage: 69:378/601 of query aligns to 61:340/491 of 1mc1A
- active site: A65 (≠ N73), G66 (= G74), D306 (≠ M344), Y332 (≠ Q370)
- binding adenosine monophosphate: V231 (≠ L265), S233 (= S267), S238 (= S272), S256 (= S291), M257 (≠ I292), G331 (= G369)
- binding magnesium ion: D237 (= D271), D335 (= D373)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ D348), Y332 (≠ Q370), G333 (= G371), I336 (≠ E374)
- binding pyrophosphate 2-: S233 (= S267), G235 (= G269), D237 (= D271), S238 (= S272), D335 (= D373)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
25% identity, 52% coverage: 69:378/601 of query aligns to 66:344/485 of 1mb9A
- active site: A70 (≠ N73), G71 (= G74), D310 (≠ M344), Y336 (≠ Q370)
- binding adenosine monophosphate: V235 (≠ L265), L236 (= L266), S242 (= S272), S260 (= S291), M261 (≠ I292), Y314 (≠ D348), L318 (≠ F352), G335 (= G369), Y336 (≠ Q370)
- binding adenosine-5'-triphosphate: V235 (≠ L265), L236 (= L266), S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), S260 (= S291), M261 (≠ I292), L318 (≠ F352), G335 (= G369), D339 (= D373)
- binding magnesium ion: D241 (= D271), D339 (= D373)
- binding pyrophosphate 2-: S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), D339 (= D373)
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)
25% identity, 51% coverage: 74:378/601 of query aligns to 57:353/503 of Q9XB61
- 244:251 (vs. 265:272, 88% identical) binding
- I270 (= I292) binding
- GYGSD 344:348 (≠ GQGAD 369:373) binding
- Y345 (≠ Q370) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G371) 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)
25% identity, 51% coverage: 74:378/601 of query aligns to 56:352/500 of 1q19A
- active site: G56 (= G74), L318 (≠ M344), E321 (≠ Q347), Y344 (≠ Q370)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L265), L244 (= L266), S245 (= S267), D249 (= D271), S250 (= S272), S268 (= S291), I269 (= I292), T342 (≠ S368), G343 (= G369), D347 (= D373)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q370), G345 (= G371), L348 (≠ E374)
Sites not aligning to the query:
Query Sequence
>WP_029908049.1 NCBI__GCF_000711315.1:WP_029908049.1
MCGICGEIYWNGRGVSEASLTPMLKALERRGPDDGGTWIQNQVGLGHRRLSIIDLSDAGH
QPMIDNELSLVFNGCIYNYQSLRSLLIELGHEFCSHSDTEVILKAYRQWGMDCVTRFEGM
FAFAVWDDHHQQLLIARDRFGIKPLYYAPVDGGVKFASNTQALLASGDINTEIDPIGLHH
QFTLHGVIPAPYTILKGIRKLEPGHWMIVNPDGQMFKKSYWHLMAERPAGAENLNEEDWI
NRIHDSLKQAVHKRLTAADVPVGVLLSGGLDSSLIVALLAEAGVENIRTFSIGFEDVPEE
KGSEFEYSDQVVERYQTIHKKYLISNEEVLPRLPGAVDAMAEPMFGQDAVAFYLLSEQVS
KDVKVVMSGQGADEVFAGYFWYPQMAEAYEKLSPGEPPVNAFAPFYFDRTHEEWLEMVNP
KYHVHDVTSEWANDRLSEPGATTFLDQVLRLDASTLIVDDPVKRVDNMTMAWSLEARVPF
LDHDLVELTMSAPESLKRKDFKYVLKKIARGIVPDSVIDRPKGYFPMPALKYVRDDFYQW
MKDVLTSDAAKTRGIFNPDYIENLLANPENEASFTAIKGSKLWHAALLELWLQRNVDRHI
S
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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