SitesBLAST
Comparing 5210610 FitnessBrowser__PV4:5210610 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)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
30% identity, 83% coverage: 29:518/590 of query aligns to 30:433/497 of 1ct9A
- active site: L50 (= L49), N74 (= N74), G75 (= G75), T305 (≠ I347), R308 (vs. gap), E332 (≠ Q367), M366 (≠ P432)
- binding adenosine monophosphate: L232 (= L262), L233 (= L263), S234 (= S264), S239 (= S269), A255 (≠ S288), V256 (≠ I289), D263 (= D296), M316 (≠ L352), S330 (= S365), G331 (= G366), E332 (≠ Q367)
- binding glutamine: R49 (= R48), L50 (= L49), I52 (= I51), V53 (≠ I52), N74 (= N74), G75 (= G75), E76 (≠ C76), D98 (= D99)
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)
32% identity, 64% coverage: 1:379/590 of query aligns to 1:361/554 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 (= D32) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y80) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K105) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q367) 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)
28% identity, 85% coverage: 1:501/590 of query aligns to 1:443/557 of P78753
- S391 (≠ D451) 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)
26% identity, 91% coverage: 1:536/590 of query aligns to 1:487/561 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 (= V209) to E: in dbSNP:rs1049674
- F362 (≠ Q364) 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: 2:517/590 of query aligns to 1:456/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L49), N74 (= N74), G75 (= G75), T324 (≠ S343), R327 (≠ H344)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R48), V51 (≠ I51), V52 (≠ I52), Y73 (≠ F73), N74 (= N74), G75 (= G75), E76 (≠ C76), V95 (≠ S98), D96 (= D99)
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 52% coverage: 70:377/590 of query aligns to 66:346/485 of 1mb9A
- active site: A70 (≠ N74), G71 (= G75), D310 (= D345), Y336 (≠ Q367)
- binding adenosine monophosphate: V235 (≠ L262), L236 (= L263), S242 (= S269), S260 (= S288), M261 (≠ I289), Y314 (≠ F349), L318 (vs. gap), G335 (= G366), Y336 (≠ Q367)
- binding adenosine-5'-triphosphate: V235 (≠ L262), L236 (= L263), S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), S260 (= S288), M261 (≠ I289), L318 (vs. gap), G335 (= G366), D339 (= D370)
- binding magnesium ion: D241 (= D268), D339 (= D370)
- binding pyrophosphate 2-: S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), D339 (= D370)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 52% coverage: 70:377/590 of query aligns to 65:347/496 of 1mbzA
- active site: A69 (≠ N74), G70 (= G75), D311 (= D345), Y337 (≠ Q367)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L262), L237 (= L263), S238 (= S264), S243 (= S269), S261 (= S288), M262 (≠ I289), Y315 (≠ F349), L319 (vs. gap), G336 (= G366), Y337 (≠ Q367), G338 (= G368), D340 (= D370), I341 (≠ E371)
- binding magnesium ion: D242 (= D268), D340 (= D370)
- binding pyrophosphate 2-: S238 (= S264), G240 (= G266), D242 (= D268), S243 (= S269), D340 (= D370)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 52% coverage: 70:377/590 of query aligns to 69:355/500 of 1jgtB
- active site: A73 (≠ N74), G74 (= G75), D319 (= D345), Y345 (≠ Q367)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L262), L245 (= L263), S246 (= S264), G248 (= G266), I249 (≠ L267), D250 (= D268), S251 (= S269), S269 (= S288), M270 (≠ I289), L327 (vs. gap), G344 (= G366), Y345 (≠ Q367), D348 (= D370)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ F349), Y345 (≠ Q367), G346 (= G368), D348 (= D370), I349 (≠ E371), M354 (≠ Y376)
- binding magnesium ion: D250 (= D268), D348 (= D370)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 52% coverage: 70:377/590 of query aligns to 61:342/491 of 1mc1A
- active site: A65 (≠ N74), G66 (= G75), D306 (= D345), Y332 (≠ Q367)
- binding adenosine monophosphate: V231 (≠ L262), S233 (= S264), S238 (= S269), S256 (= S288), M257 (≠ I289), G331 (= G366)
- binding magnesium ion: D237 (= D268), D335 (= D370)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ F349), Y332 (≠ Q367), G333 (= G368), I336 (≠ E371)
- binding pyrophosphate 2-: S233 (= S264), G235 (= G266), D237 (= D268), S238 (= S269), D335 (= D370)
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
31% identity, 20% coverage: 259:375/590 of query aligns to 240:352/500 of 1q19A
- active site: L318 (≠ M341), E321 (≠ H344), Y344 (≠ Q367)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L262), L244 (= L263), S245 (= S264), D249 (= D268), S250 (= S269), S268 (= S288), I269 (= I289), T342 (≠ S365), G343 (= G366), D347 (= D370)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q367), G345 (= G368), L348 (≠ E371)
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)
31% identity, 20% coverage: 259:375/590 of query aligns to 241:353/503 of Q9XB61
- 244:251 (vs. 262:269, 88% identical) binding
- I270 (= I289) binding
- GYGSD 344:348 (≠ GQGAD 366:370) binding
- Y345 (≠ Q367) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G368) 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
>5210610 FitnessBrowser__PV4:5210610
MCGIAGELSFTTSAKVDQVAAMLDKLAPRGPDGQGLYSLGPCCLGHRRLKIIDLSEHGAQ
PMVDAELGLTLVFNGCIYNYRALRAELSELGYHFFSHSDSEVILKAYAHWGRQCVEKFNG
MFAFAIHERDTGRLFIARDRLGIKPLYYFKDGHSLVFASSLPALLRHPVADTEIDPQSLN
HYLCFRAIVGDKTLFKQIHKLEAAHWMLVRPDGQVDHQSYWHLSPGSSLETETEETWSQQ
LEQKLFDSAKRRLEADVPVGVLLSGGLDSSLIVGLLHELGQKEIHTFSIGFDDVADEQGN
EFKYSDLIAEHYQTRHQKIVVSHSELISHLPDCVMAMSEPMVSHDVIGFYLLSKTVSQHV
KVVQSGQGADEVFGGYHWYPPMVDATAEDEAQTYQDAYFSWQYPEYQQLVAEPLLDGDHA
GDYVRRYFAHCPAETAIDKTLMLDTRVMLVDDPVKRVDNMTMAFGLEARVPFLDHELVEL
ASRIPFDLKLKEGGKYLLKQVARRIIPHQVIDRPKGYFPVPGLRNMQGPYLALAKEVFAR
PQARARGIFNMDYIDAMLASPEQQLTRFGSRLWQVTLLELWLQLHLDHES
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