SitesBLAST
Comparing 202285 FitnessBrowser__MR1:202285 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)
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, 60% coverage: 1:383/643 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 (≠ I231) to E: in dbSNP:rs1049674
- F362 (≠ L371) 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)
27% identity, 59% coverage: 2:383/643 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L52), N74 (= N77), G75 (= G78), T324 (≠ P347), R327 (≠ D350)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R51), V51 (≠ I54), V52 (= V55), Y73 (= Y76), N74 (= N77), G75 (= G78), E76 (= E79), V95 (≠ S102), D96 (= D103)
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
30% identity, 60% coverage: 1:383/643 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 (≠ N29) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H83) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A109) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D374) 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, 59% coverage: 5:383/643 of query aligns to 1:341/497 of 1ct9A
- active site: A1 (= A5), L50 (= L52), N74 (= N77), G75 (= G78), T305 (≠ P347), R308 (≠ D350), E332 (≠ D374)
- binding adenosine monophosphate: L232 (≠ F272), L233 (= L273), S234 (= S274), S239 (= S279), A255 (≠ S298), V256 (≠ I299), D263 (≠ E308), M316 (≠ V359), S330 (= S372), G331 (= G373), E332 (≠ D374)
- binding glutamine: A1 (= A5), R49 (= R51), L50 (= L52), I52 (= I54), V53 (= V55), N74 (= N77), G75 (= G78), E76 (= E79), D98 (= D103)
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, 56% coverage: 26:383/643 of query aligns to 27:365/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 489 modified: Phosphoserine
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 41% coverage: 78:338/643 of query aligns to 74:307/500 of 1jgtB
Sites not aligning to the query:
- active site: 73, 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
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 41% coverage: 78:338/643 of query aligns to 71:298/485 of 1mb9A
- active site: G71 (= G78)
- binding adenosine monophosphate: V235 (≠ F272), L236 (= L273), S242 (= S279), S260 (= S298), M261 (≠ I299)
- binding adenosine-5'-triphosphate: V235 (≠ F272), L236 (= L273), S237 (= S274), G239 (= G276), D241 (= D278), S242 (= S279), S260 (= S298), M261 (≠ I299)
- binding magnesium ion: D241 (= D278)
- binding pyrophosphate 2-: S237 (= S274), G239 (= G276), D241 (= D278), S242 (= S279)
Sites not aligning to the query:
- active site: 70, 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)
26% identity, 41% coverage: 78:338/643 of query aligns to 70:299/496 of 1mbzA
Sites not aligning to the query:
- active site: 69, 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
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 41% coverage: 78:338/643 of query aligns to 66:294/491 of 1mc1A
Sites not aligning to the query:
- active site: 65, 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
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)
37% identity, 18% coverage: 269:382/643 of query aligns to 241:353/503 of Q9XB61
- 244:251 (vs. 272:279, 75% identical) binding
- I270 (= I299) binding
- GYGSD 344:348 (≠ GDAGD 373:377) binding
- Y345 (≠ D374) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (≠ A375) 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)
37% identity, 18% coverage: 269:382/643 of query aligns to 240:352/500 of 1q19A
- active site: L318 (≠ S351), E321 (vs. gap), Y344 (≠ D374)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F272), L244 (= L273), S245 (= S274), D249 (= D278), S250 (= S279), S268 (= S298), I269 (= I299), T342 (≠ S372), G343 (= G373), D347 (= D377)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D374), G345 (≠ A375), L348 (≠ E378)
Sites not aligning to the query:
Query Sequence
>202285 FitnessBrowser__MR1:202285
MCGFAGFFNTSNLTDHARILECMGLELFNRGPDSFGIWFNSDDRIGLVHRRLAIVDLSAA
GHQPMTSDSGRYIISYNGEIYNHQELRDELESIRQYNWRGHSDTETLLAAIEQWGLKITL
QKATGMFGIALWDTLNKELYLARDRFGEKPVYYGLHKDAFIFASQLNAFRAYPDFKPEIN
RDSITLLLRHNYIPAPYSIYSDIHKLLPATILKLDSNNNISLETYWSAKDIMSNASSTET
DLPVGKQVEALENTLKKAVALQMSADVPLGAFLSGGVDSSLIVSLMQAQSNKPVKTFSIG
FDDPRFNEAVFAKEVAKHLGTEHTELYLTAEDALEVIPKLAEIYDEPFSDSSQIPTFLVS
KIARQYVTVSLSGDAGDELFCGYNRYLMTSKVWKRLSVLPVFLRSFLANVFTFVPVNVWN
LFGKLLPSRLQLSNLGDKLHKAAAVLACRDVEQLYLGLVSHWQNPEQVVLGSKEPLTVLT
DPKRKANFSDPILQMMAQDTLSYLTDDILVKVDRAAMAVSLETRVPFLDHSVLEHAWRLS
LDLKLRDGKTKWCLREILYKYVPKDLIERPKMGFAVPLDAWLRGPLKVWADNLLAAERLR
QEGFFDAELIDRMWQEHKSGKRNWQYQLWDILMFQSWYEKYHK
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