SitesBLAST
Comparing GFF4352 FitnessBrowser__Marino:GFF4352 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 12 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)
31% identity, 59% coverage: 1:390/657 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 (= H30) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H84) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ C112) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D381) 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, 60% coverage: 2:398/657 of query aligns to 1:349/497 of 1ct9A
- active site: A1 (≠ C2), L50 (= L53), N74 (= N78), G75 (= G79), T305 (≠ P354), R308 (≠ D357), E332 (≠ D381)
- binding adenosine monophosphate: L232 (≠ F279), L233 (= L280), S234 (= S281), S239 (= S286), A255 (≠ S305), V256 (= V306), D263 (≠ E315), M316 (≠ L365), S330 (= S379), G331 (= G380), E332 (≠ D381)
- binding glutamine: A1 (≠ C2), R49 (= R52), L50 (= L53), I52 (= I55), V53 (= V56), N74 (= N78), G75 (= G79), E76 (= E80), D98 (= D106)
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)
28% identity, 59% coverage: 1:390/657 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)
29% identity, 60% coverage: 1:397/657 of query aligns to 1:381/561 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 (≠ P228) to E: in dbSNP:rs1049674
- F362 (≠ L378) 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: 2:397/657 of query aligns to 1:368/509 of 6gq3A
- active site: W4 (≠ T5), L49 (= L53), N74 (= N78), G75 (= G79), T324 (≠ P354), R327 (≠ D357)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R52), V51 (≠ I55), V52 (= V56), Y73 (≠ F77), N74 (= N78), G75 (= G79), E76 (= E80), V95 (≠ S105), D96 (= D106)
1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 41% coverage: 77:348/657 of query aligns to 69:298/485 of 1mb9A
- active site: A70 (≠ N78), G71 (= G79)
- binding adenosine monophosphate: V235 (≠ F279), L236 (= L280), S242 (= S286), S260 (= S305), M261 (≠ V306)
- binding adenosine-5'-triphosphate: V235 (≠ F279), L236 (= L280), S237 (= S281), G239 (= G283), D241 (= D285), S242 (= S286), S260 (= S305), M261 (≠ V306)
- binding magnesium ion: D241 (= D285)
- binding pyrophosphate 2-: S237 (= S281), G239 (= G283), D241 (= D285), S242 (= S286)
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
1jgtB Crystal structure of beta-lactam synthetase (see paper)
28% identity, 41% coverage: 77:348/657 of query aligns to 72:307/500 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
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 41% coverage: 77:348/657 of query aligns to 68:299/496 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
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
28% identity, 28% coverage: 2:184/657 of query aligns to 1:207/455 of 1ao0A
Sites not aligning to the query:
- active site: 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 41% coverage: 77:348/657 of query aligns to 64:294/491 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
27% identity, 28% coverage: 2:184/657 of query aligns to 12:222/476 of P00497
- C12 (= C2) active site, Nucleophile; mutation to F: Loss of enzyme activity and N-terminal processing.
Sites not aligning to the query:
- 1:11 modified: propeptide
- 247 binding
- 294 binding
- 356 binding
- 357 binding
- 393 binding
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding ; C→S: Loss of activity.
- 451 binding ; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
27% identity, 28% coverage: 2:184/657 of query aligns to 1:211/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440
Query Sequence
>GFF4352 FitnessBrowser__Marino:GFF4352
MCGITGIFGGVPGSEPLKSALKQMADAITHRGPDDSGTWEELSAGLGFGHRRLSIVDLSP
AGHQPMLSGCGRFVLAFNGEIYNHNALRRELESSGKVSAGWKGHSDTETLLCAFTAWGVE
KTLEMAAGMFAIALWDREEQSLTLARDRFGEKPLYYGLVAGALVFSSELKALQRAPRWRG
EVEPSVLESYLRFGCVGGQESIFKDVFKLPAGCLLKVSLLDIRHGEMPPVVRWWSPVEAA
GAALGGRNNNPDMALDNVEQALVASIRQQMAADVPLGAFLSGGVDSSLIGALMQSQTSQK
VRTFSVGFDDPRYDESEHAAAVAAYLGTEHTTLRATSKMALDLVPKLPELYDEPFADSSQ
LPTCLISALTRQHVTVALSGDAGDELFGGYNRYVWVPRVWSKLSRMPLPMRQTLGRMLKL
VPSSRYDRLMCLGRKVLPSRYQIRTFGEKLYKLADVLACSSDRALYGGLASMNRHPEQLL
RTDYRSGNPVEDLYPALAGFDPVEWMMLMDTLNFMVDDVLVKVDRSSMASSLEVRAPFLD
PEVFKAAWQLPLDMRVRNGEGKWALRQILYRHVPRELIERPKMGFAIPLDDWLRGPLREW
AEDLLGVRWLSQIPALDAKAVHLMWDRHIQGQGHYAQQLWAVLQLSAWVKHWNPSFG
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