SitesBLAST
Comparing SM_b20652 FitnessBrowser__Smeli:SM_b20652 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 20 (the maximum) hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
37% identity, 55% coverage: 27:380/645 of query aligns to 29:347/497 of 1ct9A
- active site: L50 (= L48), N74 (= N72), G75 (= G73), T305 (≠ R340), R308 (vs. gap), E332 (= E365)
- binding adenosine monophosphate: L232 (≠ Y262), L233 (= L263), S234 (= S264), S239 (= S269), A255 (≠ S288), V256 (= V289), D263 (≠ H296), M316 (≠ L349), S330 (≠ T363), G331 (= G364), E332 (= E365)
- binding glutamine: R49 (= R47), L50 (= L48), I52 (= I50), V53 (= V51), N74 (= N72), G75 (= G73), E76 (= E74), D98 (= D97)
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)
34% identity, 59% coverage: 1:380/645 of query aligns to 1:364/554 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 (= H27) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D31) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y78) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H103) mutation to H: Little effect on the kinetic properties.
- E349 (= E365) 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)
32% identity, 57% coverage: 15:383/645 of query aligns to 18:374/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 489 modified: Phosphoserine
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
29% identity, 59% coverage: 2:380/645 of query aligns to 1:367/509 of 6gq3A
- active site: W4 (≠ G5), L49 (= L48), N74 (= N72), G75 (= G73), T324 (≠ R340), R327 (≠ P343)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R47), V51 (≠ I50), V52 (= V51), Y73 (≠ F71), N74 (= N72), G75 (= G73), E76 (= E74), V95 (≠ S96), D96 (= D97)
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, 59% coverage: 1:380/645 of query aligns to 1:380/561 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 (≠ Y222) to E: in dbSNP:rs1049674
- F362 (vs. gap) 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
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
35% identity, 20% coverage: 43:174/645 of query aligns to 68:211/465 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
35% identity, 20% coverage: 43:174/645 of query aligns to 79:222/476 of P00497
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 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.
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
35% identity, 20% coverage: 43:174/645 of query aligns to 68:207/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 27, 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 25, 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
1q19A Carbapenam synthetase (see paper)
26% identity, 43% coverage: 95:373/645 of query aligns to 78:352/500 of 1q19A
- active site: L318 (≠ A342), E321 (≠ P345), Y344 (≠ E365)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ Y262), L244 (= L263), S245 (= S264), D249 (= D268), S250 (= S269), S268 (= S288), I269 (≠ V289), T342 (= T363), G343 (= G364), D347 (= D368)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E365), G345 (= G366), L348 (≠ E369)
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)
26% identity, 43% coverage: 95:373/645 of query aligns to 79:353/503 of Q9XB61
- 244:251 (vs. 262:269, 88% identical) binding
- I270 (≠ V289) binding
- GYGSD 344:348 (≠ GEGAD 364:368) binding
- Y345 (≠ E365) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G366) 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
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
28% identity, 27% coverage: 43:215/645 of query aligns to 69:226/460 of 6lbpA
Sites not aligning to the query:
- active site: 1, 27, 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
34% identity, 19% coverage: 43:162/645 of query aligns to 155:285/561 of Q9STG9
- H187 (≠ F71) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (= R142) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P143) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
Sites not aligning to the query:
- 371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
- 476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
- 494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
33% identity, 20% coverage: 40:165/645 of query aligns to 66:199/608 of 4amvA
Sites not aligning to the query:
- active site: 1, 26, 27, 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)
33% identity, 20% coverage: 40:165/645 of query aligns to 66:199/608 of 1jxaA
Sites not aligning to the query:
- active site: 1, 26, 27, 248, 481, 485, 488, 504, 603
- binding glucose-6-phosphate: 302, 303, 347, 348, 349, 352, 401, 485, 488
2j6hA E. Coli glucosamine-6-p synthase in complex with glucose-6p and 5-oxo- l-norleucine (see paper)
33% identity, 20% coverage: 40:165/645 of query aligns to 66:199/608 of 2j6hA
Sites not aligning to the query:
- active site: 1, 26, 27, 248, 481, 485, 488, 504, 603
- binding glucose-6-phosphate: 302, 347, 348, 349, 352, 399, 401, 488
- binding 5-oxo-l-norleucine: 1
1xfgA Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate (see paper)
33% identity, 20% coverage: 40:165/645 of query aligns to 66:199/238 of 1xfgA
Sites not aligning to the query:
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
33% identity, 20% coverage: 40:165/645 of query aligns to 66:199/238 of 1xffA
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 47% coverage: 68:373/645 of query aligns to 69:353/500 of 1jgtB
- active site: A73 (≠ N72), G74 (= G73), D319 (≠ I338), Y345 (≠ E365)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ Y262), L245 (= L263), S246 (= S264), G248 (= G266), I249 (≠ L267), D250 (= D268), S251 (= S269), S269 (= S288), M270 (≠ V289), L327 (= L346), G344 (= G364), Y345 (≠ E365), D348 (= D368)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A342), Y345 (≠ E365), G346 (= G366), D348 (= D368), I349 (≠ E369)
- binding magnesium ion: D250 (= D268), D348 (= D368)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 47% coverage: 68:373/645 of query aligns to 66:344/485 of 1mb9A
- active site: A70 (≠ N72), G71 (= G73), D310 (≠ I338), Y336 (≠ E365)
- binding adenosine monophosphate: V235 (≠ Y262), L236 (= L263), S242 (= S269), S260 (= S288), M261 (≠ V289), Y314 (≠ A342), L318 (= L346), G335 (= G364), Y336 (≠ E365)
- binding adenosine-5'-triphosphate: V235 (≠ Y262), L236 (= L263), S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), S260 (= S288), M261 (≠ V289), L318 (= L346), G335 (= G364), D339 (= D368)
- binding magnesium ion: D241 (= D268), D339 (= D368)
- binding pyrophosphate 2-: S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), D339 (= D368)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 47% coverage: 68:373/645 of query aligns to 65:345/496 of 1mbzA
- active site: A69 (≠ N72), G70 (= G73), D311 (≠ I338), Y337 (≠ E365)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ Y262), L237 (= L263), S238 (= S264), S243 (= S269), S261 (= S288), M262 (≠ V289), Y315 (≠ A342), L319 (= L346), G336 (= G364), Y337 (≠ E365), G338 (= G366), D340 (= D368), I341 (≠ E369)
- binding magnesium ion: D242 (= D268), D340 (= D368)
- binding pyrophosphate 2-: S238 (= S264), G240 (= G266), D242 (= D268), S243 (= S269), D340 (= D368)
Sites not aligning to the query:
Query Sequence
>SM_b20652 FitnessBrowser__Smeli:SM_b20652
MCGFGGYLGSIRDGKPLLERMTAAIGHRGPDERGIFTAPGAGLGHVRLSIVGLGDGQQPM
SNPSGELTIAFNGEIFNYVELRDELRARGRQFRTSSDTEVILHLYEEMGEDCLSLLNGDF
AFAIWDARRRRMMLARDRMGVRPLFHTLKGGTLYFASEVKALLEVPGVSAEIDPIALDQI
FTLWAPIAPRTPFRDIHELEPGHLMIADQNGTTTRPYWQLDYPDRDERPAYAEESRAAEE
LRALLTDATRIRMRADVPVGAYLSGGLDSSIISALAAGMTSQGLRTFSVTFDSAEHDESA
FQEEMAAALGTEHRAVACRAGDIARDFPDVIRFTEKPIIRTAPAPLYKLSGLVREAGLKV
VLTGEGADEVFAGYDIFKEARVRRFCGRQPGSRIRPHLFRKLYPYLPGLQQQSAEYLAAF
FGAGDVALDDPLFSHRPRLKGTAATKMFFSSDLRAELTGYDAAEELVSRLPAAFGRWHPL
HQAQYLESRFLLPGYILSSQGDRMAMAHGIEGRFPFLDHRLVEFAAKLPPEMKLRGLVEK
HILREATKDLLPPAIGRRTKQPYRAPDSHSFSGAGELDYVRSAMSEDAVAAGGLFNAKAV
TKLYEKCQSRPASGFRDNAAFVGVLSTQLWLQTFTGTSLRKAEAA
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