SitesBLAST
Comparing WP_011382552.1 NCBI__GCF_000009985.1:WP_011382552.1 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 19 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)
33% identity, 59% coverage: 1:370/627 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 (= H24) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D28) mutation D->N,E: Little effect on the kinetic properties.
- H81 (= H78) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ R103) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D361) 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)
34% identity, 56% coverage: 19:370/627 of query aligns to 23:341/497 of 1ct9A
- active site: L50 (= L47), N74 (= N72), G75 (= G73), T305 (≠ P334), R308 (≠ N337), E332 (≠ D361)
- binding adenosine monophosphate: L232 (≠ F260), L233 (= L261), S234 (= S262), S239 (= S267), A255 (≠ T286), V256 (≠ M287), D263 (≠ E296), M316 (≠ D345), S330 (≠ V359), G331 (= G360), E332 (≠ D361)
- binding glutamine: R49 (= R46), L50 (= L47), I52 (≠ V49), V53 (≠ I50), N74 (= N72), G75 (= G73), E76 (= E74), D98 (= D97)
Sites not aligning to the query:
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: 1:374/627 of query aligns to 1:378/561 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 (= V218) to E: in dbSNP:rs1049674
- F362 (≠ L358) 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
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)
29% identity, 59% coverage: 1:370/627 of query aligns to 1:365/557 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: 2:374/627 of query aligns to 1:365/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L47), N74 (= N72), G75 (= G73), T324 (≠ P338), R327 (vs. gap)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R46), V51 (= V49), V52 (≠ I50), Y73 (= Y71), N74 (= N72), G75 (= G73), E76 (= E74), V95 (≠ S96), D96 (= D97)
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)
29% identity, 30% coverage: 2:190/627 of query aligns to 87:318/561 of Q9STG9
- H187 (≠ Y71) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K142) 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.
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
29% identity, 30% coverage: 2:190/627 of query aligns to 1:232/460 of 6lbpA
Sites not aligning to the query:
- active site: 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
28% identity, 26% coverage: 2:166/627 of query aligns to 1:197/455 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
27% identity, 26% coverage: 2:166/627 of query aligns to 12:212/476 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, 26% coverage: 2:166/627 of query aligns to 1:201/465 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
1mb9A Beta-lactam synthetase complexed with atp (see paper)
32% identity, 45% coverage: 30:314/627 of query aligns to 25:286/485 of 1mb9A
- active site: A70 (= A70), G71 (= G73)
- binding adenosine monophosphate: V235 (≠ F260), L236 (= L261), S242 (= S267), S260 (≠ R283), M261 (≠ T284)
- binding adenosine-5'-triphosphate: V235 (≠ F260), L236 (= L261), S237 (= S262), G239 (= G264), D241 (= D266), S242 (= S267), S260 (≠ R283), M261 (≠ T284)
- binding magnesium ion: D241 (= D266)
- binding pyrophosphate 2-: S237 (= S262), G239 (= G264), D241 (= D266), S242 (= S267)
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
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
31% identity, 21% coverage: 2:135/627 of query aligns to 1:171/608 of 4amvA
Sites not aligning to the query:
- active site: 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)
31% identity, 21% coverage: 2:135/627 of query aligns to 1:171/608 of 1jxaA
Sites not aligning to the query:
- active site: 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)
31% identity, 21% coverage: 2:135/627 of query aligns to 1:171/608 of 2j6hA
- active site: C1 (= C2), R26 (= R25), G27 (= G26), W74 (≠ L47), N98 (= N72), G99 (= G73)
- binding 5-oxo-l-norleucine: C1 (= C2), R73 (= R46), W74 (≠ L47), T76 (≠ V49), H86 (≠ Q58), N98 (= N72), G99 (= G73), D123 (= D97)
Sites not aligning to the query:
- active site: 248, 481, 485, 488, 504, 603
- binding glucose-6-phosphate: 302, 347, 348, 349, 352, 399, 401, 488
1xfgA Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate (see paper)
31% identity, 21% coverage: 2:135/627 of query aligns to 1:171/238 of 1xfgA
- active site: C1 (= C2), R26 (= R25), G27 (= G26), W74 (≠ L47), N98 (= N72), G99 (= G73)
- binding glutamine hydroxamate: C1 (= C2), R73 (= R46), W74 (≠ L47), T76 (≠ V49), H86 (≠ Q58), N98 (= N72), G99 (= G73), D123 (= D97)
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
31% identity, 21% coverage: 2:135/627 of query aligns to 1:171/238 of 1xffA
- active site: C1 (= C2), R26 (= R25), G27 (= G26), W74 (≠ L47), N98 (= N72), G99 (= G73)
- binding glutamic acid: C1 (= C2), R73 (= R46), W74 (≠ L47), T76 (≠ V49), H86 (≠ Q58), N98 (= N72), G99 (= G73), D123 (= D97)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
32% identity, 46% coverage: 25:314/627 of query aligns to 13:282/491 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
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
31% identity, 45% coverage: 30:314/627 of query aligns to 24:287/496 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
1jgtB Crystal structure of beta-lactam synthetase (see paper)
31% identity, 45% coverage: 30:314/627 of query aligns to 28:295/500 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
Query Sequence
>WP_011382552.1 NCBI__GCF_000009985.1:WP_011382552.1
MCGIAGTTAAQPAILAGLLARLAHRGPDGQGRWTEPDSGMGLVHARLAVIDLSQAGAQPM
VSPCGRWVLAYNGEIYNHAQLRAELEAVGEHFTSASDTEVLLRLLMRDGVECLPRLVGMF
AFALWDRQTRQLLLARDRVGIKPLVWAALPGGGLAFASEIHALRAVPGIDLSLDREALSE
YLACLYVPAPRTIHAGIRKLPPGSWLSWSPGKAATIGVWWRPIYGGGRRPGQDEAVEELL
PVLRRAVKDCLVSDVQVGCFLSGGIDSSVVAALMAEGAADPVRTFTMTFDEVHYDEREAA
AQVAAHVGSRHVELPASSGLADGLDTMIERFGEPFGNPTALLIGDLSRLARQHVTVALVG
DGGDEVFAGYPRYQGGLLAERVRLLPGVLRRNLLAPLARMIPERSDGRHAWRRAREFLAS
TGLDGAETYAAWVEYFSPAERRELLRLARTPASPIAARYGEVVSENALDAMQETDLATFL
PGNLLAYGDAMSMNHALELRLPLLDHRVIEAAGRLDASLRFAEGKKTLLRAVARKLLPRA
IVDRPKLGFNPPLGMWLQGPLKAMVAERLTPKRLEELGLAAPAVAAVLAEQAGGRRDHSL
KIWSLLVLDAWERGLQPVPATAIGAGA
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