SitesBLAST
Comparing WP_012970981.1 NCBI__GCF_000025485.1:WP_012970981.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
32% identity, 62% coverage: 1:391/628 of query aligns to 1:379/554 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 (≠ F81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H106) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D366) 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, 62% coverage: 2:391/628 of query aligns to 1:362/497 of 1ct9A
- active site: A1 (≠ C2), L50 (= L51), N74 (= N75), G75 (= G76), T305 (≠ S343), R308 (≠ M346), E332 (≠ D366)
- binding adenosine monophosphate: L232 (≠ F265), L233 (= L266), S234 (= S267), S239 (= S272), A255 (≠ S293), V256 (≠ F294), D263 (≠ E301), M316 (≠ L354), S330 (= S364), G331 (= G365), E332 (≠ D366)
- binding glutamine: A1 (≠ C2), R49 (= R50), L50 (= L51), I52 (= I53), V53 (≠ I54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D100)
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)
29% identity, 62% coverage: 1:389/628 of query aligns to 1:384/557 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)
27% identity, 60% coverage: 1:375/628 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 (≠ I211) to E: in dbSNP:rs1049674
- F362 (≠ L363) 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, 60% coverage: 2:375/628 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ S5), L49 (= L51), N74 (= N75), G75 (= G76), T324 (≠ P339), R327 (≠ D342)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (≠ I53), V52 (≠ I54), Y73 (= Y74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ C99), D96 (= D100)
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
30% identity, 18% coverage: 69:178/628 of query aligns to 96:212/460 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)
30% identity, 18% coverage: 69:178/628 of query aligns to 182:298/561 of Q9STG9
- H187 (≠ Y74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K145) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P146) 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, 15% coverage: 43:139/628 of query aligns to 66:173/608 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, 15% coverage: 43:139/628 of query aligns to 66:173/608 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, 15% coverage: 43:139/628 of query aligns to 66:173/608 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, 15% coverage: 43:139/628 of query aligns to 66:173/238 of 1xfgA
Sites not aligning to the query:
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
33% identity, 15% coverage: 43:139/628 of query aligns to 66:173/238 of 1xffA
Sites not aligning to the query:
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
24% identity, 19% coverage: 61:178/628 of query aligns to 81:207/455 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
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
24% identity, 19% coverage: 61:178/628 of query aligns to 96:222/476 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 [4Fe-4S] cluster
- 294 binding Mg(2+)
- 356 binding Mg(2+)
- 357 binding Mg(2+)
- 393 binding [4Fe-4S] cluster
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding [4Fe-4S] cluster; C→S: Loss of activity.
- 451 binding [4Fe-4S] cluster; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
24% identity, 19% coverage: 61:178/628 of query aligns to 85:211/465 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
1jgtB Crystal structure of beta-lactam synthetase (see paper)
26% identity, 43% coverage: 70:336/628 of query aligns to 68:331/500 of 1jgtB
- active site: A73 (≠ N75), G74 (= G76), D319 (= D324)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F265), L245 (= L266), S246 (= S267), G248 (= G269), I249 (≠ V270), D250 (= D271), S251 (= S272), S269 (= S293), M270 (≠ F294), L327 (= L332)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ L328)
- binding magnesium ion: D250 (= D271)
Sites not aligning to the query:
- active site: 345, 379, 440
- binding diphosphomethylphosphonic acid adenosyl ester: 344, 345, 348, 420, 440
- binding n2-(carboxyethyl)-l-arginine: 345, 346, 348, 349, 354, 370, 379
- binding magnesium ion: 348
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 43% coverage: 70:336/628 of query aligns to 64:323/496 of 1mbzA
- active site: A69 (≠ N75), G70 (= G76), D311 (= D324)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F265), L237 (= L266), S238 (= S267), S243 (= S272), S261 (= S293), M262 (≠ F294), Y315 (≠ L328), L319 (= L332)
- binding magnesium ion: D242 (= D271)
- binding pyrophosphate 2-: S238 (= S267), G240 (= G269), D242 (= D271), S243 (= S272)
Sites not aligning to the query:
- active site: 337, 371, 432
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: 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, 43% coverage: 70:336/628 of query aligns to 60:318/491 of 1mc1A
Sites not aligning to the query:
- active site: 332, 366, 427
- binding adenosine monophosphate: 331, 427, 430
- binding magnesium ion: 335
- binding deoxyguanidinoproclavaminic acid: 332, 333, 336, 357, 366, 427
- binding pyrophosphate 2-: 335, 407, 427, 428
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 43% coverage: 70:336/628 of query aligns to 65:322/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (= D324)
- binding adenosine monophosphate: V235 (≠ F265), L236 (= L266), S242 (= S272), S260 (= S293), M261 (≠ F294), Y314 (≠ L328), L318 (= L332)
- binding adenosine-5'-triphosphate: V235 (≠ F265), L236 (= L266), S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), S260 (= S293), M261 (≠ F294), L318 (= L332)
- binding magnesium ion: D241 (= D271)
- binding pyrophosphate 2-: S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272)
Sites not aligning to the query:
Query Sequence
>WP_012970981.1 NCBI__GCF_000025485.1:WP_012970981.1
MCGISGLFDTRERRAVDASLLARMNQSLFHRGPDEGGQHTEPGVGLAHRRLSIIDLASGQ
QPLFNEDQTVVVVYNGEIYNFQALAHELTAAGHVFRTHCDTEVIVHAWEQWGEGCVERFR
GMFAFALWDRNRETLFLARDRLGIKPLHYAWRPDGQLLFGSEIKALLEDASLSREIDPLA
VEEYFAYGYVPDPRSIFKSIHKLPPGHTLTIRRGVNQRPEPREYWDVSFRPNGVQDVAEA
TAEVIERLREAVNIRLVAEVPLGAFLSGGVDSSAVVAMMAGLSDQPVNTCSISFGDPAFN
ESAYAEQVARRYATNHHVESVEPDDFELIERLAGIYDEPYADSSAMPTYRVCELARKRVT
VCLSGDGGDESFAGYRRYRWHLHEERVRRRLPQAVRGPVFGLLGALYPKADWAPKVLRAK
STLQALALDSVEGYFESVSILTDGVRRDLFSARLKRELQGYRAVEVLRRHAARAPEHPLS
RVQYLDMKTYLPGDILTKVDRASMAHALEVRVPILDHLFLDWVSGLSPDLKYAGGEGKWI
LKKALEPYLGPETLYRPKMGFAVPLTSWFRGPLRERVRQLLLGAPLLDSGFFDERQVRWI
VDQHQSGMRDFSPAIWSLMMFAAFNARL
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