SitesBLAST
Comparing WP_013074756.1 NCBI__GCF_000092905.1:WP_013074756.1 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 17 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: 1:381/648 of query aligns to 1:371/554 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 (= H28) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D32) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y79) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H104) mutation to H: Little effect on the kinetic properties.
- E349 (= E359) 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)
33% identity, 55% coverage: 28:381/648 of query aligns to 29:354/497 of 1ct9A
- active site: L50 (= L49), N74 (= N73), G75 (= G74), T305 (≠ V333), R308 (≠ P336), E332 (= E359)
- binding adenosine monophosphate: L232 (≠ F258), L233 (= L259), S234 (= S260), S239 (= S265), A255 (≠ T282), V256 (= V283), D263 (≠ E293), M316 (≠ V344), S330 (= S357), G331 (= G358), E332 (= E359)
- binding glutamine: R49 (= R48), L50 (= L49), I52 (= I51), V53 (≠ I52), N74 (= N73), G75 (= G74), E76 (= E75), D98 (= D98)
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, 60% coverage: 1:389/648 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, 58% coverage: 1:376/648 of query aligns to 1:382/561 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 (≠ L200) to E: in dbSNP:rs1049674
- F362 (≠ L356) 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, 58% coverage: 2:376/648 of query aligns to 1:369/509 of 6gq3A
- active site: W4 (≠ C5), L49 (= L49), N74 (= N73), G75 (= G74), T324 (≠ V333), R327 (≠ P336)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R48), V51 (≠ I51), V52 (≠ I52), Y73 (≠ F72), N74 (= N73), G75 (= G74), E76 (= E75), V95 (≠ T97), D96 (= D98)
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
32% identity, 16% coverage: 59:159/648 of query aligns to 96:205/476 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)
32% identity, 16% coverage: 59:159/648 of query aligns to 85:194/465 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
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
32% identity, 16% coverage: 59:159/648 of query aligns to 81:190/455 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
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)
24% identity, 53% coverage: 27:367/648 of query aligns to 19:353/503 of Q9XB61
- 244:251 (vs. 258:265, 63% identical) binding ATP
- I270 (≠ V283) binding ATP
- GYGSD 344:348 (≠ GEGAD 358:362) binding ATP
- Y345 (≠ E359) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G360) binding substrate
Sites not aligning to the query:
- 371 binding substrate
- 374 binding substrate
- 380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
- 421 binding ATP
- 443 mutation K->A,M: Loss of activity.
- 444:446 binding ATP
1q19A Carbapenam synthetase (see paper)
24% identity, 53% coverage: 27:367/648 of query aligns to 18:352/500 of 1q19A
- active site: G56 (= G74), L318 (≠ V333), E321 (≠ P336), Y344 (≠ E359)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F258), L244 (= L259), S245 (= S260), D249 (= D264), S250 (= S265), S268 (≠ T282), I269 (≠ V283), T342 (≠ S357), G343 (= G358), D347 (= D362)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E359), G345 (= G360), L348 (≠ E363)
Sites not aligning to the query:
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
35% identity, 15% coverage: 66:163/648 of query aligns to 95:199/460 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)
35% identity, 15% coverage: 66:163/648 of query aligns to 181:285/561 of Q9STG9
- H187 (≠ F72) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K143) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P144) 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.
2j6hA E. Coli glucosamine-6-p synthase in complex with glucose-6p and 5-oxo- l-norleucine (see paper)
31% identity, 21% coverage: 2:137/648 of query aligns to 1:173/608 of 2j6hA
- active site: C1 (= C2), R26 (= R29), G27 (= G30), W74 (vs. gap), N98 (= N73), G99 (= G74)
- binding 5-oxo-l-norleucine: C1 (= C2), R73 (vs. gap), W74 (vs. gap), T76 (vs. gap), H86 (vs. gap), N98 (= N73), G99 (= G74), D123 (= D98)
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
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
31% identity, 21% coverage: 2:137/648 of query aligns to 1:173/608 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: 2:137/648 of query aligns to 1:173/608 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
1xfgA Glutaminase domain of glucosamine 6-phosphate synthase complexed with l-glu hydroxamate (see paper)
30% identity, 21% coverage: 2:138/648 of query aligns to 1:174/238 of 1xfgA
- active site: C1 (= C2), R26 (= R29), G27 (= G30), W74 (vs. gap), N98 (= N73), G99 (= G74)
- binding glutamine hydroxamate: C1 (= C2), R73 (vs. gap), W74 (vs. gap), T76 (vs. gap), H86 (vs. gap), N98 (= N73), G99 (= G74), D123 (= D98)
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
30% identity, 21% coverage: 2:138/648 of query aligns to 1:174/238 of 1xffA
- active site: C1 (= C2), R26 (= R29), G27 (= G30), W74 (vs. gap), N98 (= N73), G99 (= G74)
- binding glutamic acid: C1 (= C2), R73 (vs. gap), W74 (vs. gap), T76 (vs. gap), H86 (vs. gap), N98 (= N73), G99 (= G74), D123 (= D98)
Query Sequence
>WP_013074756.1 NCBI__GCF_000092905.1:WP_013074756.1
MCGICGIANRDGNVEMETLRQMAERIIHRGPDDEGFYLGSGVGFGFRRLSIIDVAGGHQP
MSNEDGSIWVVFNGEIYNYKWLRRELVERGHQFRTDTDTEVLVHLYEEEGLDLVGRLRGM
FAFAIWDEPRRTLLLARDHFGIKPLYYTLTPEGLVFASEIKSLLAVPGIEARVKPESLWN
YLTFQYVPDPETMFEGIKKLPPAHRLIWREGEAKLGRYWEATFEPVDRPLPAFVDEVREV
LRESVRAHMNSDVPRGAFLSSGVDSSTIVALLKELEQVKTFTVGFEGAGGMSEIEYARET
ARILGTDHRDVVISANRYAEVLPDLAYHQDEPVADPSAIALYFVAELASSDVAVVLSGEG
ADELFGGYTIYREPLSLRMFHFLPDGVRRGLGEWARGLPSGMKGRGFLLRGSRLLSDRFV
GNANIFSDNEKRAFLKWTPDGGFACVKVVTEPLYERFADMDEVTQMQLVDIHTWLPGDIL
MKADKMTMANSLELRVPFLDVRVFDVARRIPTSLRLLEGTTKYVLREAVRDILPEAVTRR
KKLGFPVPTRRWLRDELYEWARERLSDKSVDEYFDRAWLLARLEDHRLGRGDYARKLWTV
LMFLLWHDIYISGHVAVQPTVRPGVLRRRERLFGRGAAQGQRLESYAP
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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