SitesBLAST
Comparing WP_013819820.1 NCBI__GCF_000214665.1:WP_013819820.1 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 14 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
33% identity, 54% coverage: 30:388/668 of query aligns to 29:346/497 of 1ct9A
- active site: L50 (= L51), N74 (= N77), G75 (= G78), T305 (≠ N349), R308 (≠ G352), E332 (= E374)
- binding adenosine monophosphate: L232 (≠ Y271), L233 (= L272), S234 (= S273), S239 (= S278), A255 (≠ T297), V256 (≠ I298), D263 (≠ E307), M316 (= M358), S330 (≠ T372), G331 (= G373), E332 (= E374)
- binding glutamine: R49 (= R50), L50 (= L51), I52 (= I53), V53 (≠ I54), N74 (= N77), G75 (= G78), E76 (= E79), D98 (= D102)
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)
30% identity, 58% coverage: 1:388/668 of query aligns to 1:363/554 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 (≠ Y83) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H108) mutation to H: Little effect on the kinetic properties.
- E349 (= E374) 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)
30% identity, 58% coverage: 1:386/668 of query aligns to 1:368/557 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)
28% identity, 58% coverage: 1:388/668 of query aligns to 1:379/561 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 (≠ M229) 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
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
28% identity, 58% coverage: 2:388/668 of query aligns to 1:366/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L51), N74 (= N77), G75 (= G78), T324 (≠ N349), R327 (vs. gap)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (≠ I53), V52 (≠ I54), Y73 (≠ Q76), N74 (= N77), G75 (= G78), E76 (= E79), V95 (≠ S101), D96 (= D102)
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
28% identity, 25% coverage: 2:168/668 of query aligns to 1:199/460 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
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)
28% identity, 25% coverage: 2:168/668 of query aligns to 87:285/561 of Q9STG9
- H187 (≠ Q76) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K148) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P149) 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.
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
27% identity, 24% coverage: 2:164/668 of query aligns to 1:190/455 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, 24% coverage: 2:164/668 of query aligns to 12:205/476 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 [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)
27% identity, 24% coverage: 2:164/668 of query aligns to 1:194/465 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
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)
25% identity, 42% coverage: 101:382/668 of query aligns to 80:353/503 of Q9XB61
- 244:251 (vs. 271:278, 75% identical) binding ATP
- I270 (= I298) binding ATP
- GYGSD 344:348 (≠ GEGSD 373:377) binding ATP
- Y345 (≠ E374) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G375) 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)
25% identity, 42% coverage: 101:382/668 of query aligns to 79:352/500 of 1q19A
- active site: L318 (= L351), E321 (vs. gap), Y344 (≠ E374)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ Y271), L244 (= L272), S245 (= S273), D249 (= D277), S250 (= S278), S268 (≠ T297), I269 (= I298), T342 (= T372), G343 (= G373), D347 (= D377)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E374), G345 (= G375), L348 (≠ E378)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 46% coverage: 78:382/668 of query aligns to 71:344/485 of 1mb9A
- active site: G71 (= G78), D310 (≠ N349), Y336 (≠ E374)
- binding adenosine monophosphate: V235 (≠ Y271), L236 (= L272), S242 (= S278), S260 (≠ G299), M261 (≠ F300), Y314 (vs. gap), L318 (= L356), G335 (= G373), Y336 (≠ E374)
- binding adenosine-5'-triphosphate: V235 (≠ Y271), L236 (= L272), S237 (= S273), G239 (= G275), D241 (= D277), S242 (= S278), S260 (≠ G299), M261 (≠ F300), L318 (= L356), G335 (= G373), D339 (= D377)
- binding magnesium ion: D241 (= D277), D339 (= D377)
- binding pyrophosphate 2-: S237 (= S273), G239 (= G275), D241 (= D277), S242 (= S278), D339 (= D377)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
26% identity, 46% coverage: 78:382/668 of query aligns to 66:340/491 of 1mc1A
- active site: G66 (= G78), D306 (≠ N349), Y332 (≠ E374)
- binding adenosine monophosphate: V231 (≠ Y271), S233 (= S273), S238 (= S278), S256 (≠ G299), M257 (≠ F300), G331 (= G373)
- binding magnesium ion: D237 (= D277), D335 (= D377)
- binding deoxyguanidinoproclavaminic acid: Y310 (vs. gap), Y332 (≠ E374), G333 (= G375), I336 (≠ E378)
- binding pyrophosphate 2-: S233 (= S273), G235 (= G275), D237 (= D277), S238 (= S278), D335 (= D377)
Sites not aligning to the query:
Query Sequence
>WP_013819820.1 NCBI__GCF_000214665.1:WP_013819820.1
MCGIAGFIYADRNRPVDPETLVAMAAIQYHRGPDGFGWQARDGVGFSHARLSIIDLNQER
GRQPFISADGRLMLTQNGELYDYQRLRADLTARGDRFRSKSDSELILHLYPRLGLDASLP
HLRGEFAFALHDREQDVVHLVRDRFGIKPLYWTEIDGGLVFGSELKVLFAHPEVTRQFDS
AGLYHQLMQTMVPGSTAFAGVHQVKPGHVVSIERRNGRLQISDRRYWDMPFPQEHERGAP
GNQTQYIDGVRERLIEAVQLRLEADVPVGCYLSGGIDSCSIIGLATASTQGAVKAFTIGF
DNADYDETPIATEMAQATGADQEILRLDATHLYDHFEETLWHTERTIYNTLGVAKLLMSR
RVNEIGYKVVLTGEGSDELFGGYPAFRRDMFLHGLDHMPPDERREWEAMLAESNKLFTGA
MLSEDTIDDPALRAKVGFTPSCLQPWLASARRVPDLLHPDRRAELAHYSPGAAIAEALDQ
DALQGRHPLDKAQYVWIKTMLEGQILTWGGDRVDMANSMEARPPFLDHHLAEYAATLPPS
MRIHGRTEKYVLREAMKGLLPETLYKREKFAFMAPPAHTDPGKWAAMRVLAERHLNSDAI
VQAGLLDSQGVDALFALHDAPDTSVATQTQLDAVINHLLGVQILHERFIAADIPAQARRK
AAELGWRA
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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