SitesBLAST
Comparing WP_010876053.1 NCBI__GCF_000008645.1:WP_010876053.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
30% identity, 91% coverage: 18:446/469 of query aligns to 19:437/497 of 1ct9A
- active site: L50 (= L68), N74 (= N86), G75 (= G87), T305 (≠ M307), R308 (≠ G310), E332 (≠ Q334), M366 (≠ H368)
- binding adenosine monophosphate: L232 (≠ V233), L233 (≠ F234), S234 (= S235), S239 (= S240), A255 (≠ T257), V256 (= V258), D263 (= D265), M316 (≠ A318), S330 (= S332), G331 (= G333), E332 (≠ Q334)
- binding glutamine: R49 (≠ L67), L50 (= L68), I52 (= I70), V53 (= V71), N74 (= N86), G75 (= G87), E76 (= E88), D98 (= D101)
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)
29% identity, 94% coverage: 4:446/469 of query aligns to 1:457/554 of P22106
- M1 (= M4) modified: Initiator methionine, Removed
- C2 (= C5) 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 (≠ Q92) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ D107) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q334) 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, 90% coverage: 26:446/469 of query aligns to 28:472/557 of P78753
- S391 (≠ V369) modified: Phosphoserine
Sites not aligning to the query:
- 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, 95% coverage: 4:449/469 of query aligns to 1:477/561 of P08243
- C2 (= C5) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- A6 (≠ G9) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ L195) to E: in dbSNP:rs1049674
- F362 (= F331) 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, 92% coverage: 5:436/469 of query aligns to 1:453/509 of 6gq3A
- active site: W4 (≠ A8), L49 (= L68), N74 (= N86), G75 (= G87), T324 (≠ M307), R327 (≠ G310)
- binding 5-oxo-l-norleucine: C1 (= C5), R48 (≠ L67), V51 (≠ I70), V52 (= V71), Y73 (≠ F85), N74 (= N86), G75 (= G87), E76 (= E88), V95 (≠ S100), D96 (= D101)
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 83% coverage: 69:455/469 of query aligns to 58:450/496 of 1mbzA
- active site: A69 (≠ N86), G70 (= G87), D311 (≠ M307), Y337 (≠ Q334), E371 (≠ L371), K432 (= K437)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (= V233), L237 (≠ F234), S238 (= S235), S243 (= S240), S261 (≠ G259), M262 (≠ L260), Y315 (≠ V311), L319 (= L315), G336 (= G333), Y337 (≠ Q334), G338 (= G335), D340 (= D337), I341 (≠ E338), D362 (= D362), E371 (≠ L371), K432 (= K437), G434 (≠ A439), V435 (≠ A440)
- binding magnesium ion: D242 (= D239), D340 (= D337)
- binding pyrophosphate 2-: S238 (= S235), G240 (= G237), D242 (= D239), S243 (= S240), D340 (= D337), K412 (= K416), K432 (= K437), L433 (≠ K438)
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 83% coverage: 69:455/469 of query aligns to 54:445/491 of 1mc1A
- active site: A65 (≠ N86), G66 (= G87), D306 (≠ M307), Y332 (≠ Q334), E366 (≠ L371), K427 (= K437)
- binding adenosine monophosphate: V231 (= V233), S233 (= S235), S238 (= S240), S256 (≠ G259), M257 (≠ L260), G331 (= G333), K427 (= K437), V430 (≠ A440)
- binding magnesium ion: D237 (= D239), D335 (= D337)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ V311), Y332 (≠ Q334), G333 (= G335), I336 (≠ E338), D357 (= D362), E366 (≠ L371), K427 (= K437)
- binding pyrophosphate 2-: S233 (= S235), G235 (= G237), D237 (= D239), S238 (= S240), D335 (= D337), K407 (= K416), K427 (= K437), L428 (≠ K438)
1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 79% coverage: 69:439/469 of query aligns to 59:433/485 of 1mb9A
- active site: A70 (≠ N86), G71 (= G87), D310 (≠ M307), Y336 (≠ Q334), E370 (≠ L371), K431 (= K437)
- binding adenosine monophosphate: V235 (= V233), L236 (≠ F234), S242 (= S240), S260 (≠ G259), M261 (≠ L260), Y314 (≠ V311), L318 (= L315), G335 (= G333), Y336 (≠ Q334)
- binding adenosine-5'-triphosphate: V235 (= V233), L236 (≠ F234), S237 (= S235), G239 (= G237), D241 (= D239), S242 (= S240), S260 (≠ G259), M261 (≠ L260), L318 (= L315), G335 (= G333), D339 (= D337), K411 (= K416), K431 (= K437)
- binding magnesium ion: D241 (= D239), D339 (= D337)
- binding pyrophosphate 2-: S237 (= S235), G239 (= G237), D241 (= D239), S242 (= S240), D339 (= D337), K411 (= K416), K431 (= K437)
1jgtB Crystal structure of beta-lactam synthetase (see paper)
28% identity, 80% coverage: 69:444/469 of query aligns to 62:447/500 of 1jgtB
- active site: A73 (≠ N86), G74 (= G87), D319 (≠ M307), Y345 (≠ Q334), E379 (≠ L371), K440 (= K437)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (= V233), L245 (≠ F234), S246 (= S235), G248 (= G237), I249 (≠ V238), D250 (= D239), S251 (= S240), S269 (≠ G259), M270 (≠ L260), L327 (= L315), G344 (= G333), Y345 (≠ Q334), D348 (= D337), K420 (= K416), K440 (= K437)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ V311), Y345 (≠ Q334), G346 (= G335), D348 (= D337), I349 (≠ E338), M354 (≠ Y343), D370 (= D362), E379 (≠ L371)
- binding magnesium ion: D250 (= D239), D348 (= D337)
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
25% identity, 45% coverage: 5:216/469 of query aligns to 1:250/460 of 6lbpA
Sites not aligning to the query:
1q19A Carbapenam synthetase (see paper)
24% identity, 48% coverage: 227:450/469 of query aligns to 237:455/500 of 1q19A
- active site: L318 (≠ M307), E321 (≠ G310), Y344 (≠ Q334), E379 (≠ D374), K442 (= K437)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ V233), L244 (≠ F234), S245 (= S235), D249 (= D239), S250 (= S240), S268 (≠ T257), I269 (≠ V258), T342 (≠ S332), G343 (= G333), D347 (= D337), K442 (= K437), I443 (≠ K438), G444 (≠ A439), I445 (≠ A440)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q334), G345 (= G335), L348 (≠ E338), R373 (≠ H368), E379 (≠ D374)
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)
24% identity, 48% coverage: 227:450/469 of query aligns to 238:456/503 of Q9XB61
- 244:251 (vs. 233:240, 63% identical) binding
- I270 (≠ V258) binding
- GYGSD 344:348 (≠ GQGAD 333:337) binding
- Y345 (≠ Q334) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G335) binding
- Q371 (≠ N365) binding
- R374 (≠ H368) binding
- E380 (≠ D374) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
- K421 (= K416) binding
- K443 (= K437) mutation K->A,M: Loss of activity.
- IGI 444:446 (≠ KAA 438:440) binding
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)
25% identity, 45% coverage: 5:216/469 of query aligns to 87:336/561 of Q9STG9
- H187 (≠ F85) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K151) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P152) 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.
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
26% identity, 39% coverage: 5:185/469 of query aligns to 12:227/476 of P00497
- C12 (= C5) 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)
26% identity, 39% coverage: 5:185/469 of query aligns to 1:216/465 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)
26% identity, 39% coverage: 5:185/469 of query aligns to 1:212/455 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
P41390 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; EC 2.4.2.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 39% coverage: 4:185/469 of query aligns to 1:234/533 of P41390
Sites not aligning to the query:
- 506 modified: Phosphoserine
Query Sequence
>WP_010876053.1 NCBI__GCF_000008645.1:WP_010876053.1
MTAMCAIAGFRGDDAPVKVQEMLDVLRHRGPDATGIYHDSRIVIRTATGEDVKEAPQSAE
IAVGHNLLSIVGGPQPVSGDGVLVFNGEIYNQEELNWTGSDSELILDLIEGHGGDLEDAL
RFTVNKIDGDYAFAYTDGENLASRQDPVGVKPLYHSGEAFASEKKALWRIGLRNVETLPP
GHAMINGVKVKLRGLPRAEPSDAEPEELRENLKSALRESVERRVRGLDEAALVFSGGVDS
TLLAVLLDEHIDVRLYTVGLPGSSDPQFASRAAADLGMELEVLEVTEDTIREALPHVLGA
IEEYNLMKIGVAMPLYLASEAASADGYRVMFSGQGADELFAGYHRYRRLLAEGRLEDALR
HDLENIHHVNLERDDAVTMANSVELRVPFLDLQLIGVALTIPADLKIRGPEDELRKRILR
EAALEMGVPEYIAMRPKKAAQYGSGIDKVLRRKVLPGFDHETFLRRLMF
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