SitesBLAST
Comparing WP_027458901.1 NCBI__GCF_000519045.1:WP_027458901.1 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 15 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)
30% identity, 62% coverage: 1:394/635 of query aligns to 1:383/554 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 (≠ Y81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H106) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D365) 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)
30% identity, 62% coverage: 2:394/635 of query aligns to 1:366/497 of 1ct9A
- active site: A1 (≠ C2), L50 (= L51), N74 (= N75), G75 (= G76), T305 (≠ P338), R308 (≠ D341), E332 (≠ D365), M366 (≠ L394)
- binding adenosine monophosphate: L232 (≠ F264), L233 (= L265), S234 (= S266), S239 (= S271), A255 (≠ S290), V256 (≠ I291), D263 (≠ E300), M316 (≠ V350), S330 (= S363), G331 (= G364), E332 (≠ D365)
- binding glutamine: A1 (≠ C2), R49 (= R50), L50 (= L51), I52 (= I53), V53 (≠ I54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D100)
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: 1:374/635 of query aligns to 1:365/557 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, 59% coverage: 1:374/635 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 (≠ Q219) to E: in dbSNP:rs1049674
- F362 (≠ L362) 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, 59% coverage: 2:374/635 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ T5), L49 (= L51), N74 (= N75), G75 (= G76), T324 (≠ P338), R327 (≠ D341)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (≠ I53), V52 (≠ I54), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S99), D96 (= D100)
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)
24% identity, 44% coverage: 2:279/635 of query aligns to 87:377/561 of Q9STG9
- H187 (≠ F74) 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.
- G371 (≠ A273) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734.
Sites not aligning to the query:
- 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)
25% identity, 28% coverage: 2:178/635 of query aligns to 1:212/460 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
1q19A Carbapenam synthetase (see paper)
34% identity, 18% coverage: 261:373/635 of query aligns to 240:352/500 of 1q19A
- active site: L318 (≠ S342), E321 (vs. gap), Y344 (≠ D365)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F264), L244 (= L265), S245 (= S266), D249 (= D270), S250 (= S271), S268 (= S290), I269 (= I291), T342 (≠ S363), G343 (= G364), D347 (= D368)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D365), G345 (= G366), L348 (≠ E369)
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)
34% identity, 18% coverage: 261:373/635 of query aligns to 241:353/503 of Q9XB61
- 244:251 (vs. 264:271, 75% identical) binding ATP
- I270 (= I291) binding ATP
- GYGSD 344:348 (≠ GDGGD 364:368) binding ATP
- Y345 (≠ D365) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G366) 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
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
24% identity, 28% coverage: 2:178/635 of query aligns to 1:207/455 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
4amvA E.Coli glucosamine-6p synthase in complex with fructose-6p (see paper)
25% identity, 26% coverage: 2:166/635 of query aligns to 1:197/608 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)
25% identity, 26% coverage: 2:166/635 of query aligns to 1:197/608 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)
25% identity, 26% coverage: 2:166/635 of query aligns to 1:197/608 of 2j6hA
- active site: C1 (= C2), R26 (= R31), G27 (= G32), W74 (vs. gap), N98 (= N75), G99 (= G76)
- binding 5-oxo-l-norleucine: C1 (= C2), R73 (vs. gap), W74 (vs. gap), T76 (vs. gap), H86 (vs. gap), N98 (= N75), G99 (= G76), D123 (= D100)
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)
25% identity, 26% coverage: 2:166/635 of query aligns to 1:197/238 of 1xfgA
- active site: C1 (= C2), R26 (= R31), G27 (= G32), W74 (≠ L51), N98 (= N75), G99 (= G76)
- binding glutamine hydroxamate: C1 (= C2), R73 (= R50), W74 (≠ L51), T76 (≠ I53), H86 (≠ L63), N98 (= N75), G99 (= G76), D123 (= D100)
1xffA Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate (see paper)
25% identity, 26% coverage: 2:166/635 of query aligns to 1:197/238 of 1xffA
- active site: C1 (= C2), R26 (= R31), G27 (= G32), W74 (≠ L51), N98 (= N75), G99 (= G76)
- binding glutamic acid: C1 (= C2), R73 (= R50), W74 (≠ L51), T76 (≠ I53), H86 (≠ L63), N98 (= N75), G99 (= G76), D123 (= D100)
Query Sequence
>WP_027458901.1 NCBI__GCF_000519045.1:WP_027458901.1
MCGITGIFDTRSRRDIDRAVLHRMNEAQFHRGPDEGGLHIEPGLGLGHRRLSIIDLSTGQ
QPLYNEDKSVCVVFNGEIYNYQELIPELQALGHVFHTRSDTEVIVHAWEAWGERCVDRFR
GMFAFALWDRNRETLFLARDRLGVKPLFYALLDDGSFLFGSELKSLLAHGGLKRDIDPCA
VEEYFALGYVAEPRAIFKQARKLPPACTLLLRRGQPVGQPREYWDVRFTLDNPISDADAQ
AELTHRLEESIKLRMISEVPLGAFLSGGVDSSAVVAMMAGLSANPVNTCSIGFSDPAFNE
SEFARMVADRYHTNHHLDVVESDDFDLIDTLARLYDEPYADSSAIPTYRVCQLARKHVTV
ALSGDGGDESFGGYRRYKLHLMEEKMRSALPLGLRRPLFGTLGKLYPKADWAPRVFRAKT
TFEGIARSSVEGYFHSVSILRAPMRNQLFSPQFKAALGGYDALQVFTDHAAKADTQDPLA
LIQYLDLKTYLIGDINTKVDRASMAHSLEVREPLMDHKLVEWLATLPSTQKIRGQEGKYL
LKKAMEPHLPNDVLYRPKMGFSVPLARWFRGPLKARVQESILGSRLADTGWFNRDYLQEL
VRDHNNGNRDYSASIWTILMLEAFLRNVMEAGEAA
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