SitesBLAST
Comparing SMc00394 FitnessBrowser__Smeli:SMc00394 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
52% identity, 100% coverage: 3:520/520 of query aligns to 1:501/501 of 1gpmA
- active site: G57 (≠ S59), C84 (= C86), Y85 (= Y87), H179 (= H176), E181 (= E178), D237 (= D234), K357 (= K376)
- binding adenosine monophosphate: G231 (≠ A228), L232 (= L229), S233 (= S230), V258 (= V255), F313 (= F310)
- binding pyrophosphate 2-: S233 (= S230), G235 (= G232), V236 (= V233), D237 (= D234), S238 (= S235), K357 (= K376)
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
49% identity, 100% coverage: 1:520/520 of query aligns to 1:490/490 of 5tw7F
Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
41% identity, 99% coverage: 8:520/520 of query aligns to 7:555/555 of Q8IJR9
- Y18 (≠ V19) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- H20 (≠ Q21) mutation to A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
- K24 (≠ R25) mutation to L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
- R25 (= R26) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- C89 (= C86) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
- Q93 (= Q90) binding L-glutamine
- C113 (vs. gap) mutation to A: 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-89.
- K160 (≠ W126) mutation to L: No effect on glutaminase activity. 1.2-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
- W167 (= W135) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ S137) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (= D140) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H176) binding L-glutamine
- Y212 (≠ V180) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ H181) mutation to A: 40 percent decrease in glutaminase activity. 1.4-fold decrease in affinity for glutamine. 1.3-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
- R336 (= R303) binding XMP
- D371 (= D335) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- E374 (= E338) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- K376 (≠ S341) mutation to L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
- K386 (= K351) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- T387 (≠ S352) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- H388 (= H353) Important for ATPPase activity; mutation to A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
- H389 (= H354) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- N390 (= N355) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- K411 (= K376) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- D412 (= D377) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- D413 (≠ E378) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- K415 (≠ R380) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- Q476 (= Q441) binding XMP
- R539 (= R504) mutation to L: 85 percent decrease in glutaminase activity.
- K547 (= K512) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- I552 (= I517) binding XMP
- E553 (= E518) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- E555 (= E520) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.
2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
48% identity, 98% coverage: 10:520/520 of query aligns to 2:475/475 of 2ywcA
- active site: G51 (≠ S59), R53 (≠ A61), C78 (= C86), Y79 (= Y87), H164 (= H176), E166 (= E178), D221 (= D234), K343 (= K376)
- binding xanthosine-5'-monophosphate: R288 (= R303), P366 (= P399), G367 (= G400), P368 (= P401), Q408 (= Q441), K467 (= K512), T471 (= T516), I472 (= I517), E473 (= E518)
4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
39% identity, 99% coverage: 8:520/520 of query aligns to 1:525/525 of 4wioA
- active site: G52 (≠ S59), A83 (≠ C86), Y84 (= Y87), H197 (= H176), E199 (= E178), D255 (= D234), K393 (= K376)
- binding glutamine: Q87 (= Q90), N158 (≠ S137), H159 (= H138), N160 (≠ G139), D161 (= D140), H197 (= H176)
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
38% identity, 99% coverage: 8:520/520 of query aligns to 2:517/517 of 3uowA
- active site: G53 (≠ S59), C84 (= C86), Y85 (= Y87), H198 (= H176), E200 (= E178), D255 (= D234), K381 (= K376)
- binding xanthosine-5'-monophosphate: R325 (= R303), P404 (= P399), G405 (= G400), P406 (= P401), Q446 (= Q441), K509 (= K512), T513 (= T516), I514 (= I517), E515 (= E518)
3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 98% coverage: 10:520/520 of query aligns to 2:477/477 of 3uowB
- active site: G47 (≠ S59), C67 (= C86), Y68 (= Y87), H162 (= H176), E164 (= E178), D218 (= D234), K340 (= K376)
- binding xanthosine-5'-monophosphate: R288 (= R303), P363 (= P399), G364 (= G400), P365 (= P401), Q405 (= Q441), K469 (= K512), T473 (= T516), I474 (= I517), E475 (= E518)
6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
51% identity, 60% coverage: 211:520/520 of query aligns to 10:298/298 of 6jp9A
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
36% identity, 96% coverage: 10:507/520 of query aligns to 28:562/693 of P49915
- C104 (= C86) active site, For GATase activity
- H190 (= H176) active site, For GATase activity
- E192 (= E178) active site, For GATase activity
- R337 (= R303) binding XMP
- D522 (= D457) binding XMP
Sites not aligning to the query:
- 610 binding XMP
- 685 binding XMP
- 691 binding XMP
2vxoB Human gmp synthetase in complex with xmp (see paper)
36% identity, 96% coverage: 10:507/520 of query aligns to 6:527/658 of 2vxoB