SitesBLAST
Comparing Ga0059261_0317 FitnessBrowser__Korea:Ga0059261_0317 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 hits to proteins with known functional sites (download)
1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
53% identity, 99% coverage: 8:518/518 of query aligns to 8:501/501 of 1gpmA
- active site: G57 (≠ S57), C84 (= C84), Y85 (= Y85), H179 (= H174), E181 (= E176), D237 (= D232), K357 (= K374)
- binding adenosine monophosphate: G231 (= G226), L232 (= L227), S233 (= S228), V258 (= V253), F313 (= F308)
- binding pyrophosphate 2-: S233 (= S228), G235 (= G230), V236 (= V231), D237 (= D232), S238 (= S233), K357 (= K374)
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
51% identity, 100% coverage: 1:518/518 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)
40% identity, 99% coverage: 6:518/518 of query aligns to 7:555/555 of Q8IJR9
- Y18 (≠ V17) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- H20 (≠ Q19) 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 (≠ R23) 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 (= R24) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- C89 (= C84) 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 (= Q88) binding
- C113 (≠ R108) 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 (≠ W124) 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 (= W133) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ S135) binding ; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (= D138) binding ; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H174) binding
- Y212 (≠ V178) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ H179) 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 (= R301) binding
- D371 (= D333) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- E374 (= E336) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- K376 (≠ S339) 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 (= K349) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- T387 (≠ S350) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- H388 (= H351) 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 (= H352) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- N390 (= N353) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- K411 (= K374) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- D412 (= D375) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- D413 (≠ E376) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- K415 (≠ R378) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- Q476 (= Q439) binding
- R539 (= R502) mutation to L: 85 percent decrease in glutaminase activity.
- K547 (= K510) binding ; mutation to L: 85 percent decrease in glutaminase activity.
- I552 (= I515) binding
- E553 (= E516) binding ; mutation to L: 85 percent decrease in glutaminase activity.
- E555 (= E518) 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
47% identity, 99% coverage: 8:518/518 of query aligns to 2:475/475 of 2ywcA
- active site: G51 (≠ S57), R53 (≠ A59), C78 (= C84), Y79 (= Y85), H164 (= H174), E166 (= E176), D221 (= D232), K343 (= K374)
- binding xanthosine-5'-monophosphate: R288 (= R301), P366 (= P397), G367 (= G398), P368 (= P399), Q408 (= Q439), K467 (= K510), T471 (= T514), I472 (= I515), E473 (= E516)
4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
38% identity, 99% coverage: 6:518/518 of query aligns to 1:525/525 of 4wioA
- active site: G52 (≠ S57), A83 (≠ C84), Y84 (= Y85), H197 (= H174), E199 (= E176), D255 (= D232), K393 (= K374)
- binding glutamine: Q87 (= Q88), N158 (≠ S135), H159 (= H136), N160 (≠ G137), D161 (= D138), H197 (= H174)
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
37% identity, 99% coverage: 6:518/518 of query aligns to 2:517/517 of 3uowA
- active site: G53 (≠ S57), C84 (= C84), Y85 (= Y85), H198 (= H174), E200 (= E176), D255 (= D232), K381 (= K374)
- binding xanthosine-5'-monophosphate: R325 (= R301), P404 (= P397), G405 (= G398), P406 (= P399), Q446 (= Q439), K509 (= K510), T513 (= T514), I514 (= I515), E515 (= E516)
3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
38% identity, 99% coverage: 8:518/518 of query aligns to 2:477/477 of 3uowB
- active site: G47 (≠ S57), C67 (= C84), Y68 (= Y85), H162 (= H174), E164 (= E176), D218 (= D232), K340 (= K374)
- binding xanthosine-5'-monophosphate: R288 (= R301), P363 (= P397), G364 (= G398), P365 (= P399), Q405 (= Q439), K469 (= K510), T473 (= T514), I474 (= I515), E475 (= E516)
2vxoB Human gmp synthetase in complex with xmp (see paper)
38% identity, 98% coverage: 7:515/518 of query aligns to 5:540/658 of 2vxoB
- active site: G55 (≠ S57), C82 (= C84), Y83 (= Y85), H165 (= H174), E167 (= E176), D223 (= D232), K381 (= K374)
- binding xanthosine-5'-monophosphate: R302 (= R301), G348 (= G343), K349 (≠ P344), P404 (= P397), G405 (= G398), P406 (= P399), R489 (= R457)
Sites not aligning to the query:
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
37% identity, 98% coverage: 7:515/518 of query aligns to 27:575/693 of P49915
- C104 (= C84) active site, For GATase activity
- H190 (= H174) active site, For GATase activity
- E192 (= E176) active site, For GATase activity
- R337 (= R301) binding
- D522 (= D455) binding
Sites not aligning to the query:
- 610 binding
- 685 binding
- 691 binding
6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
53% identity, 61% coverage: 205:518/518 of query aligns to 6:298/298 of 6jp9A
7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
34% identity, 37% coverage: 8:198/518 of query aligns to 2:181/183 of 7yc6A
P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
30% identity, 35% coverage: 8:187/518 of query aligns to 4:183/193 of P00900
- C84 (= C84) active site, Nucleophile; for GATase activity
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1i7qB Anthranilate synthase from s. Marcescens (see paper)
30% identity, 35% coverage: 8:187/518 of query aligns to 3:182/192 of 1i7qB
- active site: G58 (≠ A59), C83 (= C84), L84 (≠ Y85), H169 (= H174), E171 (= E176)
- binding glutamic acid: P55 (≠ G56), G56 (≠ S57), G58 (≠ A59), C83 (= C84), L84 (≠ Y85), Q87 (= Q88), H132 (= H136), S133 (≠ D138), L134 (≠ K139)
P07259 Multifunctional protein URA2; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 37% coverage: 8:198/518 of query aligns to 229:411/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
31% identity, 26% coverage: 56:190/518 of query aligns to 58:187/673 of 8hx8A
Sites not aligning to the query:
- binding magnesium ion: 521, 655, 658
- binding tryptophan: 231, 232, 233, 241, 243, 458, 459, 460, 614
Q09794 Multifunctional protein ura1; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 43% coverage: 8:231/518 of query aligns to 265:485/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
27% identity, 36% coverage: 8:192/518 of query aligns to 2:186/187 of P00903
- C79 (= C84) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H174) mutation to Q: Loss of activity.
- E170 (= E176) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.
7d54A Crstal structure msgatase with gln (see paper)
30% identity, 20% coverage: 75:177/518 of query aligns to 92:182/242 of 7d54A
Sites not aligning to the query:
Q9LVW7 Carbamoyl phosphate synthase small chain, chloroplastic; Carbamoyl phosphate synthetase glutamine chain; Protein VENOSA 6; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 18% coverage: 2:96/518 of query aligns to 236:330/430 of Q9LVW7
Sites not aligning to the query:
- 410 H→Y: In ven6-1; reticulate leaf phenotype.
Query Sequence
>Ga0059261_0317 FitnessBrowser__Korea:Ga0059261_0317
MTQPGESILIVDFGSQVTQLIARRVREAGVYSEIAPFNAAAEAFERMKPGGVILSGSPAS
VLEDGSPRVPQAIFESGLPVLGICYGQQVMMQQLGGNVQLGDSGEFGRAFIEIADSCVLF
DGLWAEGETHQVWMSHGDKVTSLAPGFRPVAASAGAPFAVIADDTRRYYAMQFHPEVVHT
PDGAKLLANFVRHVCGLKGDWTMAEFRQTKIEEIRKQVGTGKVICGLSGGVDSAVAAVLI
HEAIGEQLTCVFVDHGLMRSGEADQVVSLFRGHYNIPLVHVNAETLFLNGLAGVTDPEAK
RKFIGKTFIDVFEEEAKKIGGAEFLAQGTLYPDVIESVSFTGGPSVTIKSHHNVGGLPER
MNMKLVEPLRELFKDEVRALGRELGLPDVFVGRHPFPGPGLAIRIPGEVTKERCDILRKA
DAVYLEEIRNAGLYDAIWQAFAVLLPVKTVGVMGDGRTYDSVCGLRAVTSTDGMTADVYP
FDASFLTRVATRIVNEVKGVNRVVYDYTSKPPGTIEWE
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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