SitesBLAST
Comparing HSERO_RS11020 FitnessBrowser__HerbieS:HSERO_RS11020 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)
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
69% identity, 99% coverage: 5:530/530 of query aligns to 2:490/490 of 5tw7F
1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
63% identity, 100% coverage: 2:530/530 of query aligns to 2:501/501 of 1gpmA
- active site: G57 (= G58), C84 (= C85), Y85 (= Y86), H179 (= H180), E181 (= E182), D237 (= D238), K357 (= K380)
- binding adenosine monophosphate: G231 (= G232), L232 (= L233), S233 (= S234), V258 (= V259), F313 (= F314)
- binding pyrophosphate 2-: S233 (= S234), G235 (= G236), V236 (= V237), D237 (= D238), S238 (= S239), K357 (= K380)
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, 100% coverage: 1:530/530 of query aligns to 1:555/555 of Q8IJR9
- Y18 (≠ V18) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- H20 (≠ Q20) 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 (≠ R24) 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 (= R25) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- C89 (= C85) 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 (= Q89) binding L-glutamine
- C113 (≠ Y109) 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 (vs. gap) 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 (= W139) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ S141) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (= D144) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H180) binding L-glutamine
- Y212 (≠ T184) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ H185) 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 (= R307) binding XMP
- D371 (= D339) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- E374 (= E342) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- K376 (≠ A344) 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 (= K355) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- T387 (≠ S356) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- H388 (= H357) 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 (= H358) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- N390 (= N359) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- K411 (= K380) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- D412 (= D381) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- D413 (≠ E382) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- K415 (≠ R384) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- Q476 (= Q451) binding XMP
- R539 (= R514) mutation to L: 85 percent decrease in glutaminase activity.
- K547 (= K522) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- I552 (= I527) binding XMP
- E553 (= E528) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- E555 (= E530) 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, 98% coverage: 9:530/530 of query aligns to 2:475/475 of 2ywcA
- active site: G51 (= G58), R53 (≠ N60), C78 (= C85), Y79 (= Y86), H164 (= H180), E166 (= E182), D221 (= D238), K343 (= K380)
- binding xanthosine-5'-monophosphate: R288 (= R307), P366 (= P403), G367 (= G404), P368 (= P405), Q408 (= Q451), K467 (= K522), T471 (= T526), I472 (= I527), E473 (= E528)
4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
38% identity, 99% coverage: 8:530/530 of query aligns to 2:525/525 of 4wioA
- active site: G52 (= G58), A83 (≠ C85), Y84 (= Y86), H197 (= H180), E199 (= E182), D255 (= D238), K393 (= K380)
- binding glutamine: Q87 (= Q89), N158 (≠ S141), H159 (= H142), N160 (≠ G143), D161 (= D144), H197 (= H180)
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
38% identity, 99% coverage: 6:530/530 of query aligns to 1:517/517 of 3uowA
- active site: G53 (= G58), C84 (= C85), Y85 (= Y86), H198 (= H180), E200 (= E182), D255 (= D238), K381 (= K380)
- binding xanthosine-5'-monophosphate: R325 (= R307), P404 (= P403), G405 (= G404), P406 (= P405), Q446 (= Q451), K509 (= K522), T513 (= T526), I514 (= I527), E515 (= E528)
3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 99% coverage: 8:530/530 of query aligns to 1:477/477 of 3uowB
- active site: G47 (= G58), C67 (= C85), Y68 (= Y86), H162 (= H180), E164 (= E182), D218 (= D238), K340 (= K380)
- binding xanthosine-5'-monophosphate: R288 (= R307), P363 (= P403), G364 (= G404), P365 (= P405), Q405 (= Q451), K469 (= K522), T473 (= T526), I474 (= I527), E475 (= E528)
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
37% identity, 98% coverage: 4:523/530 of query aligns to 23:567/693 of P49915
- C104 (= C85) active site, For GATase activity
- H190 (= H180) active site, For GATase activity
- E192 (= E182) active site, For GATase activity
- R337 (= R307) binding XMP
- D522 (= D467) 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)
38% identity, 98% coverage: 4:523/530 of query aligns to 1:532/658 of 2vxoB
- active site: G55 (= G58), C82 (= C85), Y83 (= Y86), H165 (= H180), E167 (= E182), D223 (= D238), K381 (= K380)
- binding xanthosine-5'-monophosphate: R302 (= R307), G348 (= G347), K349 (= K348), P404 (= P403), G405 (= G404), P406 (= P405), R489 (= R469)
Sites not aligning to the query:
6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
50% identity, 60% coverage: 212:530/530 of query aligns to 7:298/298 of 6jp9A
7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
34% identity, 37% coverage: 9:202/530 of query aligns to 2:179/183 of 7yc6A
Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 37% coverage: 2:197/530 of query aligns to 68:264/276 of Q42565
- G150 (= G83) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
- G176 (= G116) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
26% identity, 36% coverage: 6:196/530 of query aligns to 3:187/673 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
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)
26% identity, 28% coverage: 53:199/530 of query aligns to 47:187/187 of P00903
- C79 (= C85) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H180) mutation to Q: Loss of activity.
- E170 (= E182) 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.
8rp0AAA Aminodeoxychorismate synthase component 1
26% identity, 28% coverage: 53:199/530 of query aligns to 48:188/188 of 8rp0AAA
8rp6AAA Aminodeoxychorismate synthase component 2
26% identity, 28% coverage: 53:199/530 of query aligns to 49:189/189 of 8rp6AAA
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)
27% identity, 35% coverage: 7:193/530 of query aligns to 2:183/193 of P00900
- C84 (= C85) 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)
27% identity, 35% coverage: 7:193/530 of query aligns to 1:182/192 of 1i7qB
- active site: G58 (≠ N60), C83 (= C85), L84 (≠ Y86), H169 (= H180), E171 (= E182)
- binding glutamic acid: P55 (≠ G57), G56 (= G58), G58 (≠ N60), C83 (= C85), L84 (≠ Y86), Q87 (= Q89), H132 (= H142), S133 (≠ G143), L134 (≠ D144)
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)
28% identity, 33% coverage: 8:184/530 of query aligns to 243:406/430 of Q9LVW7
Sites not aligning to the query:
- 410 H→Y: In ven6-1; reticulate leaf phenotype.
P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
28% identity, 33% coverage: 8:182/530 of query aligns to 177:338/2225 of P08955
Sites not aligning to the query:
- 1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.
Query Sequence
>HSERO_RS11020 FitnessBrowser__HerbieS:HSERO_RS11020
MSTHSHSKILILDFGSQVTQLIARRVREAGVFSEVFPHDVTDEFVRNYGAAGVILSGGPN
SVTEGDTPRAPQAVFELGVPVLGICYGMQTMAEQLGGKVDNGHLREFGYAEVRAHGHTKL
LDNISDFTNAQGHGMLKVWMSHGDKVNEMPAGFKLMASTGNCPIAGMADEERRFYGVQFH
PEVTHTVQGKAMLGRFVHEICGCQSDWNMPDYIAEAVEMIRQQVGSDEVILGLSGGVDSS
VAAALIHRAIGDQLTCVFVDHGLLRLDEGKMVMEMFAKNLGVKVIHVDATAQFMGHLAGV
TDPEAKRKIIGREFVEVFQAESAKLTSAKWLAQGTIYPDVIESAGKGKKTAHTIKSHHNV
GGLPETLNLKLLEPLRELFKDEVRELGVALGLPPEMVYRHPFPGPGLGVRILGEVKKEYA
DLLRRADAIFIEELRNTKDEDGQTWYEKTSQAFAVFLPVKSVGVMGDGRTYEYVVALRAV
QTQDFMTAHWAHLPHELLGRVSNRIINEVRGLNRVVYDISGKPPATIEWE
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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