SitesBLAST
Comparing HSERO_RS19440 FitnessBrowser__HerbieS:HSERO_RS19440 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)
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)
63% identity, 97% coverage: 1:185/191 of query aligns to 1:185/187 of P00903
- C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H168) mutation to Q: Loss of activity.
- E170 (= E170) 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.
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)
49% identity, 96% coverage: 2:185/191 of query aligns to 75:264/276 of Q42565
- G150 (= G77) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
- G176 (= G102) 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)
51% identity, 95% coverage: 3:184/191 of query aligns to 7:187/673 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
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)
44% identity, 97% coverage: 2:186/191 of query aligns to 4:188/193 of P00900
- C84 (= C79) 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)
44% identity, 97% coverage: 2:186/191 of query aligns to 3:187/192 of 1i7qB
- active site: G58 (≠ C54), C83 (= C79), L84 (= L80), H169 (= H168), E171 (= E170)
- binding glutamic acid: P55 (= P51), G56 (= G52), G58 (≠ C54), C83 (= C79), L84 (= L80), Q87 (= Q83), H132 (= H128), S133 (= S129), L134 (= L130)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
41% identity, 95% coverage: 3:184/191 of query aligns to 6:144/632 of 8hx9A
Sites not aligning to the query:
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: 453, 454, 455, 456, 547, 570, 590, 603, 604, 605, 606, 619, 623
- binding tryptophan: 189, 190, 191, 199, 201, 419, 420, 421, 574, 575
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)
32% identity, 71% coverage: 41:176/191 of query aligns to 280:410/430 of Q9LVW7
- H410 (= H176) mutation to Y: In ven6-1; reticulate leaf phenotype.
7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
30% identity, 96% coverage: 1:184/191 of query aligns to 1:174/183 of 7yc6A
2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
29% identity, 97% coverage: 1:186/191 of query aligns to 1:182/475 of 2ywcA
Sites not aligning to the query:
1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
29% identity, 81% coverage: 27:181/191 of query aligns to 215:365/379 of 1ce8B
Sites not aligning to the query:
P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
29% identity, 81% coverage: 27:181/191 of query aligns to 216:366/382 of P0A6F1
- G241 (= G52) binding
- G243 (≠ C54) binding
- L270 (= L80) binding
- Q273 (= Q83) binding
- N311 (≠ Y127) binding
- G313 (≠ S129) binding
- F314 (≠ L130) binding
Sites not aligning to the query:
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
31% identity, 80% coverage: 33:185/191 of query aligns to 36:188/490 of 5tw7F
Sites not aligning to the query:
1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
29% identity, 81% coverage: 27:181/191 of query aligns to 215:365/379 of 1c3oB
- active site: S268 (≠ C79), H352 (= H168), E354 (= E170)
- binding glutamine: N239 (≠ P51), G240 (= G52), G242 (≠ C54), S268 (≠ C79), L269 (= L80), N310 (≠ Y127), H311 (= H128), G312 (≠ S129), F313 (≠ L130)
Sites not aligning to the query:
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
24% identity, 79% coverage: 34:184/191 of query aligns to 35:214/517 of 3uowA
Sites not aligning to the query:
Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
24% identity, 79% coverage: 34:184/191 of query aligns to 40:224/555 of Q8IJR9
- C89 (= C79) 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 (= Q83) binding
- C113 (≠ K103) 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 (≠ P119) 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 (≠ Y127) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ S129) binding ; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (≠ I132) binding ; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H168) binding
- Y212 (≠ I172) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ L173) 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.
Sites not aligning to the query:
- 18 Y→F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- 20 H→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.
- 24 K→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.
- 25 R→L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- 336 binding
- 371 Important for ATPPase activity; D→A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- 374 E→L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- 376 K→L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
- 386 K→L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- 387 T→A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- 388 Important for ATPPase activity; H→A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
- 389 Important for ATPPase activity; H→A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- 390 N→A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- 411 K→L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- 412 D→A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- 413 D→A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- 415 K→L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- 476 binding
- 539 R→L: 85 percent decrease in glutaminase activity.
- 547 binding ; K→L: 85 percent decrease in glutaminase activity.
- 552 binding
- 553 binding ; E→L: 85 percent decrease in glutaminase activity.
- 555 E→L: 20 percent decrease in glutaminase activity. No effect on GMP formation.
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
29% identity, 61% coverage: 69:185/191 of query aligns to 94:207/693 of P49915
- C104 (= C79) active site, For GATase activity
- H190 (= H168) active site, For GATase activity
- E192 (= E170) active site, For GATase activity
Sites not aligning to the query:
- 337 binding
- 522 binding
- 610 binding
- 685 binding
- 691 binding
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)
27% identity, 83% coverage: 13:171/191 of query aligns to 274:425/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
2vxoB Human gmp synthetase in complex with xmp (see paper)
30% identity, 61% coverage: 69:185/191 of query aligns to 72:182/658 of 2vxoB
Sites not aligning to the query:
- active site: 55, 223, 381
- binding xanthosine-5'-monophosphate: 302, 348, 349, 404, 405, 406, 489, 575, 610, 650, 654, 655, 656
Q18990 Multifunctional protein pyr-1; 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 Caenorhabditis elegans (see 3 papers)
30% identity, 64% coverage: 49:170/191 of query aligns to 223:341/2198 of Q18990
Sites not aligning to the query:
- 1602 H→Q: In cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50% of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background, prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background.
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)
29% identity, 83% coverage: 13:171/191 of query aligns to 238:389/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
Query Sequence
>HSERO_RS19440 FitnessBrowser__HerbieS:HSERO_RS19440
MLLMIDNYDSFTYNLVQYFGELGEEVLTIRNDEITLDDIRKLNPERICLSPGPCSPKEAG
ICVDLLKEFSGKLPILGVCLGHQAIGEAFGGNIIRAKQVMHGKTSKIAHTGVGVFQDLPS
PYTVIRYHSLAIERATLPDCLEVTAWTDDGEIMGVRHKEFDLQGVQFHPESILSEHGHAL
LKNFLSGSAHG
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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