SitesBLAST
Comparing WP_012505082.1 NCBI__GCF_000020625.1:WP_012505082.1 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 20 (the maximum) hits to proteins with known functional sites (download)
Q42601 Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic; CPS; CPSase; Ammonium-dependent carbamoyl phosphate synthetase; Arginine-specific carbamoyl phosphate synthetase, ammonia chain; Glutamine-dependent carbamoyl phosphate synthetase; Protein VENOSA 3; EC 6.3.4.16; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
61% identity, 98% coverage: 3:485/495 of query aligns to 94:567/1187 of Q42601
- P149 (≠ V58) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
Sites not aligning to the query:
- 587 G→E: In ven3-3; reticulate leaf phenotype.
- 844 A→T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- 1014 P→L: In ven3-1; reticulate leaf phenotype.
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
62% identity, 97% coverage: 1:482/495 of query aligns to 1:473/1058 of 1t36A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), E208 (= E208), L210 (= L210), I211 (= I211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (≠ V375)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
Sites not aligning to the query:
- active site: 507, 634, 715, 746, 754, 814, 826, 828, 833, 886
- binding adenosine-5'-diphosphate: 715, 718, 740, 741, 746, 770, 771, 772, 773, 826, 894
- binding manganese (ii) ion: 814, 826
- binding L-ornithine: 768, 776, 877, 892, 1026, 1027
- binding uridine-5'-monophosphate: 939, 959, 961, 962, 978, 1000, 1001, 1002, 1011, 1014
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
62% identity, 97% coverage: 1:482/495 of query aligns to 1:473/1058 of 1c3oA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (= L210), I211 (= I211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (≠ V375)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
Sites not aligning to the query:
- active site: 507, 634, 715, 746, 754, 814, 826, 828, 833, 886
- binding adenosine-5'-diphosphate: 715, 718, 740, 741, 746, 770, 771, 772, 773, 774, 826
- binding glutamine: 528, 537, 538, 554
- binding manganese (ii) ion: 814, 826
- binding L-ornithine: 768, 776, 877, 892, 1026, 1027
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
62% identity, 97% coverage: 1:482/495 of query aligns to 1:473/1073 of 1bxrA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (= L210), I211 (= I211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), E299 (= E299), R306 (= R306), T376 (≠ V375)
- binding manganese (ii) ion: E299 (= E299), N301 (= N301)
Sites not aligning to the query:
- active site: 507, 634, 715, 721, 722, 745, 761, 769, 829, 841, 843, 848, 901
- binding phosphoaminophosphonic acid-adenylate ester: 675, 713, 715, 720, 721, 722, 725, 753, 755, 756, 761, 785, 786, 787, 788, 829, 841, 843, 848
- binding manganese (ii) ion: 829, 841, 841, 843
- binding L-ornithine: 783, 791, 892, 907, 1041, 1042
P00968 Carbamoyl phosphate synthase large chain; Carbamoyl phosphate synthetase ammonia chain; EC 6.3.4.16; EC 6.3.5.5 from Escherichia coli (strain K12) (see 6 papers)
62% identity, 97% coverage: 1:482/495 of query aligns to 1:473/1073 of P00968
- M1 (= M1) modified: Initiator methionine, Removed
- R129 (= R129) binding
- R169 (= R169) binding
- G175 (= G175) binding
- G176 (= G176) binding
- E208 (= E208) binding
- L210 (= L210) binding
- E215 (= E215) binding
- G241 (= G241) binding
- I242 (≠ V242) binding
- H243 (= H243) binding
- Q285 (= Q285) binding ; binding
- E299 (= E299) binding ; binding ; binding
- N301 (= N301) binding
Sites not aligning to the query:
- 715 binding
- 754 binding
- 756 binding
- 761 binding
- 786 binding
- 787 binding
- 788 binding
- 789 binding
- 829 binding ; binding
- 841 binding ; binding ; binding
- 843 binding
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
62% identity, 97% coverage: 1:482/495 of query aligns to 1:473/1058 of 1a9xA
- active site: K202 (≠ G202), D338 (= D338)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (= L210), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (≠ V375)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301)
- binding phosphate ion: G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
Sites not aligning to the query:
- active site: 507, 634, 754, 886
- binding adenosine-5'-diphosphate: 715, 718, 740, 741, 746, 770, 771, 772, 773, 826
- binding manganese (ii) ion: 814, 826
- binding L-ornithine: 768, 776, 877, 892, 1025, 1026, 1027
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
62% identity, 97% coverage: 1:482/495 of query aligns to 1:473/1058 of 1ce8A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (= L210), I211 (= I211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (≠ V375)
- binding manganese (ii) ion: M174 (≠ L174), Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
Sites not aligning to the query:
- active site: 507, 634, 715, 746, 754, 814, 826, 828, 833, 886
- binding adenosine-5'-diphosphate: 715, 740, 741, 746, 770, 771, 772, 773, 774, 826
- binding inosinic acid: 933, 939, 959, 961, 962, 978, 979, 986, 1000, 1001, 1002, 1010, 1011, 1013
- binding manganese (ii) ion: 814, 826
- binding L-ornithine: 528, 537, 538, 552, 554, 768, 776, 877, 892, 1025, 1026, 1027
P03965 Carbamoyl phosphate synthase arginine-specific large chain; CPS; CPSase; CPSase-arg; Ammonium-dependent carbamoyl phosphate synthetase; Arginine-specific carbamoyl phosphate synthetase, ammonia chain; Carbamoyl phosphate synthase A; CPS-A; Glutamine-dependent carbamoyl phosphate synthetase; EC 6.3.4.16; EC 6.3.5.5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
47% identity, 97% coverage: 5:485/495 of query aligns to 26:489/1118 of P03965
- L229 (= L210) mutation to G: Abolishes ammonia-dependent ATPase activity.
- H262 (= H243) mutation to N: No effect.
- D265 (= D246) mutation D->A,E,N: Reduces ammonia-dependent ATPase activity 17-58 fold.
- I316 (= I298) mutation I->G,S,H: Reduces ammonia-dependent ATPase activity 17-64 fold.
Sites not aligning to the query:
- 807 H→N: No effect.
- 810 mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
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)
47% identity, 97% coverage: 8:485/495 of query aligns to 391:851/2198 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.
P05990 Multifunctional protein r; Protein rudimentary; 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 Drosophila melanogaster (Fruit fly) (see 2 papers)
44% identity, 97% coverage: 1:479/495 of query aligns to 402:859/2224 of P05990
Sites not aligning to the query:
- 1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
- 1883 modified: Phosphoserine
- 1885 modified: Phosphoserine
- 1892 modified: Phosphoserine
- 1894 modified: Phosphoserine
P20054 Multifunctional protein pyr1-3; 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 Dictyostelium discoideum (Social amoeba)
45% identity, 98% coverage: 7:490/495 of query aligns to 404:868/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
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)
46% identity, 96% coverage: 4:479/495 of query aligns to 435:890/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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)
45% identity, 95% coverage: 8:479/495 of query aligns to 394:844/2225 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.
P27708 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 Homo sapiens (Human) (see 7 papers)
44% identity, 95% coverage: 8:479/495 of query aligns to 394:844/2225 of P27708
- T456 (= T70) modified: Phosphothreonine; by MAPK1
- Y735 (= Y353) to C: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
- 177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
- 1406 modified: Phosphoserine; by PKA
- 1471 binding ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding ; H→A: No zinc-binding and no catalytic activity.
- 1475 binding
- 1505 binding
- 1512 D→N: No change in catalytic activity.
- 1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
- 1562 T→A: Abolishes dihydroorotase activity.
- 1563 F→A: Abolishes dihydroorotase activity.
- 1590 binding ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding ; C→S: Reduces dihydroorotase activity.
- 1614 binding ; H→A: Abolishes dihydroorotase activity.
- 1637 binding ; E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding
- 1686 binding ; D→N: Abolishes dihydroorotase activity.
- 1690 binding ; H→N: 3% of wild-type catalytic activity.
- 1702 binding
- 1789:2225 natural variant: Missing (in DEE50; uncertain significance)
- 1859 modified: Phosphoserine; by RPS6KB1 and PKA
- 1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
- 1900 modified: Phosphoserine
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
42% identity, 98% coverage: 4:488/495 of query aligns to 419:894/1500 of P07756
- S537 (≠ K119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
Sites not aligning to the query:
- 1331 modified: carbohydrate, O-linked (GlcNAc) serine
- 1332 modified: carbohydrate, O-linked (GlcNAc) threonine
- 1391 T→V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- 1394 T→A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- 1410 W→K: 60-fold increase in the activation constant of NAG.
- 1437 N→D: 70-fold increase in the activation constant of NAG.
- 1440 N→D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG.
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
42% identity, 98% coverage: 4:488/495 of query aligns to 419:894/1500 of Q8C196
Sites not aligning to the query:
- 44 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- 287 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- 1291 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
42% identity, 98% coverage: 4:488/495 of query aligns to 419:894/1500 of P31327
- A438 (= A23) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- K453 (= K38) modified: N6-glutaryllysine; alternate
- K458 (≠ R43) modified: N6-glutaryllysine; alternate
- K527 (≠ E109) modified: N6-glutaryllysine; alternate
- G530 (= G112) to V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
- K532 (≠ E114) modified: N6-glutaryllysine; alternate
- T544 (≠ A126) to M: in CPS1D; almost complete loss of enzyme activity; approximately 60-fold increase in the apparent Km for bicarbonate and approximately 4-fold respective decrease and increase in the apparent Vmax and Km for ammonia; dbSNP:rs121912592
- K553 (≠ A135) modified: N6-glutaryllysine; alternate
- Q678 (= Q262) to P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- K728 (= K313) modified: N6-glutaryllysine
- K757 (≠ S342) modified: N6-glutaryllysine; alternate
- K772 (= K357) modified: N6-glutaryllysine; alternate
- P774 (= P359) to L: in CPS1D; the enzyme is inactive
- K793 (= K378) modified: N6-glutaryllysine; alternate
- K811 (= K396) modified: N6-glutaryllysine; alternate
- K841 (≠ E435) modified: N6-glutaryllysine; alternate
- L843 (≠ I437) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (= R444) to C: in CPS1D; moderate decrease in protein yield and partial loss of enzyme activity; dbSNP:rs1015051007; to H: in CPS1D; partial loss of enzyme activity; dbSNP:rs767694281
- K856 (≠ Y450) modified: N6-glutaryllysine; alternate
- K869 (≠ E463) modified: N6-glutaryllysine
- T871 (= T465) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (≠ P469) modified: N6-glutaryllysine; alternate; to E: associated in cis with S-843 in a patient with carbamoyl-phosphate synthase deficiency; does not affect enzyme activity; significant decrease in protein yield and thermal stability; dbSNP:rs147062907
- K889 (≠ A483) modified: N6-glutaryllysine; alternate
- K892 (≠ R486) modified: N6-glutaryllysine; alternate
Sites not aligning to the query:
- 55 modified: N6-glutaryllysine; alternate
- 123 S → F: in CPS1D; modestly decreases enzyme activity; S → Y: in CPS1D; uncertain significance
- 171 modified: N6-glutaryllysine; alternate
- 174 R → W: in CPS1D; uncertain significance; dbSNP:rs1553509661
- 176 modified: N6-glutaryllysine
- 207 modified: N6-glutaryllysine; alternate
- 210 modified: N6-glutaryllysine; alternate
- 214 modified: N6-glutaryllysine; alternate
- 219 modified: N6-glutaryllysine; alternate
- 228 modified: N6-glutaryllysine; alternate
- 237 modified: N6-glutaryllysine
- 280 modified: N6-glutaryllysine; alternate
- 304 A → V: in CPS1D; associated with T-986; dbSNP:rs775920437
- 307 modified: N6-glutaryllysine; alternate
- 310 modified: N6-glutaryllysine; alternate
- 337 H → R: in CPS1D; modestly decreases enzyme activity; dbSNP:rs28940283
- 344 T → A: no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs1047883
- 355 N → D: in CPS1D; around 80% decrease in enzyme activity; significant reduction in thermal stability; approximately 4-fold decrease in the apparent Vmax for ATP, bicarbonate and ammonia; dbSNP:rs1472190012
- 389 Y → C: in CPS1D; around 40% decrease in enzyme activity; significant loss of thermal stability
- 390 L → R: in CPS1D; significant loss of protein stability
- 401 G → R: in CPS1D; uncertain significance; associated with N-937 in a patient; dbSNP:rs760895692
- 402 modified: N6-glutaryllysine; alternate
- 412 modified: N6-glutaryllysine; alternate
- 905 modified: N6-glutaryllysine
- 908 modified: N6-glutaryllysine; alternate
- 911 G → E: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs1388955593; G → V: in CPS1D; significant decrease in protein yield and enzyme activity
- 913 S → L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- 914 D → G: in CPS1D; significant decrease in protein yield and enzyme activity; D → H: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs765484849
- 915 modified: N6-glutaryllysine; alternate
- 918 S → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 919 modified: N6-glutaryllysine; alternate
- 932 R → T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- 937 I → N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- 949 A → T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- 958 L → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 959 Y → C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- 962 Y → C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- 964 G → D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- 986 I → T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- 987 G → C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- 1074 modified: N6-glutaryllysine; alternate
- 1150 modified: N6-glutaryllysine
- 1168 modified: N6-glutaryllysine; alternate
- 1183 modified: N6-glutaryllysine; alternate
- 1215 I → V: in CPS1D; uncertain significance; dbSNP:rs141373204
- 1224 modified: N6-glutaryllysine
- 1254 I → F: in CPS1D; uncertain significance
- 1266 F → S: in dbSNP:rs1047886
- 1283 M → L: in dbSNP:rs1047887
- 1356 modified: N6-glutaryllysine; alternate
- 1360 modified: N6-glutaryllysine; alternate
- 1363:1366 natural variant: Missing (in CPS1D; uncertain significance)
- 1376 G → S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- 1378 A → T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- 1381 L → S: in CPS1D; significant loss of protein stability
- 1406 T → N: probable risk factor for PHN; dbSNP:rs1047891
- 1411 P → L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- 1443 T → A: in CPS1D; almost complete loss of enzyme activity; approximately 10-fold decrease in the apparent Vmax for bicarbonate, ammonia and ATP; decreased affinity for NAG
- 1453 R → Q: in CPS1D; the enzyme is inactive; R → W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- 1479 modified: N6-glutaryllysine; alternate
- 1486 modified: N6-glutaryllysine; alternate
- 1491 Y → H: in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG); dbSNP:rs1553519513
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
42% identity, 98% coverage: 4:488/495 of query aligns to 377:852/1430 of 5douD
- active site: R505 (= R129), R545 (= R169), N576 (≠ G202), E589 (= E215), H617 (= H243), N656 (= N283), Q658 (= Q285), E672 (= E299), N674 (= N301), R676 (= R303), S680 (= S307)
- binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ V167), R545 (= R169), L550 (= L174), G551 (= G175), G552 (= G176), E581 (= E207), S583 (≠ C209), V584 (≠ L210), T585 (≠ I211), E589 (= E215), M614 (= M240), G615 (= G241), V616 (= V242), H617 (= H243), Q658 (= Q285), I671 (= I298), E672 (= E299)
- binding magnesium ion: Q658 (= Q285), E672 (= E299), E672 (= E299), N674 (= N301)
- binding phosphate ion: L550 (= L174), G551 (= G175), H617 (= H243), E672 (= E299), N674 (= N301), R676 (= R303), R679 (= R306)
Sites not aligning to the query:
- active site: 252, 335, 337, 880, 1006, 1087, 1116, 1124, 1184, 1196, 1198, 1203, 1260
- binding adenosine-5'-diphosphate: 1085, 1110, 1111, 1116, 1140, 1142, 1143, 1144, 1184, 1186, 1195, 1196
- binding n-acetyl-l-glutamate: 1307, 1308, 1332, 1334, 1335, 1351, 1379, 1384, 1385, 1386, 1390
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)
43% identity, 96% coverage: 6:479/495 of query aligns to 473:925/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
41% identity, 99% coverage: 1:488/495 of query aligns to 368:841/1422 of 6w2jA
- active site: Q651 (= Q285), E665 (= E299), N667 (= N301), S673 (= S307)
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: D605 (= D238), M607 (= M240), V615 (≠ I248), P725 (= P359), R726 (= R360), W727 (= W361), D730 (≠ E364), F732 (= F366), F756 (≠ L394), L760 (= L398), C763 (≠ L401), H764 (≠ E402), S795 (≠ A442), R797 (= R444), I798 (≠ M445)
Sites not aligning to the query:
Query Sequence
>WP_012505082.1 NCBI__GCF_000020625.1:WP_012505082.1
MPKREDIKSILVIGAGPIVIGQACEFDYSGTQACRALKEDGYRVILVNSNPATIMTDVEF
AHSTYIEPITPEYVQKIIEKEKPDALLPTMGGQTALNTAVALAERGILERNGVELIGAKL
RAIRKAENRELFSDAMKKLGLEMAKGFFVRNEKEAKEALESIGLPIVIRPSFTLGGTGGG
FAETKADYYDAVRRGIAESPIGEVLVEECLIGWKEFELEVIRDLADNVIIVCSIENVDPM
GVHTGDSITVAPAQTLSDRQYQALRDASVKIIREIGVETGGSNIQFAINPDNGRIVVIEM
NPRVSRSSALASKATGFPIAKVAAKLAVGYTLDEIQNDITKSTPASFEPVIDYCVVKVPR
WDFEKFKNVDARLGVQMKSVGEVMAFGRNFREALQKSLRGLEIGRAGLGCDGKDIMNVLG
MTPQQKKFAKDDVLEKIRIPKADRMFYLRYAFQAGATVEEVHESTKIDPWFLDNIRQIVD
CEAELRLLAETQASS
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