SitesBLAST
Comparing WP_089301120.1 NCBI__GCF_900188115.1:WP_089301120.1 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)
52% identity, 97% coverage: 3:1105/1134 of query aligns to 94:1174/1187 of Q42601
- P149 (= P58) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
- G587 (= G492) mutation to E: In ven3-3; reticulate leaf phenotype.
- A844 (= A747) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P930) mutation to L: In ven3-1; reticulate leaf phenotype.
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
52% identity, 96% coverage: 1:1093/1134 of query aligns to 1:1056/1073 of 1bxrA
- active site: R129 (= R129), R169 (= R169), M174 (= M174), G176 (= G176), K202 (≠ S202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G507), K634 (≠ Q636), R715 (= R721), G721 (= G727), G722 (= G728), S745 (= S751), E761 (= E767), D769 (= D775), Q829 (= Q835), E841 (= E847), N843 (= N849), R848 (= R854), P901 (≠ R917)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G175 (= G175), G176 (= G176), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), E299 (= E299), R306 (= R306), T376 (= T375), R675 (= R681), V713 (≠ L719), R715 (= R721), L720 (= L726), G721 (= G727), G722 (= G728), M725 (= M731), D753 (= D759), F755 (= F761), L756 (= L762), E761 (= E767), A785 (= A791), G786 (= G792), V787 (= V793), H788 (= H794), Q829 (= Q835), E841 (= E847), N843 (= N849), R848 (= R854)
- binding manganese (ii) ion: E299 (= E299), N301 (= N301), Q829 (= Q835), E841 (= E847), E841 (= E847), N843 (= N849)
- binding L-ornithine: E783 (= E789), D791 (= D797), E892 (= E908), L907 (= L928), D1041 (≠ I1078), T1042 (= T1079)
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)
52% identity, 96% coverage: 1:1093/1134 of query aligns to 1:1056/1073 of P00968
- M1 (= M1) modified: Initiator methionine, Removed
- R129 (= R129) binding
- R169 (= R169) binding
- G175 (= G175) binding
- G176 (= G176) binding
- E208 (= E208) binding
- L210 (≠ V210) 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
- R715 (= R721) binding
- H754 (≠ R760) binding
- L756 (= L762) binding
- E761 (= E767) binding
- G786 (= G792) binding
- V787 (= V793) binding
- H788 (= H794) binding
- S789 (= S795) binding
- Q829 (= Q835) binding ; binding
- E841 (= E847) binding ; binding ; binding
- N843 (= N849) binding
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
52% identity, 96% coverage: 1:1093/1134 of query aligns to 1:1041/1058 of 1t36A
- active site: R129 (= R129), R169 (= R169), M174 (= M174), G176 (= G176), K202 (≠ S202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G507), K634 (≠ Q636), R715 (= R721), E746 (= E767), D754 (= D775), Q814 (= Q835), E826 (= E847), N828 (= N849), R833 (= R854), P886 (≠ R917)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G175 (= G175), G176 (= G176), E208 (= E208), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R721), M718 (= M731), F740 (= F761), L741 (= L762), E746 (= E767), A770 (= A791), G771 (= G792), V772 (= V793), H773 (= H794), E826 (= E847), P894 (= P930)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q835), E826 (= E847)
- binding L-ornithine: E768 (= E789), D776 (= D797), E877 (= E908), L892 (= L928), D1026 (≠ I1078), T1027 (= T1079)
- binding phosphate ion: M174 (= M174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
- binding uridine-5'-monophosphate: K939 (= K975), T959 (= T995), G961 (= G997), T962 (= T998), K978 (= K1014), N1000 (= N1051), T1001 (= T1052), T1002 (≠ P1053), S1011 (≠ G1063), I1014 (= I1066)
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
52% identity, 96% coverage: 1:1093/1134 of query aligns to 1:1041/1058 of 1c3oA
- active site: R129 (= R129), R169 (= R169), M174 (= M174), G176 (= G176), K202 (≠ S202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G507), K634 (≠ Q636), R715 (= R721), E746 (= E767), D754 (= D775), Q814 (= Q835), E826 (= E847), N828 (= N849), R833 (= R854), P886 (≠ R917)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G176 (= G176), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R721), M718 (= M731), F740 (= F761), L741 (= L762), E746 (= E767), A770 (= A791), G771 (= G792), V772 (= V793), H773 (= H794), S774 (= S795), E826 (= E847)
- binding glutamine: R528 (≠ T526), A537 (= A535), T538 (≠ A536), N554 (≠ I556)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q835), E826 (= E847)
- binding L-ornithine: E768 (= E789), D776 (= D797), E877 (= E908), L892 (= L928), D1026 (≠ I1078), T1027 (= T1079)
- binding phosphate ion: M174 (= M174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
51% identity, 96% coverage: 1:1093/1134 of query aligns to 1:1041/1058 of 1ce8A
- active site: R129 (= R129), R169 (= R169), M174 (= M174), G176 (= G176), K202 (≠ S202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G507), K634 (≠ Q636), R715 (= R721), E746 (= E767), D754 (= D775), Q814 (= Q835), E826 (= E847), N828 (= N849), R833 (= R854), P886 (≠ R917)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G176 (= G176), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R721), F740 (= F761), L741 (= L762), E746 (= E767), A770 (= A791), G771 (= G792), V772 (= V793), H773 (= H794), S774 (= S795), E826 (= E847)
- binding inosinic acid: S933 (= S969), K939 (= K975), T959 (= T995), G961 (= G997), T962 (= T998), K978 (= K1014), V979 (≠ Y1015), I986 (= I1037), N1000 (= N1051), T1001 (= T1052), T1002 (≠ P1053), D1010 (= D1062), S1011 (≠ G1063), V1013 (≠ E1065)
- binding manganese (ii) ion: M174 (= M174), Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q835), E826 (= E847)
- binding L-ornithine: R528 (≠ T526), A537 (= A535), T538 (≠ A536), E552 (= E554), N554 (≠ I556), E768 (= E789), D776 (= D797), E877 (= E908), L892 (= L928), Y1025 (≠ C1077), D1026 (≠ I1078), T1027 (= T1079)
- binding phosphate ion: M174 (= M174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
51% identity, 96% coverage: 1:1093/1134 of query aligns to 1:1041/1058 of 1a9xA
- active site: K202 (≠ S202), D338 (= D338), G507 (= G507), K634 (≠ Q636), D754 (= D775), P886 (≠ R917)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G175 (= G175), G176 (= G176), L210 (≠ V210), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R721), M718 (= M731), F740 (= F761), L741 (= L762), E746 (= E767), A770 (= A791), G771 (= G792), V772 (= V793), H773 (= H794), E826 (= E847)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q835), E826 (= E847)
- binding L-ornithine: E768 (= E789), D776 (= D797), E877 (= E908), L892 (= L928), Y1025 (≠ C1077), D1026 (≠ I1078), T1027 (= T1079)
- binding phosphate ion: G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
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)
39% identity, 97% coverage: 4:1105/1134 of query aligns to 435:1499/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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)
39% identity, 97% coverage: 10:1107/1134 of query aligns to 393:1476/2198 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.
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)
39% identity, 96% coverage: 6:1091/1134 of query aligns to 473:1517/2244 of Q09794
- S1119 (= S671) modified: Phosphoserine
Sites not aligning to the query:
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
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)
39% identity, 95% coverage: 1:1082/1134 of query aligns to 402:1446/2224 of P05990
- E1167 (= E786) mutation to K: Severely diminishes UTP inhibition of CPSase; in Su(b).
Sites not aligning to the query:
- 1883 modified: Phosphoserine
- 1885 modified: Phosphoserine
- 1892 modified: Phosphoserine
- 1894 modified: Phosphoserine
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
38% identity, 95% coverage: 4:1082/1134 of query aligns to 419:1468/1500 of Q8C196
- K1291 (≠ L883) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
Sites not aligning to the query:
- 44 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- 287 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 95% coverage: 4:1082/1134 of query aligns to 419:1468/1500 of P07756
- S537 (≠ D119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S934) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T935) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T995) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T998) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ Y1015) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N1051) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ Y1054) mutation to D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG.
P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
37% identity, 97% coverage: 4:1098/1134 of query aligns to 419:1484/1500 of P31327
- A438 (= A23) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- K453 (≠ R38) modified: N6-glutaryllysine; alternate
- K458 (≠ R43) modified: N6-glutaryllysine; alternate
- K527 (≠ D109) 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 (≠ G126) 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 (≠ I135) 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 (≠ E342) 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 (≠ E424) modified: N6-glutaryllysine; alternate
- L843 (= L426) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (= R433) 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 (≠ R439) modified: N6-glutaryllysine; alternate
- K869 (≠ E452) modified: N6-glutaryllysine
- T871 (≠ S454) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (≠ P458) 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 (≠ E472) modified: N6-glutaryllysine; alternate
- K892 (≠ T475) modified: N6-glutaryllysine; alternate
- K905 (≠ L486) modified: N6-glutaryllysine
- K908 (= K489) modified: N6-glutaryllysine; alternate
- G911 (= G492) to E: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs1388955593; to V: in CPS1D; significant decrease in protein yield and enzyme activity
- S913 (= S494) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- D914 (= D495) to G: in CPS1D; significant decrease in protein yield and enzyme activity; to H: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs765484849
- K915 (≠ R496) modified: N6-glutaryllysine; alternate
- S918 (≠ A499) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ A500) modified: N6-glutaryllysine; alternate
- R932 (= R515) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (≠ V520) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (= A532) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (≠ H541) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- Y959 (= Y542) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- Y962 (= Y545) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- G964 (≠ A550) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I574) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G575) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ P666) modified: N6-glutaryllysine; alternate
- K1150 (≠ S742) modified: N6-glutaryllysine
- K1168 (≠ R760) modified: N6-glutaryllysine; alternate
- K1183 (≠ D775) modified: N6-glutaryllysine; alternate
- I1215 (≠ L807) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (≠ R816) modified: N6-glutaryllysine
- I1254 (≠ L846) to F: in CPS1D; uncertain significance
- F1266 (= F858) to S: in dbSNP:rs1047886
- M1283 (= M875) to L: in dbSNP:rs1047887
- K1356 (≠ P959) modified: N6-glutaryllysine; alternate
- K1360 (≠ S963) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ FVSV 967:970) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ F980) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (≠ V982) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (= L985) to S: in CPS1D; significant loss of protein stability
- T1406 (= T1010) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ S1016) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (≠ S1057) to 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
- R1453 (= R1067) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- K1479 (≠ A1093) 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
- 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
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)
40% identity, 95% coverage: 10:1082/1134 of query aligns to 396:1431/2225 of P08955
- S1406 (vs. gap) modified: Phosphoserine; by PKA; mutation to A: No effect on enzyme kinetics.; mutation to 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)
39% identity, 95% coverage: 10:1082/1134 of query aligns to 396:1431/2225 of P27708
- T456 (= T70) modified: Phosphothreonine; by MAPK1
- Y735 (= Y353) to C: in a colorectal cancer sample; somatic mutation
- S1406 (vs. gap) modified: Phosphoserine; by PKA
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
- 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
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)
41% identity, 88% coverage: 7:1000/1134 of query aligns to 28:1002/1118 of P03965
- L229 (≠ V210) 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.
- H807 (= H794) mutation to N: No effect.
- D810 (= D797) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
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)
37% identity, 97% coverage: 7:1104/1134 of query aligns to 404:1461/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
37% identity, 95% coverage: 4:1082/1134 of query aligns to 377:1409/1430 of 5douD
- active site: R505 (= R129), R545 (= R169), N576 (≠ S202), E589 (= E215), H617 (= H243), N656 (= N283), Q658 (= Q285), E672 (= E299), N674 (= N301), R676 (= R303), S680 (= S307), G880 (≠ P503), A1006 (≠ Q636), R1087 (= R721), E1116 (= E767), K1124 (≠ D775), Q1184 (= Q835), E1196 (= E847), N1198 (= N849), R1203 (= R854), R1260 (= R917)
- binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ V167), R545 (= R169), L550 (≠ M174), G551 (= G175), G552 (= G176), E581 (= E207), S583 (= S209), V584 (= V210), T585 (≠ L211), E589 (= E215), M614 (= M240), G615 (= G241), V616 (= V242), H617 (= H243), Q658 (= Q285), I671 (= I298), E672 (= E299), L1085 (= L719), F1110 (= F761), V1111 (≠ L762), E1116 (= E767), A1140 (= A791), V1142 (= V793), H1143 (= H794), S1144 (= S795), Q1184 (= Q835), L1186 (≠ A837), I1195 (≠ L846), E1196 (= E847)
- binding magnesium ion: Q658 (= Q285), E672 (= E299), E672 (= E299), N674 (= N301)
- binding n-acetyl-l-glutamate: I1307 (≠ V970), Q1308 (≠ A971), T1332 (= T995), A1334 (≠ G997), T1335 (= T998), W1351 (≠ Y1015), L1379 (≠ T1052), T1384 (≠ S1057), K1385 (≠ G1058), F1386 (≠ P1059), N1390 (≠ G1063)
- binding phosphate ion: L550 (≠ M174), G551 (= G175), H617 (= H243), E672 (= E299), N674 (= N301), R676 (= R303), R679 (= R306)
Sites not aligning to the query:
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
37% identity, 95% coverage: 4:1082/1134 of query aligns to 374:1398/1422 of 6w2jA
- active site: Q651 (= Q285), E665 (= E299), N667 (= N301), S673 (= S307), G869 (≠ P503), A995 (≠ Q636), K1113 (≠ D775), R1249 (= R917)
- 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 (= V248), P725 (= P359), R726 (= R360), W727 (≠ F361), D730 (≠ E364), F732 (= F366), F756 (≠ L394), L760 (= L398), C763 (≠ T401), H764 (≠ E402), S795 (≠ D431), R797 (= R433), I798 (≠ L434)
Sites not aligning to the query:
Query Sequence
>WP_089301120.1 NCBI__GCF_900188115.1:WP_089301120.1
MPRRTDLSHVLVIGSGPIVIGQAAEFDYSGTQACRVLREEGLRVSLVNSNPATIMTDPEF
ADSTYIEPVTPEFLEQVIAAERPDALLATLGGQTALNAAVELDRSGVLDKYGVELIGADI
EAIQRGEDRQKFKDIVRQAGGDVPRSAVCWTMDEVRDCVAELGLPVVIRPAFTMGGRGSG
MAHTQEDLERMAAYGLSESPVSEVLVEESVLGWKEYELELMRDHRDNVVVVCSIENVDAM
GVHTGDSVTVAPSMTLTDREYQNMRDVGIDVLREVGVDTGGCNIQFAIHPETGRMVVIEM
NPRVSRSSALASKATGFPIAKIAARLAIGYSLDEIPNDITGETPASFEPTLDYVVVKVPR
FAFEKFPGADPTLTTTMKSVGEAMSVGRSFTEALGKALRSTETRALGFWTQPDPEGVTLA
DTLEALRTPHDGRLYTVERALRWGATIEQVCEASWIDPWFVDQIQSLVELREEITEAPVL
DEALLLGAKRFGVSDRQIAALRPELAGEDGVRALRHRLGVRPVFKTVDTCAAEFAARTPY
HYSAYESDPAAESEVIAQHDKPKALILGSGPNRIGQGIEFDYSCVHATLALREAGYETVM
INCNPETVSTDYDTSDRLYFEPLTFEDVLEVVHAEQESGNLAAVIVQLGGQTPLSLSKRL
ADAGVPVVGTSPDAIHLAEERGAFGEVLGAAGLPAPKYGTATSFEGAQRIADEVGYPVLV
RPSYVLGGRGMEIVYDAAHLASYISRATEVSPEYPVLVDRFLDDAIEIDVDALYDGEELY
LGGVMEHIEEAGVHSGDSSCALPPITLGRADLERVRASTEAIAKGVGVRGLLNVQYALAG
DVLYVLEANPRASRTAPFVSKATGVPLAKAAALIMTGSSVADLRASGVLRAWGDGGTLPA
DAPIAVKEAVLPFHRFRTPEGLGVDSLLGPEMKSTGEVMGVDAAFGMAFAKSQVAAYGPL
PTSGTVFVSVANRDKRALIFPVKRLADLGFEVLATSGTAEVLRRNGVPCTVVRKYSTPEG
EHVAGAADGSGEDAPNIVEIILDGGVDMIINTPYGNSGPRIDGYEIRTAAVSRDVPCITT
VQGAGAAVHGIEASIRGDIGVQSLQRLQAAMAASAESAAAAAGVTAPAARGRQE
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