SitesBLAST
Comparing Synpcc7942_0711 FitnessBrowser__SynE:Synpcc7942_0711 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)
65% identity, 99% coverage: 3:1093/1097 of query aligns to 94:1176/1187 of Q42601
- P149 (= P58) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
- G587 (= G495) mutation to E: In ven3-3; reticulate leaf phenotype.
- A844 (= A763) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P932) mutation to L: In ven3-1; reticulate leaf phenotype.
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
59% identity, 100% coverage: 1:1096/1097 of query aligns to 1:1071/1073 of 1bxrA
- active site: R129 (= R129), R169 (= R170), M174 (= M175), G176 (= G177), K202 (≠ S203), E215 (= E216), H243 (= H244), N283 (= N284), Q285 (= Q286), E299 (= E300), N301 (= N302), R303 (= R304), S307 (= S308), D338 (= D339), G507 (= G506), K634 (≠ R647), R715 (= R737), G721 (= G743), G722 (= G744), S745 (≠ E767), E761 (= E783), D769 (= D791), Q829 (= Q852), E841 (= E864), N843 (= N866), R848 (= R871), P901 (= P924)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R129), I167 (= I168), R169 (= R170), M174 (= M175), G175 (= G176), G176 (= G177), L210 (= L211), I211 (= I212), E215 (= E216), M240 (= M241), G241 (= G242), H243 (= H244), T244 (= T245), Q285 (= Q286), E299 (= E300), R306 (= R307), T376 (= T376), R675 (= R697), V713 (= V735), R715 (= R737), L720 (= L742), G721 (= G743), G722 (= G744), M725 (= M747), D753 (= D775), F755 (= F777), L756 (= L778), E761 (= E783), A785 (= A808), G786 (= G809), V787 (≠ I810), H788 (= H811), Q829 (= Q852), E841 (= E864), N843 (= N866), R848 (= R871)
- binding manganese (ii) ion: E299 (= E300), N301 (= N302), Q829 (= Q852), E841 (= E864), E841 (= E864), N843 (= N866)
- binding L-ornithine: E783 (= E806), D791 (= D814), E892 (= E915), L907 (= L930), D1041 (≠ V1064), T1042 (= T1065)
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)
59% identity, 100% coverage: 1:1096/1097 of query aligns to 1:1071/1073 of P00968
- M1 (= M1) modified: Initiator methionine, Removed
- R129 (= R129) binding
- R169 (= R170) binding
- G175 (= G176) binding
- G176 (= G177) binding
- E208 (≠ Q209) binding
- L210 (= L211) binding
- E215 (= E216) binding
- G241 (= G242) binding
- I242 (≠ V243) binding
- H243 (= H244) binding
- Q285 (= Q286) binding ; binding
- E299 (= E300) binding ; binding ; binding
- N301 (= N302) binding
- R715 (= R737) binding
- H754 (≠ K776) binding
- L756 (= L778) binding
- E761 (= E783) binding
- G786 (= G809) binding
- V787 (≠ I810) binding
- H788 (= H811) binding
- S789 (= S812) binding
- Q829 (= Q852) binding ; binding
- E841 (= E864) binding ; binding ; binding
- N843 (= N866) binding
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
58% identity, 100% coverage: 1:1096/1097 of query aligns to 1:1056/1058 of 1t36A
- active site: R129 (= R129), R169 (= R170), M174 (= M175), G176 (= G177), K202 (≠ S203), E215 (= E216), H243 (= H244), N283 (= N284), Q285 (= Q286), E299 (= E300), N301 (= N302), R303 (= R304), S307 (= S308), D338 (= D339), G507 (= G506), K634 (≠ R647), R715 (= R737), E746 (= E783), D754 (= D791), Q814 (= Q852), E826 (= E864), N828 (= N866), R833 (= R871), P886 (= P924)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I168), R169 (= R170), M174 (= M175), G175 (= G176), G176 (= G177), E208 (≠ Q209), L210 (= L211), I211 (= I212), E215 (= E216), M240 (= M241), G241 (= G242), I242 (≠ V243), H243 (= H244), Q285 (= Q286), I298 (= I299), E299 (= E300), T376 (= T376), R715 (= R737), M718 (= M747), F740 (= F777), L741 (= L778), E746 (= E783), A770 (= A808), G771 (= G809), V772 (≠ I810), H773 (= H811), E826 (= E864), P894 (= P932)
- binding manganese (ii) ion: Q285 (= Q286), E299 (= E300), E299 (= E300), N301 (= N302), Q814 (= Q852), E826 (= E864)
- binding L-ornithine: E768 (= E806), D776 (= D814), E877 (= E915), L892 (= L930), D1026 (≠ V1064), T1027 (= T1065)
- binding phosphate ion: M174 (= M175), G175 (= G176), H243 (= H244), E299 (= E300), N301 (= N302), R303 (= R304), R306 (= R307)
- binding uridine-5'-monophosphate: K939 (= K977), T959 (= T997), G961 (= G999), T962 (= T1000), K978 (= K1016), N1000 (= N1038), T1001 (= T1039), T1002 (≠ P1040), S1011 (≠ D1049), I1014 (= I1052)
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
58% identity, 100% coverage: 1:1096/1097 of query aligns to 1:1056/1058 of 1c3oA
- active site: R129 (= R129), R169 (= R170), M174 (= M175), G176 (= G177), K202 (≠ S203), E215 (= E216), H243 (= H244), N283 (= N284), Q285 (= Q286), E299 (= E300), N301 (= N302), R303 (= R304), S307 (= S308), D338 (= D339), G507 (= G506), K634 (≠ R647), R715 (= R737), E746 (= E783), D754 (= D791), Q814 (= Q852), E826 (= E864), N828 (= N866), R833 (= R871), P886 (= P924)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I168), R169 (= R170), M174 (= M175), G176 (= G177), L210 (= L211), I211 (= I212), E215 (= E216), M240 (= M241), G241 (= G242), H243 (= H244), T244 (= T245), Q285 (= Q286), I298 (= I299), E299 (= E300), T376 (= T376), R715 (= R737), M718 (= M747), F740 (= F777), L741 (= L778), E746 (= E783), A770 (= A808), G771 (= G809), V772 (≠ I810), H773 (= H811), S774 (= S812), E826 (= E864)
- binding glutamine: R528 (≠ L527), A537 (≠ E536), T538 (≠ A537), N554 (≠ R568)
- binding manganese (ii) ion: Q285 (= Q286), E299 (= E300), E299 (= E300), N301 (= N302), Q814 (= Q852), E826 (= E864)
- binding L-ornithine: E768 (= E806), D776 (= D814), E877 (= E915), L892 (= L930), D1026 (≠ V1064), T1027 (= T1065)
- binding phosphate ion: M174 (= M175), G175 (= G176), H243 (= H244), E299 (= E300), N301 (= N302), R303 (= R304), R306 (= R307)
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
58% identity, 100% coverage: 1:1096/1097 of query aligns to 1:1056/1058 of 1ce8A
- active site: R129 (= R129), R169 (= R170), M174 (= M175), G176 (= G177), K202 (≠ S203), E215 (= E216), H243 (= H244), N283 (= N284), Q285 (= Q286), E299 (= E300), N301 (= N302), R303 (= R304), S307 (= S308), D338 (= D339), G507 (= G506), K634 (≠ R647), R715 (= R737), E746 (= E783), D754 (= D791), Q814 (= Q852), E826 (= E864), N828 (= N866), R833 (= R871), P886 (= P924)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I168), R169 (= R170), M174 (= M175), G176 (= G177), L210 (= L211), I211 (= I212), E215 (= E216), M240 (= M241), G241 (= G242), I242 (≠ V243), H243 (= H244), Q285 (= Q286), I298 (= I299), E299 (= E300), T376 (= T376), R715 (= R737), F740 (= F777), L741 (= L778), E746 (= E783), A770 (= A808), G771 (= G809), V772 (≠ I810), H773 (= H811), S774 (= S812), E826 (= E864)
- binding inosinic acid: S933 (= S971), K939 (= K977), T959 (= T997), G961 (= G999), T962 (= T1000), K978 (= K1016), V979 (= V1017), I986 (≠ V1024), N1000 (= N1038), T1001 (= T1039), T1002 (≠ P1040), D1010 (= D1048), S1011 (≠ D1049), V1013 (≠ I1051)
- binding manganese (ii) ion: M174 (= M175), Q285 (= Q286), E299 (= E300), E299 (= E300), N301 (= N302), Q814 (= Q852), E826 (= E864)
- binding L-ornithine: R528 (≠ L527), A537 (≠ E536), T538 (≠ A537), E552 (= E566), N554 (≠ R568), E768 (= E806), D776 (= D814), E877 (= E915), L892 (= L930), Y1025 (≠ T1063), D1026 (≠ V1064), T1027 (= T1065)
- binding phosphate ion: M174 (= M175), G175 (= G176), H243 (= H244), E299 (= E300), N301 (= N302), R303 (= R304), R306 (= R307)
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
57% identity, 100% coverage: 1:1096/1097 of query aligns to 1:1056/1058 of 1a9xA
- active site: K202 (≠ S203), D338 (= D339), G507 (= G506), K634 (≠ R647), D754 (= D791), P886 (= P924)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I168), R169 (= R170), M174 (= M175), G175 (= G176), G176 (= G177), L210 (= L211), E215 (= E216), M240 (= M241), G241 (= G242), I242 (≠ V243), H243 (= H244), T244 (= T245), Q285 (= Q286), I298 (= I299), E299 (= E300), T376 (= T376), R715 (= R737), M718 (= M747), F740 (= F777), L741 (= L778), E746 (= E783), A770 (= A808), G771 (= G809), V772 (≠ I810), H773 (= H811), E826 (= E864)
- binding manganese (ii) ion: Q285 (= Q286), E299 (= E300), E299 (= E300), N301 (= N302), Q814 (= Q852), E826 (= E864)
- binding L-ornithine: E768 (= E806), D776 (= D814), E877 (= E915), L892 (= L930), Y1025 (≠ T1063), D1026 (≠ V1064), T1027 (= T1065)
- binding phosphate ion: G175 (= G176), H243 (= H244), E299 (= E300), N301 (= N302), R303 (= R304), R306 (= R307)
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)
42% identity, 99% coverage: 6:1091/1097 of query aligns to 473:1531/2244 of Q09794
- S1119 (= S687) modified: Phosphoserine
Sites not aligning to the query:
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
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)
42% identity, 98% coverage: 4:1077/1097 of query aligns to 435:1485/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
41% identity, 100% coverage: 4:1095/1097 of query aligns to 419:1493/1500 of P07756
- S537 (≠ K119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S936) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T937) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T997) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T1000) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ L1015) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N1038) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ A1041) 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.
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
41% identity, 100% coverage: 4:1095/1097 of query aligns to 419:1493/1500 of Q8C196
- K1291 (≠ L900) 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
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)
42% identity, 98% coverage: 8:1077/1097 of query aligns to 394:1440/2225 of P27708
- T456 (= T70) modified: Phosphothreonine; by MAPK1
- Y735 (= Y354) to C: in a colorectal cancer sample; somatic mutation
- S1406 (≠ D1049) 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
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)
42% identity, 98% coverage: 8:1077/1097 of query aligns to 394:1440/2225 of P08955
- S1406 (≠ D1049) 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.
P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
41% identity, 100% coverage: 4:1095/1097 of query aligns to 419:1493/1500 of P31327
- A438 (= A23) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- K453 (≠ R38) modified: N6-glutaryllysine; alternate
- K458 (≠ E43) 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 (≠ 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 (= Q263) to P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- K728 (= K314) modified: N6-glutaryllysine
- K757 (≠ Q343) modified: N6-glutaryllysine; alternate
- K772 (= K358) modified: N6-glutaryllysine; alternate
- P774 (= P360) to L: in CPS1D; the enzyme is inactive
- K793 (= K379) modified: N6-glutaryllysine; alternate
- K811 (= K397) modified: N6-glutaryllysine; alternate
- K841 (≠ P425) modified: N6-glutaryllysine; alternate
- L843 (= L427) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (= R434) 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 (≠ Q440) modified: N6-glutaryllysine; alternate
- K869 (≠ Q453) modified: N6-glutaryllysine
- T871 (= T455) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (≠ P459) 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 (≠ D473) modified: N6-glutaryllysine; alternate
- K892 (= K476) modified: N6-glutaryllysine; alternate
- K905 (≠ L489) modified: N6-glutaryllysine
- K908 (= K492) modified: N6-glutaryllysine; alternate
- G911 (= G495) 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 (= S497) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- D914 (= D498) 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 (≠ R499) modified: N6-glutaryllysine; alternate
- S918 (≠ A502) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ F503) modified: N6-glutaryllysine; alternate
- R932 (= R516) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (= I521) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (= A533) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (≠ Y542) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- Y959 (= Y543) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- Y962 (= Y546) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- G964 (≠ S548) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I585) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G586) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ Q682) modified: N6-glutaryllysine; alternate
- K1150 (≠ R758) modified: N6-glutaryllysine
- K1168 (= K776) modified: N6-glutaryllysine; alternate
- K1183 (≠ R792) modified: N6-glutaryllysine; alternate
- I1215 (≠ L824) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (≠ R833) modified: N6-glutaryllysine
- I1254 (≠ L863) to F: in CPS1D; uncertain significance
- F1266 (= F875) to S: in dbSNP:rs1047886
- M1283 (= M892) to L: in dbSNP:rs1047887
- K1356 (≠ R961) modified: N6-glutaryllysine; alternate
- K1360 (≠ Q965) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ FISV 969:972) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ P982) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (= A984) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (≠ F987) to S: in CPS1D; significant loss of protein stability
- T1406 (≠ E1012) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ K1016) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (≠ R1044) 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 (= R1053) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- K1479 (≠ A1079) modified: N6-glutaryllysine; alternate
- K1486 (= K1088) modified: N6-glutaryllysine; alternate
- Y1491 (= Y1093) to H: in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG); dbSNP:rs1553519513
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
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)
41% identity, 99% coverage: 8:1092/1097 of query aligns to 391:1466/2198 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)
41% identity, 98% coverage: 8:1078/1097 of query aligns to 404:1456/2224 of P05990
- E1167 (= E803) 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
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)
40% identity, 99% coverage: 5:1090/1097 of query aligns to 402:1461/2225 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)
40% identity, 100% coverage: 4:1095/1097 of query aligns to 377:1430/1430 of 5douD
- active site: R505 (= R129), R545 (= R170), N576 (≠ S203), E589 (= E216), H617 (= H244), N656 (= N284), Q658 (= Q286), E672 (= E300), N674 (= N302), R676 (= R304), S680 (= S308), G880 (= G506), A1006 (≠ R647), R1087 (= R737), E1116 (= E783), K1124 (≠ R792), Q1184 (= Q852), E1196 (= E864), N1198 (= N866), R1203 (= R871), R1260 (≠ P924)
- binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ I168), R545 (= R170), L550 (≠ M175), G551 (= G176), G552 (= G177), E581 (= E208), S583 (= S210), V584 (≠ L211), T585 (≠ I212), E589 (= E216), M614 (= M241), G615 (= G242), V616 (= V243), H617 (= H244), Q658 (= Q286), I671 (= I299), E672 (= E300), L1085 (≠ V735), F1110 (= F777), V1111 (≠ L778), E1116 (= E783), A1140 (= A808), V1142 (≠ I810), H1143 (= H811), S1144 (= S812), Q1184 (= Q852), L1186 (≠ A854), I1195 (≠ L863), E1196 (= E864)
- binding magnesium ion: Q658 (= Q286), E672 (= E300), E672 (= E300), N674 (= N302)
- binding n-acetyl-l-glutamate: I1307 (≠ V972), Q1308 (≠ S973), T1332 (= T997), A1334 (≠ G999), T1335 (= T1000), W1351 (≠ L1015), L1379 (≠ T1039), T1384 (≠ R1044), K1385 (≠ A1045), F1386 (≠ K1046), N1390 (≠ D1049)
- binding phosphate ion: L550 (≠ M175), G551 (= G176), H617 (= H244), E672 (= E300), N674 (= N302), R676 (= R304), R679 (= R307)
Sites not aligning to the query:
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
39% identity, 100% coverage: 4:1095/1097 of query aligns to 374:1419/1422 of 6w2jA
- active site: Q651 (= Q286), E665 (= E300), N667 (= N302), S673 (= S308), G869 (= G506), A995 (≠ R647), K1113 (≠ R792), R1249 (≠ P924)
- 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 (= D239), M607 (= M241), V615 (≠ I249), P725 (= P360), R726 (= R361), W727 (≠ F362), D730 (≠ E365), F732 (= F367), F756 (= F395), L760 (= L399), C763 (≠ L402), H764 (≠ E403), S795 (≠ P432), R797 (= R434), I798 (= I435)
Sites not aligning to the query:
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)
39% identity, 99% coverage: 7:1092/1097 of query aligns to 28:1099/1118 of P03965
- L229 (= L211) mutation to G: Abolishes ammonia-dependent ATPase activity.
- H262 (= H244) mutation to N: No effect.
- D265 (= D247) mutation D->A,E,N: Reduces ammonia-dependent ATPase activity 17-58 fold.
- I316 (= I299) mutation I->G,S,H: Reduces ammonia-dependent ATPase activity 17-64 fold.
- H807 (= H811) mutation to N: No effect.
- D810 (= D814) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
Query Sequence
>Synpcc7942_0711 FitnessBrowser__SynE:Synpcc7942_0711
MPRRQDIRKILLLGSGPIVIGQACEFDYSGTQACKALREEGYEVVLVNSNPATIMTDPET
ADRTYIEPLTPELVAQVIERERPDALLPTMGGQTALNLAVALAKNGTLDRFGVELIGAKL
EAIEKAEDRLLFKEAMERIGVKVCPSGIANNMAEAQAIAEQIGTYPLIIRPAFTMGGTGG
GIAYNQEEFELIVQSGLDASPVSQILVEQSLIGWKEFELEVMRDLADNVVIICSIENLDP
MGVHTGDSITVAPAQTLTDKEYQRLRDQAIAIIREIGVETGGSNIQFAINPQDGDVIVIE
MNPRVSRSSALASKATGFPIAKIAAKLAVGYSLDELKNDITRQTPASFEPTIDYVVTKIP
RFAFEKFPGTPAQLTTMMKSVGEAMAIGRTFPESFQKALRSLEIGRSGWGCDRPETLPTL
EQIKPQLRTPSPDRIFAVRQAMLLGLSDGDIYQLTGIDPWFLEKFREILEGEDFLKRASI
EQITPAQWLEVKQLGFSDRQIAFALGSSEEAVRQRRQQQGIKPVYKLVDTCAAEFEAYTP
YYYSCYESPRSHLAESGLTTIPAESEVRPSDRPKVMILGGGPNRIGQGIEFDYCCCHAAF
ALAADGYETIMVNSNPETVSTDYDTSDRLYFEPLTREDVLNILEAERPQGVIIQFGGQTP
LKLAVPLQTFLQTPEGQALGTQIWGTSPDSIDTAEDRERFEQILRQLDIAQPANGLARSP
EEALAIAHRIGYPTVVRPSYVLGGRAMEIVYSDAELERYMTEAVQVEPDHPILIDKFLEN
AIEVDVDALADRTGQVVIGGIMEHIEQAGIHSGDSACSLPTVSLNETVLETIRAWTTQLA
KALNVIGLMNIQFAVKDEQVYILEANPRASRTVPFVSKAIGRPLAKIAARLMSGQTLADL
GITSELVPSYLSVKEAVLPFDRFPGTDTLLGPEMRSTGEVMGIDVDFGRAFAKAELAASQ
RLPRQGTVFISVSDRDKAAIGPIAREFLQLGFRVVATGGTQKVLAEQRLSVEPILKVHEG
RPHVLDALKNDQIQLIINTPAGARAKVDDQIIRRAALDYKVPTVTTIAGAKATVEAIRAL
LEQPLQVKSLQDYQQQG
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