SitesBLAST
Comparing WP_015738405.1 NCBI__GCF_000024605.1:WP_015738405.1 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)
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)
50% identity, 99% coverage: 3:1070/1075 of query aligns to 94:1178/1187 of Q42601
- P149 (= P58) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
- G587 (= G491) mutation to E: In ven3-3; reticulate leaf phenotype.
- A844 (= A735) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P905) mutation to L: In ven3-1; reticulate leaf phenotype.
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
51% identity, 100% coverage: 1:1073/1075 of query aligns to 1:1073/1073 of 1bxrA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N282), Q285 (= Q284), E299 (= E298), N301 (= N300), R303 (= R302), S307 (= S306), D338 (≠ A337), G507 (= G502), K634 (= K628), R715 (= R709), G721 (= G715), G722 (= G716), S745 (= S739), E761 (= E754), D769 (= D762), Q829 (= Q822), E841 (= E835), N843 (= N837), R848 (= R842), P901 (≠ L897)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (≠ V210), I211 (≠ S211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q284), E299 (= E298), R306 (= R305), T376 (= T374), R675 (= R669), V713 (≠ L707), R715 (= R709), L720 (= L714), G721 (= G715), G722 (= G716), M725 (= M719), D753 (= D747), F755 (≠ Y749), L756 (≠ I750), E761 (= E754), A785 (= A778), G786 (= G779), V787 (≠ I780), H788 (= H781), Q829 (= Q822), E841 (= E835), N843 (= N837), R848 (= R842)
- binding manganese (ii) ion: E299 (= E298), N301 (= N300), Q829 (= Q822), E841 (= E835), E841 (= E835), N843 (= N837)
- binding L-ornithine: E783 (= E776), D791 (= D784), E892 (≠ V888), L907 (= L903), D1041 (≠ I1038), T1042 (= T1039)
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)
51% identity, 100% coverage: 1:1073/1075 of query aligns to 1:1073/1073 of P00968
- M1 (= M1) modified: Initiator methionine, Removed
- R129 (= R129) binding ATP
- R169 (= R169) binding ATP
- G175 (= G175) binding ATP
- G176 (= G176) binding ATP
- E208 (≠ Q208) binding ATP
- L210 (≠ V210) binding ATP
- E215 (= E215) binding ATP
- G241 (= G241) binding ATP
- I242 (= I242) binding ATP
- H243 (= H243) binding ATP
- Q285 (= Q284) binding ATP; binding Mn(2+)
- E299 (= E298) binding ATP; binding Mn(2+); binding Mn(2+)
- N301 (= N300) binding Mn(2+)
- R715 (= R709) binding ATP
- H754 (≠ K748) binding ATP
- L756 (≠ I750) binding ATP
- E761 (= E754) binding ATP
- G786 (= G779) binding ATP
- V787 (≠ I780) binding ATP
- H788 (= H781) binding ATP
- S789 (= S782) binding ATP
- Q829 (= Q822) binding ATP; binding Mn(2+)
- E841 (= E835) binding ATP; binding Mn(2+); binding Mn(2+)
- N843 (= N837) binding Mn(2+)
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
50% identity, 100% coverage: 1:1073/1075 of query aligns to 1:1058/1058 of 1t36A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N282), Q285 (= Q284), E299 (= E298), N301 (= N300), R303 (= R302), S307 (= S306), D338 (≠ A337), G507 (= G502), K634 (= K628), R715 (= R709), E746 (= E754), D754 (= D762), Q814 (= Q822), E826 (= E835), N828 (= N837), R833 (= R842), P886 (≠ L897)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), E208 (≠ Q208), L210 (≠ V210), I211 (≠ S211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (= I242), H243 (= H243), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R709), M718 (= M719), F740 (≠ Y749), L741 (≠ I750), E746 (= E754), A770 (= A778), G771 (= G779), V772 (≠ I780), H773 (= H781), E826 (= E835), P894 (= P905)
- binding manganese (ii) ion: Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q822), E826 (= E835)
- binding L-ornithine: E768 (= E776), D776 (= D784), E877 (≠ V888), L892 (= L903), D1026 (≠ I1038), T1027 (= T1039)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)
- binding uridine-5'-monophosphate: K939 (= K950), T959 (= T970), G961 (= G972), T962 (= T973), K978 (= K989), N1000 (= N1011), T1001 (= T1012), T1002 (= T1014), S1011 (≠ G1023), I1014 (= I1026)
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
50% identity, 100% coverage: 1:1073/1075 of query aligns to 1:1058/1058 of 1c3oA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N282), Q285 (= Q284), E299 (= E298), N301 (= N300), R303 (= R302), S307 (= S306), D338 (≠ A337), G507 (= G502), K634 (= K628), R715 (= R709), E746 (= E754), D754 (= D762), Q814 (= Q822), E826 (= E835), N828 (= N837), R833 (= R842), P886 (≠ L897)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ V210), I211 (≠ S211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R709), M718 (= M719), F740 (≠ Y749), L741 (≠ I750), E746 (= E754), A770 (= A778), G771 (= G779), V772 (≠ I780), H773 (= H781), S774 (= S782), E826 (= E835)
- binding glutamine: R528 (≠ M523), A537 (≠ E532), T538 (≠ A533), N554 (vs. gap)
- binding manganese (ii) ion: Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q822), E826 (= E835)
- binding L-ornithine: E768 (= E776), D776 (= D784), E877 (≠ V888), L892 (= L903), D1026 (≠ I1038), T1027 (= T1039)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
50% identity, 100% coverage: 1:1073/1075 of query aligns to 1:1058/1058 of 1ce8A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ G202), E215 (= E215), H243 (= H243), N283 (= N282), Q285 (= Q284), E299 (= E298), N301 (= N300), R303 (= R302), S307 (= S306), D338 (≠ A337), G507 (= G502), K634 (= K628), R715 (= R709), E746 (= E754), D754 (= D762), Q814 (= Q822), E826 (= E835), N828 (= N837), R833 (= R842), P886 (≠ L897)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ V210), I211 (≠ S211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (= I242), H243 (= H243), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R709), F740 (≠ Y749), L741 (≠ I750), E746 (= E754), A770 (= A778), G771 (= G779), V772 (≠ I780), H773 (= H781), S774 (= S782), E826 (= E835)
- binding inosinic acid: S933 (≠ T944), K939 (= K950), T959 (= T970), G961 (= G972), T962 (= T973), K978 (= K989), V979 (≠ L990), I986 (= I997), N1000 (= N1011), T1001 (= T1012), T1002 (= T1014), D1010 (≠ E1022), S1011 (≠ G1023), V1013 (≠ R1025)
- binding manganese (ii) ion: M174 (≠ L174), Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q822), E826 (= E835)
- binding L-ornithine: R528 (≠ M523), A537 (≠ E532), T538 (≠ A533), E552 (= E547), N554 (vs. gap), E768 (= E776), D776 (= D784), E877 (≠ V888), L892 (= L903), Y1025 (≠ C1037), D1026 (≠ I1038), T1027 (= T1039)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
49% identity, 100% coverage: 1:1073/1075 of query aligns to 1:1058/1058 of 1a9xA
- active site: K202 (≠ G202), D338 (≠ A337), G507 (= G502), K634 (= K628), D754 (= D762), P886 (≠ L897)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (≠ V210), E215 (= E215), M240 (= M240), G241 (= G241), I242 (= I242), H243 (= H243), T244 (= T244), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R709), M718 (= M719), F740 (≠ Y749), L741 (≠ I750), E746 (= E754), A770 (= A778), G771 (= G779), V772 (≠ I780), H773 (= H781), E826 (= E835)
- binding manganese (ii) ion: Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q822), E826 (= E835)
- binding L-ornithine: E768 (= E776), D776 (= D784), E877 (≠ V888), L892 (= L903), Y1025 (≠ C1037), D1026 (≠ I1038), T1027 (= T1039)
- binding phosphate ion: G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)
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, 97% coverage: 4:1051/1075 of query aligns to 435:1485/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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, 98% coverage: 1:1052/1075 of query aligns to 402:1456/2224 of P05990
- E1167 (= E773) 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
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)
44% identity, 99% coverage: 6:1066/1075 of query aligns to 473:1531/2244 of Q09794
- S1119 (≠ A659) modified: Phosphoserine
Sites not aligning to the query:
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
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)
45% identity, 97% coverage: 8:1051/1075 of query aligns to 394:1440/2225 of P27708
- T456 (= T70) modified: Phosphothreonine; by MAPK1
- Y735 (= Y352) 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 Zn(2+); binding Zn(2+); H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding Zn(2+); H→A: No zinc-binding and no catalytic activity.
- 1475 binding (S)-dihydroorotate
- 1505 binding (S)-dihydroorotate
- 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 Zn(2+); H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding Zn(2+); C→S: Reduces dihydroorotase activity.
- 1614 binding Zn(2+); H→A: Abolishes dihydroorotase activity.
- 1637 binding Zn(2+); E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding (S)-dihydroorotate
- 1686 binding Zn(2+); D→N: Abolishes dihydroorotase activity.
- 1690 binding (S)-dihydroorotate; H→N: 3% of wild-type catalytic activity.
- 1702 binding (S)-dihydroorotate
- 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)
45% identity, 97% coverage: 8:1051/1075 of query aligns to 394:1440/2225 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.
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
43% identity, 98% coverage: 4:1055/1075 of query aligns to 419:1481/1500 of P07756
- S537 (≠ P119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S909) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T910) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T970) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T973) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ K989) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N1011) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ T1014) 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)
43% identity, 98% coverage: 4:1056/1075 of query aligns to 419:1482/1500 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 (≠ T135) modified: N6-glutaryllysine; alternate
- Q678 (= Q262) to P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- K728 (= K312) modified: N6-glutaryllysine
- K757 (= K341) modified: N6-glutaryllysine; alternate
- K772 (= K356) modified: N6-glutaryllysine; alternate
- P774 (= P358) to L: in CPS1D; the enzyme is inactive
- K793 (= K377) modified: N6-glutaryllysine; alternate
- K811 (= K395) modified: N6-glutaryllysine; alternate
- K841 (≠ S422) modified: N6-glutaryllysine; alternate
- L843 (= L424) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (= R431) 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 (≠ E437) modified: N6-glutaryllysine; alternate
- K869 (≠ S450) modified: N6-glutaryllysine
- T871 (≠ S452) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (≠ P456) 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 (≠ E470) modified: N6-glutaryllysine; alternate
- K892 (≠ R473) modified: N6-glutaryllysine; alternate
- K905 (≠ R485) modified: N6-glutaryllysine
- K908 (= K488) modified: N6-glutaryllysine; alternate
- G911 (= G491) 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 (= S493) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- D914 (= D494) 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 (≠ R495) modified: N6-glutaryllysine; alternate
- S918 (≠ A498) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ E499) modified: N6-glutaryllysine; alternate
- R932 (= R512) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (= I517) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (= A529) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (≠ Y538) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- Y959 (= Y539) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- Y962 (= Y542) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- G964 (≠ Q544) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I566) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G567) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (= K654) modified: N6-glutaryllysine; alternate
- K1150 (≠ E730) modified: N6-glutaryllysine
- K1168 (= K748) modified: N6-glutaryllysine; alternate
- K1183 (≠ D762) modified: N6-glutaryllysine; alternate
- I1215 (≠ L794) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (≠ V803) modified: N6-glutaryllysine
- I1254 (≠ L834) to F: in CPS1D; uncertain significance
- F1266 (≠ Y846) to S: in dbSNP:rs1047886
- M1283 (≠ I863) to L: in dbSNP:rs1047887
- K1356 (≠ A934) modified: N6-glutaryllysine; alternate
- K1360 (= K938) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ LVTV 942:945) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ P955) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (≠ V957) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (= L960) to S: in CPS1D; significant loss of protein stability
- T1406 (≠ E985) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ L990) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (≠ R1017) 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 (= R1027) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- K1479 (≠ A1053) 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
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
43% identity, 98% coverage: 4:1055/1075 of query aligns to 419:1481/1500 of Q8C196
- K1291 (≠ L871) 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
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)
44% identity, 97% coverage: 5:1051/1075 of query aligns to 402:1449/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
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)
44% identity, 97% coverage: 5:1051/1075 of query aligns to 388:1452/2198 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.
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
42% identity, 98% coverage: 4:1058/1075 of query aligns to 377:1425/1430 of 5douD
- active site: R505 (= R129), R545 (= R169), N576 (≠ G202), E589 (= E215), H617 (= H243), N656 (= N282), Q658 (= Q284), E672 (= E298), N674 (= N300), R676 (= R302), S680 (= S306), G880 (= G502), A1006 (≠ K628), R1087 (= R709), E1116 (= E754), K1124 (≠ D762), Q1184 (= Q822), E1196 (= E835), N1198 (= N837), R1203 (= R842), R1260 (≠ L897)
- binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ V167), R545 (= R169), L550 (= L174), G551 (= G175), G552 (= G176), E581 (= E207), S583 (≠ C209), V584 (= V210), T585 (≠ S211), E589 (= E215), M614 (= M240), G615 (= G241), V616 (≠ I242), H617 (= H243), Q658 (= Q284), I671 (= I297), E672 (= E298), L1085 (= L707), F1110 (≠ Y749), V1111 (≠ I750), E1116 (= E754), A1140 (= A778), V1142 (≠ I780), H1143 (= H781), S1144 (= S782), Q1184 (= Q822), L1186 (≠ V824), I1195 (≠ L834), E1196 (= E835)
- binding magnesium ion: Q658 (= Q284), E672 (= E298), E672 (= E298), N674 (= N300)
- binding n-acetyl-l-glutamate: I1307 (≠ V945), Q1308 (≠ S946), T1332 (= T970), A1334 (≠ G972), T1335 (= T973), W1351 (≠ K989), L1379 (≠ T1012), T1384 (≠ R1017), K1385 (≠ R1018), F1386 (≠ P1019), N1390 (≠ G1023)
- binding phosphate ion: L550 (= L174), G551 (= G175), H617 (= H243), E672 (= E298), N674 (= N300), R676 (= R302), R679 (= R305)
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)
42% identity, 97% coverage: 7:1054/1075 of query aligns to 28:1087/1118 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 (= I297) mutation I->G,S,H: Reduces ammonia-dependent ATPase activity 17-64 fold.
- H807 (= H781) mutation to N: No effect.
- D810 (= D784) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
42% identity, 98% coverage: 4:1058/1075 of query aligns to 374:1414/1422 of 6w2jA
- active site: Q651 (= Q284), E665 (= E298), N667 (= N300), S673 (= S306), G869 (= G502), A995 (≠ K628), K1113 (≠ D762), R1249 (≠ L897)
- 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 (= P358), R726 (= R359), W727 (= W360), D730 (= D363), F732 (= F365), F756 (≠ L393), L760 (≠ V397), C763 (≠ L400), H764 (≠ E401), S795 (≠ D429), R797 (= R431), I798 (≠ L432)
Sites not aligning to the query:
Query Sequence
>WP_015738405.1 NCBI__GCF_000024605.1:WP_015738405.1
MPRRKDLKKVMVIGSGPIIIGQAAEFDYSGTQACRALREEGLEVVLVNSNPATIMTDPNM
ADRVYIEPLTPEFVAKVLRKERPDGLLPTLGGQVGLNLAVELSRMGVLDELGVELLGTPL
ETIEKAEDRELFKETMRAIGEPIPESRIVSRLEDAVSFAREIGFPVVVRPAYTLGGTGGG
IARNEEELLEIAARGLKHSLIGQILVEQCVSGWKEIEFEVMRDGADNCITVCCMENLDPM
GIHTGDSIVVAPSQTLTDKEYQMLRRAAIKIIRALGIRGGCNIQFALDPRSLRYYVIEVN
PRVSRSSALASKATGYPIAKVAAKIAVGLRLDEIQNAVTGKTTACFEPSIDYVVVKFPRW
PFDKFALANRVLGTQMKSTGEVMAIGRTFEEALLKAVRSLEIGLHGLVLPEAERFSDMEI
ESKLESPTDERLFVVAEALRRGYPVSKVASLSAIDPWFLERIKRLVEFEEALRRAGKELD
PEILRQAKTLGFSDRTIAEFTGLPEDVVREKRKVWGIKPVYKMVDTCAAEFEAATPYYYS
TYEQEDEAPALEGRKVVVLGSGPIRIGQGIEFDYCSVHCVWALREEGIKAIIINNNPETV
STDFDTADRLYFEPLVAEDVLNVLEKEKPEGVLVQFGGQTAINLAKPLAAAGFKILGTAV
EDIDRAEDREKFDRVLEAENIPRPPGGAAKSPEEALAVAERVGFPVLVRPSYVLGGRAME
IVYNREELEEYMRFAARVSPEYPVLVDKYIFGKEVEVDAISDGEDVLIPGIMEHIERAGI
HSGDSIAVYPPRTLNGEVVEQVVSYTTALARALRVRGLLNIQYVVDAEGKVYVLEVNPRA
SRTVPYLSKITGIPMIPLAVKVILGKKLKELGYGTGLYRGGRYFGIKVPVFSFAKLLDVD
VSLGPEMKSTGEVMGVAEDFAAALYKGCVAAGYAFPEKGAVLVTVSDRDKEEALPLVKEL
ARLGFKILATSGTARMLSAAGVPVETVKKLHEGSPNIIDLLRAGKIQMVLNTLTKGRRPE
REGFRIRRTAVELGIPCITSLDTMRAVVEVMRARRQGIRLPVISLQEYQEREKEA
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