SitesBLAST
Comparing WP_058932374.1 NCBI__GCF_001484605.1:WP_058932374.1 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)
54% identity, 97% coverage: 3:1088/1114 of query aligns to 94:1175/1187 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 (= A739) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P923) mutation to L: In ven3-1; reticulate leaf phenotype.
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
53% identity, 98% coverage: 1:1093/1114 of query aligns to 1:1072/1073 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 (≠ H502), K634 (≠ E628), R715 (= R713), G721 (= G719), G722 (= G720), S745 (≠ T743), E761 (= E759), D769 (= D767), Q829 (= Q827), E841 (= E839), N843 (= N841), R848 (= R846), P901 (≠ R910)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G175 (= G175), G176 (= G176), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (≠ V240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), E299 (= E299), R306 (= R306), T376 (= T375), R675 (= R673), V713 (≠ L711), R715 (= R713), L720 (= L718), G721 (= G719), G722 (= G720), M725 (= M723), D753 (= D751), F755 (= F753), L756 (= L754), E761 (= E759), A785 (= A783), G786 (= G784), V787 (≠ I785), H788 (= H786), Q829 (= Q827), E841 (= E839), N843 (= N841), R848 (= R846)
- binding manganese (ii) ion: E299 (= E299), N301 (= N301), Q829 (= Q827), E841 (= E839), E841 (= E839), N843 (= N841)
- binding L-ornithine: E783 (= E781), D791 (= D789), E892 (= E901), L907 (= L921), D1041 (≠ I1060), T1042 (= T1061)
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)
53% identity, 98% coverage: 1:1093/1114 of query aligns to 1:1072/1073 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 (= E208) binding ATP
- L210 (≠ I210) binding ATP
- E215 (= E215) binding ATP
- G241 (= G241) binding ATP
- I242 (≠ V242) binding ATP
- H243 (= H243) binding ATP
- Q285 (= Q285) binding ATP; binding Mn(2+)
- E299 (= E299) binding ATP; binding Mn(2+); binding Mn(2+)
- N301 (= N301) binding Mn(2+)
- R715 (= R713) binding ATP
- H754 (≠ R752) binding ATP
- L756 (= L754) binding ATP
- E761 (= E759) binding ATP
- G786 (= G784) binding ATP
- V787 (≠ I785) binding ATP
- H788 (= H786) binding ATP
- S789 (= S787) binding ATP
- Q829 (= Q827) binding ATP; binding Mn(2+)
- E841 (= E839) binding ATP; binding Mn(2+); binding Mn(2+)
- N843 (= N841) binding Mn(2+)
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
53% identity, 98% coverage: 1:1093/1114 of query aligns to 1:1057/1058 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 (≠ H502), K634 (≠ E628), R715 (= R713), E746 (= E759), D754 (= D767), Q814 (= Q827), E826 (= E839), N828 (= N841), R833 (= R846), P886 (≠ R910)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G175 (= G175), G176 (= G176), E208 (= E208), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (≠ V240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R713), M718 (= M723), F740 (= F753), L741 (= L754), E746 (= E759), A770 (= A783), G771 (= G784), V772 (≠ I785), H773 (= H786), E826 (= E839), P894 (= P923)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q827), E826 (= E839)
- binding L-ornithine: E768 (= E781), D776 (= D789), E877 (= E901), L892 (= L921), D1026 (≠ I1060), T1027 (= T1061)
- binding phosphate ion: M174 (= M174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
- binding uridine-5'-monophosphate: K939 (= K968), T959 (= T988), G961 (= G990), T962 (= T991), K978 (= K1007), N1000 (= N1034), T1001 (= T1035), T1002 (≠ P1036), S1011 (≠ G1045), I1014 (≠ L1048)
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
53% identity, 98% coverage: 1:1093/1114 of query aligns to 1:1057/1058 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 (≠ H502), K634 (≠ E628), R715 (= R713), E746 (= E759), D754 (= D767), Q814 (= Q827), E826 (= E839), N828 (= N841), R833 (= R846), P886 (≠ R910)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G176 (= G176), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (≠ V240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R713), M718 (= M723), F740 (= F753), L741 (= L754), E746 (= E759), A770 (= A783), G771 (= G784), V772 (≠ I785), H773 (= H786), S774 (= S787), E826 (= E839)
- binding glutamine: R528 (≠ T523), A537 (= A532), T538 (≠ A533), N554 (≠ A549)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q827), E826 (= E839)
- binding L-ornithine: E768 (= E781), D776 (= D789), E877 (= E901), L892 (= L921), D1026 (≠ I1060), T1027 (= T1061)
- 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)
52% identity, 98% coverage: 1:1093/1114 of query aligns to 1:1057/1058 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 (≠ H502), K634 (≠ E628), R715 (= R713), E746 (= E759), D754 (= D767), Q814 (= Q827), E826 (= E839), N828 (= N841), R833 (= R846), P886 (≠ R910)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G176 (= G176), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (≠ V240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R713), F740 (= F753), L741 (= L754), E746 (= E759), A770 (= A783), G771 (= G784), V772 (≠ I785), H773 (= H786), S774 (= S787), E826 (= E839)
- binding inosinic acid: S933 (= S962), K939 (= K968), T959 (= T988), G961 (= G990), T962 (= T991), K978 (= K1007), V979 (= V1008), I986 (= I1020), N1000 (= N1034), T1001 (= T1035), T1002 (≠ P1036), D1010 (= D1044), S1011 (≠ G1045), V1013 (≠ A1047)
- binding manganese (ii) ion: M174 (= M174), Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q827), E826 (= E839)
- binding L-ornithine: R528 (≠ T523), A537 (= A532), T538 (≠ A533), E552 (= E547), N554 (≠ A549), E768 (= E781), D776 (= D789), E877 (= E901), L892 (= L921), Y1025 (≠ C1059), D1026 (≠ I1060), T1027 (= T1061)
- 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)
52% identity, 98% coverage: 1:1093/1114 of query aligns to 1:1057/1058 of 1a9xA
- active site: K202 (≠ S202), D338 (= D338), G507 (≠ H502), K634 (≠ E628), D754 (= D767), P886 (≠ R910)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (= M174), G175 (= G175), G176 (= G176), L210 (≠ I210), E215 (= E215), M240 (≠ V240), G241 (= G241), I242 (≠ V242), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R713), M718 (= M723), F740 (= F753), L741 (= L754), E746 (= E759), A770 (= A783), G771 (= G784), V772 (≠ I785), H773 (= H786), E826 (= E839)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q827), E826 (= E839)
- binding L-ornithine: E768 (= E781), D776 (= D789), E877 (= E901), L892 (= L921), Y1025 (≠ C1059), D1026 (≠ I1060), T1027 (= T1061)
- binding phosphate ion: G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
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)
41% identity, 97% coverage: 6:1086/1114 of query aligns to 473:1528/2244 of Q09794
- S1119 (= S663) 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)
40% identity, 96% coverage: 4:1073/1114 of query aligns to 435:1485/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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, 96% coverage: 7:1077/1114 of query aligns to 404:1453/2225 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)
41% identity, 96% coverage: 8:1074/1114 of query aligns to 391:1453/2198 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.
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, 96% coverage: 8:1073/1114 of query aligns to 394:1440/2225 of P08955
- S1406 (= S1043) 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.
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, 96% coverage: 8:1077/1114 of query aligns to 404:1456/2224 of P05990
- E1167 (= E778) 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
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)
40% identity, 96% coverage: 8:1073/1114 of query aligns to 394:1440/2225 of P27708
- T456 (= T70) modified: Phosphothreonine; by MAPK1
- Y735 (= Y353) to C: in a colorectal cancer sample; somatic mutation
- S1406 (= S1043) 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
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, 97% coverage: 4:1080/1114 of query aligns to 419:1484/1500 of P07756
- S537 (≠ N119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S927) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T928) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T988) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T991) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ K1007) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N1034) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ S1037) 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)
38% identity, 97% coverage: 4:1080/1114 of query aligns to 419:1484/1500 of Q8C196
- K1291 (≠ L875) 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
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)
40% identity, 94% coverage: 7:1058/1114 of query aligns to 28:1069/1118 of P03965
- L229 (≠ I210) 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 (= H786) mutation to N: No effect.
- D810 (= D789) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
38% identity, 96% coverage: 4:1077/1114 of query aligns to 419:1481/1500 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 (≠ A109) modified: N6-glutaryllysine; alternate
- G530 (≠ N112) 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 (≠ V135) 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 (= K342) 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 (≠ E423) modified: N6-glutaryllysine; alternate
- L843 (≠ A425) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (= R432) 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 (≠ R438) modified: N6-glutaryllysine; alternate
- K869 (≠ E451) modified: N6-glutaryllysine
- T871 (= T453) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (≠ P457) 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 (≠ H471) modified: N6-glutaryllysine; alternate
- K892 (≠ R474) modified: N6-glutaryllysine; alternate
- K905 (= K485) 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 (≠ E495) modified: N6-glutaryllysine; alternate
- S918 (≠ G498) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ S499) 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 (≠ H538) 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 (≠ E544) 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 (≠ P658) modified: N6-glutaryllysine; alternate
- K1150 (≠ R734) modified: N6-glutaryllysine
- K1168 (≠ R752) modified: N6-glutaryllysine; alternate
- K1183 (≠ D767) modified: N6-glutaryllysine; alternate
- I1215 (≠ L799) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (≠ R808) modified: N6-glutaryllysine
- I1254 (≠ L838) to F: in CPS1D; uncertain significance
- F1266 (= F850) to S: in dbSNP:rs1047886
- M1283 (≠ G867) to L: in dbSNP:rs1047887
- K1356 (≠ A952) modified: N6-glutaryllysine; alternate
- K1360 (≠ E956) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ FVSV 960:963) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ M973) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (≠ V975) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (= L978) to S: in CPS1D; significant loss of protein stability
- T1406 (≠ S1003) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ V1008) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (vs. gap) 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 (= R1049) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- K1479 (≠ A1075) 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
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
37% identity, 95% coverage: 4:1062/1114 of query aligns to 377:1407/1430 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 (≠ H502), A1006 (≠ R629), R1087 (= R713), E1116 (= E759), K1124 (≠ D767), Q1184 (= Q827), E1196 (= E839), N1198 (= N841), R1203 (= R846), R1260 (= R910)
- binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ V167), R545 (= R169), L550 (≠ M174), G551 (= G175), G552 (= G176), E581 (= E207), S583 (= S209), V584 (≠ I210), T585 (≠ L211), E589 (= E215), M614 (≠ V240), G615 (= G241), V616 (= V242), H617 (= H243), Q658 (= Q285), I671 (= I298), E672 (= E299), L1085 (= L711), F1110 (= F753), V1111 (≠ L754), E1116 (= E759), A1140 (= A783), V1142 (≠ I785), H1143 (= H786), S1144 (= S787), Q1184 (= Q827), L1186 (≠ A829), I1195 (≠ L838), E1196 (= E839)
- binding magnesium ion: Q658 (= Q285), E672 (= E299), E672 (= E299), N674 (= N301)
- binding n-acetyl-l-glutamate: I1307 (≠ V963), Q1308 (≠ A964), T1332 (= T988), A1334 (≠ G990), T1335 (= T991), W1351 (≠ K1007), L1379 (≠ T1035), T1384 (vs. gap), K1385 (≠ E1040), F1386 (≠ A1041), N1390 (≠ G1045)
- 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, 98% coverage: 1:1091/1114 of query aligns to 368:1422/1422 of 6w2jA
- active site: Q651 (= Q285), E665 (= E299), N667 (= N301), S673 (= S307), G869 (≠ H502), A995 (≠ R629), K1113 (≠ D767), R1249 (= R910)
- 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 (≠ V240), V615 (≠ I248), P725 (= P359), R726 (= R360), W727 (≠ F361), D730 (≠ E364), F732 (= F366), F756 (≠ L394), L760 (= L398), C763 (vs. gap), H764 (vs. gap), S795 (≠ T430), R797 (= R432), I798 (≠ L433)
Sites not aligning to the query:
Query Sequence
>WP_058932374.1 NCBI__GCF_001484605.1:WP_058932374.1
MPKRTDLKSVLVIGSGPIVIGQAAEFDYSGTQALRVLKEEGLRVILVNSNPATIMTDPEF
ADATYIEPITPEVVEKIIAKERPDAILPTLGGQTALNTAIALDKNGVLAKYNVELIGANI
AAIELGEDREKFKGVVERCGAESARSHIIHTMDEAFTAAEDLGYPMVVRPSFTMGGLGSG
LAYNENDLRRIVGQGLQYSPTSEVLLEESILGWKEYELEMMRDKNDNVVVVCSIENFDPV
GVHTGDSITVAPALTLTDREYQRLRDISIAVIREVGVDTGGCNIQFAIEPDTGRVVVIEM
NPRVSRSSALASKATGFAIAKIATKLSLGYTLDEIPNDITQKTPASFEPTLDYVVVKVPR
FAFEKFPAADDTLTTTMKSVGEAMAMGRNFTEALQKALRSLEQKGSQLDFSSVPEWEVPE
LIEKAKRPTTERLHQVQRALLGGATVEQLFEATKIDPWYLDQLQLLNEISHEIRQAGALT
VEMLKRAKRHGFSDEQIGSLTHNSEAVVRGVRQALGIRPVYKTVDTCAAEFAAYTPYHYS
SYDEEDEIALHSKPSILILGSGPNRIGQGIEFDYSCVHASMALRKAGYETVMVNCNPETV
STDYDVSTRLYFEPLTLEDVLEVIAAEERTGGVMGVFVQLGGQTPLKLAQQLADAGVPIL
GTSPEAIDLAEHRGEFSRVLDNAGLIAPKNGTAVSFDDAKKIADEIGYPVLVRPSYVLGG
RGMEIVYDEPNLSRYIANATEITPDHPVLIDRFLEDAVEIDVDALFDGTDMYLGGIMEHI
EEAGIHSGDSACVLPPITLGNNVIERVRTATRAIAEGVGVRGLINIQFALASDVLYVLEA
NPRASRTVPFVSKATGVQMAKAAALIGTGVTIHQLRTAYKMLPETGDGSTLPLDAPVSVK
EAVLPFSRFRTPEGKVVDSLLGPEMRSTGEVMGIDKHFDTAFAKSQAAANNALPTEGKIF
VSVANRDKRAVIMAVKRLADLGFEIVSTGGTADVLRRNGIQASTVRKVAEGSSAEGEGTI
ADLVIAGEIDMVFNTPSGGEARSDGYALRAAATSIGIPCITTVAEFNAAVQAIEAMRTYE
WSVTSLQEHAAALVASQKAVAENAAAESAVSQNA
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