SitesBLAST
Comparing WP_012466868.1 NCBI__GCF_000020465.1:WP_012466868.1 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)
48% identity, 98% coverage: 12:617/618 of query aligns to 568:1181/1187 of Q42601
- G587 (= G31) mutation to E: In ven3-3; reticulate leaf phenotype.
- A844 (= A275) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P449) mutation to L: In ven3-1; reticulate leaf phenotype.
Sites not aligning to the query:
- 149 P→L: In ven3-2; reduced plant size and reticulate leaf phenotype.
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
49% identity, 96% coverage: 24:614/618 of query aligns to 489:1070/1073 of 1bxrA
- active site: G507 (≠ K42), K634 (≠ Q168), R715 (= R249), G721 (= G255), G722 (= G256), S745 (= S279), E761 (= E295), D769 (= D303), Q829 (= Q363), E841 (= E375), N843 (= N377), R848 (= R382), P901 (≠ V441)
- binding phosphoaminophosphonic acid-adenylate ester: R675 (= R209), V713 (≠ L247), R715 (= R249), L720 (= L254), G721 (= G255), G722 (= G256), M725 (= M259), D753 (= D287), F755 (= F289), L756 (= L290), E761 (= E295), A785 (= A319), G786 (= G320), V787 (≠ I321), H788 (= H322), Q829 (= Q363), E841 (= E375), N843 (= N377), R848 (= R382)
- binding manganese (ii) ion: Q829 (= Q363), E841 (= E375), E841 (= E375), N843 (= N377)
- binding L-ornithine: E783 (= E317), D791 (= D325), E892 (= E432), L907 (= L447), D1041 (≠ V583), T1042 (= T584)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338
- binding phosphoaminophosphonic acid-adenylate ester: 129, 167, 169, 174, 175, 176, 210, 211, 215, 240, 241, 243, 244, 285, 299, 306, 376
- binding manganese (ii) ion: 299, 301
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)
49% identity, 96% coverage: 24:614/618 of query aligns to 489:1070/1073 of P00968
- R715 (= R249) binding ATP
- H754 (≠ R288) binding ATP
- L756 (= L290) binding ATP
- E761 (= E295) binding ATP
- G786 (= G320) binding ATP
- V787 (≠ I321) binding ATP
- H788 (= H322) binding ATP
- S789 (= S323) binding ATP
- Q829 (= Q363) binding ATP; binding Mn(2+)
- E841 (= E375) binding ATP; binding Mn(2+); binding Mn(2+)
- N843 (= N377) binding Mn(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 129 binding ATP
- 169 binding ATP
- 175 binding ATP
- 176 binding ATP
- 208 binding ATP
- 210 binding ATP
- 215 binding ATP
- 241 binding ATP
- 242 binding ATP
- 243 binding ATP
- 285 binding ATP; binding Mn(2+)
- 299 binding ATP; binding Mn(2+); binding Mn(2+)
- 301 binding Mn(2+)
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
48% identity, 96% coverage: 24:614/618 of query aligns to 489:1055/1058 of 1t36A
- active site: G507 (≠ K42), K634 (≠ Q168), R715 (= R249), E746 (= E295), D754 (= D303), Q814 (= Q363), E826 (= E375), N828 (= N377), R833 (= R382), P886 (≠ V441)
- binding adenosine-5'-diphosphate: R715 (= R249), M718 (= M259), F740 (= F289), L741 (= L290), E746 (= E295), A770 (= A319), G771 (= G320), V772 (≠ I321), H773 (= H322), E826 (= E375), P894 (= P449)
- binding manganese (ii) ion: Q814 (= Q363), E826 (= E375)
- binding L-ornithine: E768 (= E317), D776 (= D325), E877 (= E432), L892 (= L447), D1026 (≠ V583), T1027 (= T584)
- binding uridine-5'-monophosphate: K939 (= K494), T959 (= T515), G961 (= G517), T962 (= T518), K978 (= K534), N1000 (= N557), T1001 (= T558), T1002 (≠ P559), S1011 (≠ E568), I1014 (= I571)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 175, 176, 208, 210, 211, 215, 240, 241, 242, 243, 285, 298, 299, 376
- binding manganese (ii) ion: 285, 299, 299, 301
- binding phosphate ion: 174, 175, 243, 299, 301, 303, 306
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
48% identity, 96% coverage: 24:614/618 of query aligns to 489:1055/1058 of 1c3oA
- active site: G507 (≠ K42), K634 (≠ Q168), R715 (= R249), E746 (= E295), D754 (= D303), Q814 (= Q363), E826 (= E375), N828 (= N377), R833 (= R382), P886 (≠ V441)
- binding adenosine-5'-diphosphate: R715 (= R249), M718 (= M259), F740 (= F289), L741 (= L290), E746 (= E295), A770 (= A319), G771 (= G320), V772 (≠ I321), H773 (= H322), S774 (= S323), E826 (= E375)
- binding glutamine: R528 (≠ T63), A537 (≠ D72), T538 (≠ A73), N554 (≠ V89)
- binding manganese (ii) ion: Q814 (= Q363), E826 (= E375)
- binding L-ornithine: E768 (= E317), D776 (= D325), E877 (= E432), L892 (= L447), D1026 (≠ V583), T1027 (= T584)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 176, 210, 211, 215, 240, 241, 243, 244, 285, 298, 299, 376
- binding manganese (ii) ion: 285, 299, 299, 301
- binding phosphate ion: 174, 175, 243, 299, 301, 303, 306
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
48% identity, 96% coverage: 24:614/618 of query aligns to 489:1055/1058 of 1ce8A
- active site: G507 (≠ K42), K634 (≠ Q168), R715 (= R249), E746 (= E295), D754 (= D303), Q814 (= Q363), E826 (= E375), N828 (= N377), R833 (= R382), P886 (≠ V441)
- binding adenosine-5'-diphosphate: R715 (= R249), F740 (= F289), L741 (= L290), E746 (= E295), A770 (= A319), G771 (= G320), V772 (≠ I321), H773 (= H322), S774 (= S323), E826 (= E375)
- binding inosinic acid: S933 (= S488), K939 (= K494), T959 (= T515), G961 (= G517), T962 (= T518), K978 (= K534), V979 (= V535), I986 (= I543), N1000 (= N557), T1001 (= T558), T1002 (≠ P559), D1010 (= D567), S1011 (≠ E568), V1013 (≠ A570)
- binding manganese (ii) ion: Q814 (= Q363), E826 (= E375)
- binding L-ornithine: R528 (≠ T63), A537 (≠ D72), T538 (≠ A73), E552 (= E87), N554 (≠ V89), E768 (= E317), D776 (= D325), E877 (= E432), L892 (= L447), Y1025 (≠ F582), D1026 (≠ V583), T1027 (= T584)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 176, 210, 211, 215, 240, 241, 242, 243, 285, 298, 299, 376
- binding manganese (ii) ion: 174, 285, 299, 299, 301
- binding phosphate ion: 174, 175, 243, 299, 301, 303, 306
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
47% identity, 96% coverage: 24:614/618 of query aligns to 489:1055/1058 of 1a9xA
- active site: G507 (≠ K42), K634 (≠ Q168), D754 (= D303), P886 (≠ V441)
- binding adenosine-5'-diphosphate: R715 (= R249), M718 (= M259), F740 (= F289), L741 (= L290), E746 (= E295), A770 (= A319), G771 (= G320), V772 (≠ I321), H773 (= H322), E826 (= E375)
- binding manganese (ii) ion: Q814 (= Q363), E826 (= E375)
- binding L-ornithine: E768 (= E317), D776 (= D325), E877 (= E432), L892 (= L447), Y1025 (≠ F582), D1026 (≠ V583), T1027 (= T584)
Sites not aligning to the query:
- active site: 202, 338
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 175, 176, 210, 215, 240, 241, 242, 243, 244, 285, 298, 299, 376
- binding manganese (ii) ion: 285, 299, 299, 301
- binding phosphate ion: 175, 243, 299, 301, 303, 306
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)
37% identity, 94% coverage: 14:596/618 of query aligns to 900:1485/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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, 99% coverage: 7:615/618 of query aligns to 886:1494/1500 of P31327
- K889 (≠ Q10) modified: N6-glutaryllysine; alternate
- K892 (≠ S13) modified: N6-glutaryllysine; alternate
- K905 (≠ I25) modified: N6-glutaryllysine
- K908 (= K28) modified: N6-glutaryllysine; alternate
- G911 (= G31) 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 (= S33) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- D914 (= D34) 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 (≠ C35) modified: N6-glutaryllysine; alternate
- S918 (≠ A38) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ N39) modified: N6-glutaryllysine; alternate
- R932 (= R52) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (≠ V57) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (= A69) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (≠ H78) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- Y959 (= Y79) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- Y962 (= Y82) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- G964 (≠ E84) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I106) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G107) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ T194) modified: N6-glutaryllysine; alternate
- K1150 (≠ E270) modified: N6-glutaryllysine
- K1168 (≠ R288) modified: N6-glutaryllysine; alternate
- K1183 (≠ D303) modified: N6-glutaryllysine; alternate
- I1215 (= I335) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (= K344) modified: N6-glutaryllysine
- I1254 (= I374) to F: in CPS1D; uncertain significance
- F1266 (= F386) to S: in dbSNP:rs1047886
- M1283 (= M403) to L: in dbSNP:rs1047887
- K1356 (≠ E478) modified: N6-glutaryllysine; alternate
- K1360 (≠ S482) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ FISV 486:489) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ A500) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (= A502) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (= L505) to S: in CPS1D; significant loss of protein stability
- T1406 (≠ K530) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ V535) 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 (≠ G572) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- K1479 (≠ C598) modified: N6-glutaryllysine; alternate
- K1486 (= K607) modified: N6-glutaryllysine; alternate
- Y1491 (= Y612) 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
- 438 A → P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- 453 modified: N6-glutaryllysine; alternate
- 458 modified: N6-glutaryllysine; alternate
- 527 modified: N6-glutaryllysine; alternate
- 530 G → V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
- 532 modified: N6-glutaryllysine; alternate
- 544 T → 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
- 553 modified: N6-glutaryllysine; alternate
- 678 Q → P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- 728 modified: N6-glutaryllysine
- 757 modified: N6-glutaryllysine; alternate
- 772 modified: N6-glutaryllysine; alternate
- 774 P → L: in CPS1D; the enzyme is inactive
- 793 modified: N6-glutaryllysine; alternate
- 811 modified: N6-glutaryllysine; alternate
- 841 modified: N6-glutaryllysine; alternate
- 843 L → S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- 850 R → C: in CPS1D; moderate decrease in protein yield and partial loss of enzyme activity; dbSNP:rs1015051007; R → H: in CPS1D; partial loss of enzyme activity; dbSNP:rs767694281
- 856 modified: N6-glutaryllysine; alternate
- 869 modified: N6-glutaryllysine
- 871 T → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 875 modified: N6-glutaryllysine; alternate; K → 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
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
36% identity, 99% coverage: 7:615/618 of query aligns to 886:1494/1500 of Q8C196
- K1291 (≠ L411) 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)
36% identity, 99% coverage: 7:615/618 of query aligns to 886:1494/1500 of P07756
- S1331 (= S453) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T454) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T515) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T518) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ K534) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N557) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ R560) 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.
Sites not aligning to the query:
- 537 modified: carbohydrate, O-linked (GlcNAc) serine; alternate
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)
36% identity, 97% coverage: 17:616/618 of query aligns to 937:1535/2244 of Q09794
- S1119 (= S199) modified: Phosphoserine
Sites not aligning to the query:
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
6w2jB Cps1 bound to allosteric inhibitor h3b-374 (see paper)
35% identity, 98% coverage: 7:614/618 of query aligns to 775:1364/1364 of 6w2jB
Sites not aligning to the query:
- active site: 593, 607, 609, 615
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 547, 549, 557, 668, 669, 672, 673, 698, 702, 705, 706, 737, 739, 740
- binding zinc ion: 273, 293, 295, 320
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
35% identity, 98% coverage: 7:614/618 of query aligns to 833:1422/1422 of 6w2jA
Sites not aligning to the query:
- active site: 651, 665, 667, 673
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 605, 607, 615, 725, 726, 727, 730, 732, 756, 760, 763, 764, 795, 797, 798
- binding zinc ion: 273, 293, 295, 320
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
35% identity, 95% coverage: 7:596/618 of query aligns to 844:1418/1430 of 5douD
- active site: G880 (≠ K42), A1006 (≠ Q168), R1087 (= R249), E1116 (= E295), K1124 (≠ D303), Q1184 (= Q363), E1196 (= E375), N1198 (= N377), R1203 (= R382), R1260 (≠ V441)
- binding adenosine-5'-diphosphate: L1085 (= L247), F1110 (= F289), V1111 (≠ L290), E1116 (= E295), A1140 (= A319), V1142 (≠ I321), H1143 (= H322), S1144 (= S323), Q1184 (= Q363), L1186 (≠ A365), I1195 (= I374), E1196 (= E375)
- binding n-acetyl-l-glutamate: I1307 (≠ V489), Q1308 (≠ N490), T1332 (= T515), A1334 (≠ G517), T1335 (= T518), W1351 (≠ K534), L1379 (≠ T558), T1384 (vs. gap), K1385 (= K563), F1386 (≠ A564), N1390 (≠ E568)
Sites not aligning to the query:
- active site: 252, 335, 337, 505, 545, 576, 589, 617, 656, 658, 672, 674, 676, 680
- binding adenosine-5'-diphosphate: 505, 543, 545, 550, 551, 552, 581, 583, 584, 585, 589, 614, 615, 616, 617, 658, 671, 672
- binding magnesium ion: 658, 672, 672, 674
- binding phosphate ion: 550, 551, 617, 672, 674, 676, 679
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)
36% identity, 89% coverage: 8:559/618 of query aligns to 861:1411/2224 of P05990
- E1167 (≠ Q314) 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
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)
34% identity, 97% coverage: 3:602/618 of query aligns to 854:1458/2198 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)
36% identity, 87% coverage: 19:557/618 of query aligns to 858:1394/2225 of P08955
Sites not aligning to the query:
- 1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.
P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
37% identity, 83% coverage: 19:532/618 of query aligns to 858:1362/2225 of P27708
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
- 456 modified: Phosphothreonine; by MAPK1
- 735 Y → C: in a colorectal cancer sample; somatic mutation
- 1406 modified: Phosphoserine; by PKA
- 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
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)
34% identity, 94% coverage: 17:600/618 of query aligns to 870:1453/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Query Sequence
>WP_012466868.1 NCBI__GCF_000020465.1:WP_012466868.1
MTTQVSSLSQELSGLASKLPKKTLIKAKEHGFSDCQLANIFKTTETVIRTLRKQYGVESV
FKTVDTCAAEFDAKTPYHYSTYDEENESVRSDRKKVIILGGGPNRIGQGIEFDYCCVQAV
FALREAGYETIMVNCNPETVSTDYDIADKLYFEPLTFEDTIRIIEHEQPLGVIVSFGGQT
PLKLSTKLDEAGVTILGTSSKGIDLAEDRKKFGALLEKLDILHPDYGTAICFDEALAITE
RIGYPVLVRPSYVLGGRAMKIIYNKDSLKEYVDQALFISEKYPLLIDRFLETAVEFDIDA
IADTTDCVISGIMQHVEAAGIHSGDSTSILPYRNISQEVINTMKAYTRTLAEHLKVVGLM
NVQYAVQNESVYVIEVNPRASRTVPFVGKATAVPVVKIATRVMLGEKLSDLRKEYDLKDC
DELGMKHMAIKEPVFPFSKFVKSGVYLGPEMRSTGEAMSLAEQFPEAFAKAYQAANMELP
LSGSVFISVNDQDKSQRIIAIAKELYRMDFDLVATAGTHRFLIENGIECKKVFKVGEEGR
PNIFDIIKHGKIDFVINTPRGEKALHDEEAIGAASVLSNVPFVTTIEAAEASVQAIDCIR
RQEFGVKSLQEYSAYRNK
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