SitesBLAST
Comparing WP_015944958.1 NCBI__GCF_000021925.1:WP_015944958.1 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)
47% identity, 99% coverage: 14:1064/1065 of query aligns to 99:1170/1187 of Q42601
- P149 (≠ Q64) 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 (= A739) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P908) mutation to L: In ven3-1; reticulate leaf phenotype.
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
48% identity, 98% coverage: 16:1054/1065 of query aligns to 10:1054/1073 of 1bxrA
- active site: R129 (= R135), R169 (= R175), M174 (≠ L180), G176 (= G182), K202 (≠ D208), E215 (= E221), H243 (= H249), N283 (= N288), Q285 (= Q290), E299 (= E304), N301 (= N306), R303 (= R308), S307 (= S312), D338 (≠ A343), G507 (≠ Q506), K634 (≠ Q632), R715 (= R713), G721 (= G719), G722 (= G720), S745 (≠ F743), E761 (= E758), D769 (= D766), Q829 (= Q826), E841 (= E838), N843 (= N840), R848 (= R845), P901 (≠ H900)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R135), I167 (= I173), R169 (= R175), M174 (≠ L180), G175 (= G181), G176 (= G182), L210 (≠ V216), I211 (≠ A217), E215 (= E221), M240 (≠ V246), G241 (= G247), H243 (= H249), T244 (= T250), Q285 (= Q290), E299 (= E304), R306 (= R311), T376 (= T380), R675 (= R673), V713 (≠ M711), R715 (= R713), L720 (= L718), G721 (= G719), G722 (= G720), M725 (= M723), D753 (= D751), F755 (≠ Y753), L756 (= L754), E761 (= E758), A785 (= A782), G786 (= G783), V787 (= V784), H788 (= H785), Q829 (= Q826), E841 (= E838), N843 (= N840), R848 (= R845)
- binding manganese (ii) ion: E299 (= E304), N301 (= N306), Q829 (= Q826), E841 (= E838), E841 (= E838), N843 (= N840)
- binding L-ornithine: E783 (= E780), D791 (= D788), E892 (≠ V891), L907 (= L906), D1041 (≠ F1041), T1042 (= T1042)
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)
48% identity, 98% coverage: 16:1054/1065 of query aligns to 10:1054/1073 of P00968
- R129 (= R135) binding ATP
- R169 (= R175) binding ATP
- G175 (= G181) binding ATP
- G176 (= G182) binding ATP
- E208 (≠ K214) binding ATP
- L210 (≠ V216) binding ATP
- E215 (= E221) binding ATP
- G241 (= G247) binding ATP
- I242 (≠ V248) binding ATP
- H243 (= H249) binding ATP
- Q285 (= Q290) binding ATP; binding Mn(2+)
- E299 (= E304) binding ATP; binding Mn(2+); binding Mn(2+)
- N301 (= N306) binding Mn(2+)
- R715 (= R713) binding ATP
- H754 (≠ Q752) binding ATP
- L756 (= L754) binding ATP
- E761 (= E758) binding ATP
- G786 (= G783) binding ATP
- V787 (= V784) binding ATP
- H788 (= H785) binding ATP
- S789 (= S786) binding ATP
- Q829 (= Q826) binding ATP; binding Mn(2+)
- E841 (= E838) binding ATP; binding Mn(2+); binding Mn(2+)
- N843 (= N840) binding Mn(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
47% identity, 98% coverage: 16:1054/1065 of query aligns to 10:1039/1058 of 1t36A
- active site: R129 (= R135), R169 (= R175), M174 (≠ L180), G176 (= G182), K202 (≠ D208), E215 (= E221), H243 (= H249), N283 (= N288), Q285 (= Q290), E299 (= E304), N301 (= N306), R303 (= R308), S307 (= S312), D338 (≠ A343), G507 (≠ Q506), K634 (≠ Q632), R715 (= R713), E746 (= E758), D754 (= D766), Q814 (= Q826), E826 (= E838), N828 (= N840), R833 (= R845), P886 (≠ H900)
- binding adenosine-5'-diphosphate: R129 (= R135), I167 (= I173), R169 (= R175), M174 (≠ L180), G175 (= G181), G176 (= G182), E208 (≠ K214), L210 (≠ V216), I211 (≠ A217), E215 (= E221), M240 (≠ V246), G241 (= G247), I242 (≠ V248), H243 (= H249), Q285 (= Q290), I298 (= I303), E299 (= E304), T376 (= T380), R715 (= R713), M718 (= M723), F740 (≠ Y753), L741 (= L754), E746 (= E758), A770 (= A782), G771 (= G783), V772 (= V784), H773 (= H785), E826 (= E838), P894 (= P908)
- binding manganese (ii) ion: Q285 (= Q290), E299 (= E304), E299 (= E304), N301 (= N306), Q814 (= Q826), E826 (= E838)
- binding L-ornithine: E768 (= E780), D776 (= D788), E877 (≠ V891), L892 (= L906), D1026 (≠ F1041), T1027 (= T1042)
- binding phosphate ion: M174 (≠ L180), G175 (= G181), H243 (= H249), E299 (= E304), N301 (= N306), R303 (= R308), R306 (= R311)
- binding uridine-5'-monophosphate: K939 (= K953), T959 (= T973), G961 (= G975), T962 (= T976), K978 (= K992), N1000 (= N1014), T1001 (= T1015), T1002 (= T1016), S1011 (≠ G1026), I1014 (= I1029)
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
47% identity, 98% coverage: 16:1054/1065 of query aligns to 10:1039/1058 of 1c3oA
- active site: R129 (= R135), R169 (= R175), M174 (≠ L180), G176 (= G182), K202 (≠ D208), E215 (= E221), H243 (= H249), N283 (= N288), Q285 (= Q290), E299 (= E304), N301 (= N306), R303 (= R308), S307 (= S312), D338 (≠ A343), G507 (≠ Q506), K634 (≠ Q632), R715 (= R713), E746 (= E758), D754 (= D766), Q814 (= Q826), E826 (= E838), N828 (= N840), R833 (= R845), P886 (≠ H900)
- binding adenosine-5'-diphosphate: R129 (= R135), I167 (= I173), R169 (= R175), M174 (≠ L180), G176 (= G182), L210 (≠ V216), I211 (≠ A217), E215 (= E221), M240 (≠ V246), G241 (= G247), H243 (= H249), T244 (= T250), Q285 (= Q290), I298 (= I303), E299 (= E304), T376 (= T380), R715 (= R713), M718 (= M723), F740 (≠ Y753), L741 (= L754), E746 (= E758), A770 (= A782), G771 (= G783), V772 (= V784), H773 (= H785), S774 (= S786), E826 (= E838)
- binding glutamine: R528 (≠ M527), A537 (≠ E536), T538 (≠ A537), N554 (≠ I553)
- binding manganese (ii) ion: Q285 (= Q290), E299 (= E304), E299 (= E304), N301 (= N306), Q814 (= Q826), E826 (= E838)
- binding L-ornithine: E768 (= E780), D776 (= D788), E877 (≠ V891), L892 (= L906), D1026 (≠ F1041), T1027 (= T1042)
- binding phosphate ion: M174 (≠ L180), G175 (= G181), H243 (= H249), E299 (= E304), N301 (= N306), R303 (= R308), R306 (= R311)
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
47% identity, 98% coverage: 16:1054/1065 of query aligns to 10:1039/1058 of 1ce8A
- active site: R129 (= R135), R169 (= R175), M174 (≠ L180), G176 (= G182), K202 (≠ D208), E215 (= E221), H243 (= H249), N283 (= N288), Q285 (= Q290), E299 (= E304), N301 (= N306), R303 (= R308), S307 (= S312), D338 (≠ A343), G507 (≠ Q506), K634 (≠ Q632), R715 (= R713), E746 (= E758), D754 (= D766), Q814 (= Q826), E826 (= E838), N828 (= N840), R833 (= R845), P886 (≠ H900)
- binding adenosine-5'-diphosphate: R129 (= R135), I167 (= I173), R169 (= R175), M174 (≠ L180), G176 (= G182), L210 (≠ V216), I211 (≠ A217), E215 (= E221), M240 (≠ V246), G241 (= G247), I242 (≠ V248), H243 (= H249), Q285 (= Q290), I298 (= I303), E299 (= E304), T376 (= T380), R715 (= R713), F740 (≠ Y753), L741 (= L754), E746 (= E758), A770 (= A782), G771 (= G783), V772 (= V784), H773 (= H785), S774 (= S786), E826 (= E838)
- binding inosinic acid: S933 (≠ T947), K939 (= K953), T959 (= T973), G961 (= G975), T962 (= T976), K978 (= K992), V979 (≠ L993), I986 (= I1000), N1000 (= N1014), T1001 (= T1015), T1002 (= T1016), D1010 (= D1025), S1011 (≠ G1026), V1013 (≠ A1028)
- binding manganese (ii) ion: M174 (≠ L180), Q285 (= Q290), E299 (= E304), E299 (= E304), N301 (= N306), Q814 (= Q826), E826 (= E838)
- binding L-ornithine: R528 (≠ M527), A537 (≠ E536), T538 (≠ A537), E552 (= E551), N554 (≠ I553), E768 (= E780), D776 (= D788), E877 (≠ V891), L892 (= L906), Y1025 (≠ C1040), D1026 (≠ F1041), T1027 (= T1042)
- binding phosphate ion: M174 (≠ L180), G175 (= G181), H243 (= H249), E299 (= E304), N301 (= N306), R303 (= R308), R306 (= R311)
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
47% identity, 98% coverage: 16:1054/1065 of query aligns to 10:1039/1058 of 1a9xA
- active site: K202 (≠ D208), D338 (≠ A343), G507 (≠ Q506), K634 (≠ Q632), D754 (= D766), P886 (≠ H900)
- binding adenosine-5'-diphosphate: R129 (= R135), I167 (= I173), R169 (= R175), M174 (≠ L180), G175 (= G181), G176 (= G182), L210 (≠ V216), E215 (= E221), M240 (≠ V246), G241 (= G247), I242 (≠ V248), H243 (= H249), T244 (= T250), Q285 (= Q290), I298 (= I303), E299 (= E304), T376 (= T380), R715 (= R713), M718 (= M723), F740 (≠ Y753), L741 (= L754), E746 (= E758), A770 (= A782), G771 (= G783), V772 (= V784), H773 (= H785), E826 (= E838)
- binding manganese (ii) ion: Q285 (= Q290), E299 (= E304), E299 (= E304), N301 (= N306), Q814 (= Q826), E826 (= E838)
- binding L-ornithine: E768 (= E780), D776 (= D788), E877 (≠ V891), L892 (= L906), Y1025 (≠ C1040), D1026 (≠ F1041), T1027 (= T1042)
- binding phosphate ion: G175 (= G181), H243 (= H249), E299 (= E304), N301 (= N306), R303 (= R308), R306 (= R311)
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
42% identity, 97% coverage: 14:1044/1065 of query aligns to 423:1467/1500 of P07756
- S537 (= S125) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S912) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T913) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T973) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T976) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ K992) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N1014) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ T1017) 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)
42% identity, 97% coverage: 14:1044/1065 of query aligns to 423:1467/1500 of Q8C196
- K1291 (≠ L874) 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
P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
42% identity, 97% coverage: 14:1044/1065 of query aligns to 423:1467/1500 of P31327
- A438 (= A29) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- K453 (≠ Q44) modified: N6-glutaryllysine; alternate
- K458 (≠ E49) modified: N6-glutaryllysine; alternate
- K527 (≠ Q115) modified: N6-glutaryllysine; alternate
- G530 (= G118) to V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
- K532 (≠ Q120) modified: N6-glutaryllysine; alternate
- T544 (≠ A132) 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 (≠ L141) modified: N6-glutaryllysine; alternate
- Q678 (= Q268) to P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- K728 (= K318) modified: N6-glutaryllysine
- K757 (= K347) modified: N6-glutaryllysine; alternate
- K772 (= K362) modified: N6-glutaryllysine; alternate
- P774 (= P364) to L: in CPS1D; the enzyme is inactive
- K793 (= K383) modified: N6-glutaryllysine; alternate
- K811 (= K401) modified: N6-glutaryllysine; alternate
- K841 (≠ E428) modified: N6-glutaryllysine; alternate
- L843 (≠ C430) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (≠ L437) 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 (≠ E443) modified: N6-glutaryllysine; alternate
- K869 (= K456) modified: N6-glutaryllysine
- T871 (≠ S458) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (≠ P462) 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 (≠ E476) modified: N6-glutaryllysine; alternate
- K892 (≠ Q479) 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 (≠ A497) 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 (≠ R503) modified: N6-glutaryllysine; alternate
- R932 (= R516) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (≠ L521) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (≠ G533) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (≠ F542) 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 (≠ Q548) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I570) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G571) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ N658) modified: N6-glutaryllysine; alternate
- K1150 (≠ N734) modified: N6-glutaryllysine
- K1168 (≠ Q752) modified: N6-glutaryllysine; alternate
- K1183 (≠ D766) modified: N6-glutaryllysine; alternate
- I1215 (≠ L798) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (≠ T807) modified: N6-glutaryllysine
- I1254 (= I837) to F: in CPS1D; uncertain significance
- F1266 (= F849) to S: in dbSNP:rs1047886
- M1283 (≠ I866) to L: in dbSNP:rs1047887
- K1356 (≠ N937) modified: N6-glutaryllysine; alternate
- K1360 (≠ H941) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ LVTL 945:948) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ P958) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (≠ V960) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (≠ F963) to S: in CPS1D; significant loss of protein stability
- T1406 (≠ A988) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ L993) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (≠ K1020) 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 (= R1030) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
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
- 1479 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
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, 98% coverage: 15:1054/1065 of query aligns to 476:1517/2244 of Q09794
- S1119 (≠ G663) 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: 15:1054/1065 of query aligns to 440:1485/2214 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)
42% identity, 98% coverage: 11:1054/1065 of query aligns to 402:1449/2225 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)
41% identity, 97% coverage: 14:1044/1065 of query aligns to 381:1408/1430 of 5douD
- active site: R505 (= R135), R545 (= R175), N576 (≠ D208), E589 (= E221), H617 (= H249), N656 (= N288), Q658 (= Q290), E672 (= E304), N674 (= N306), R676 (= R308), S680 (= S312), G880 (≠ Q506), A1006 (≠ Q632), R1087 (= R713), E1116 (= E758), K1124 (≠ D766), Q1184 (= Q826), E1196 (= E838), N1198 (= N840), R1203 (= R845), R1260 (≠ H900)
- binding adenosine-5'-diphosphate: R505 (= R135), M543 (≠ I173), R545 (= R175), L550 (= L180), G551 (= G181), G552 (= G182), E581 (= E213), S583 (= S215), V584 (= V216), T585 (≠ A217), E589 (= E221), M614 (≠ V246), G615 (= G247), V616 (= V248), H617 (= H249), Q658 (= Q290), I671 (= I303), E672 (= E304), L1085 (≠ M711), F1110 (≠ Y753), V1111 (≠ L754), E1116 (= E758), A1140 (= A782), V1142 (= V784), H1143 (= H785), S1144 (= S786), Q1184 (= Q826), L1186 (≠ V828), I1195 (= I837), E1196 (= E838)
- binding magnesium ion: Q658 (= Q290), E672 (= E304), E672 (= E304), N674 (= N306)
- binding n-acetyl-l-glutamate: I1307 (≠ L948), Q1308 (≠ A949), T1332 (= T973), A1334 (≠ G975), T1335 (= T976), W1351 (≠ K992), L1379 (≠ T1015), T1384 (≠ K1020), K1385 (= K1021), F1386 (≠ Q1022), N1390 (≠ G1026)
- binding phosphate ion: L550 (= L180), G551 (= G181), H617 (= H249), E672 (= E304), N674 (= N306), R676 (= R308), R679 (= R311)
Sites not aligning to the query:
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, 97% coverage: 15:1044/1065 of query aligns to 405:1445/2224 of P05990
- E1167 (= E777) 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
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)
41% identity, 98% coverage: 15:1060/1065 of query aligns to 395:1446/2225 of P08955
- S1406 (vs. gap) modified: Phosphoserine; by PKA; mutation to A: No effect on enzyme kinetics.; mutation to D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.
P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
42% identity, 98% coverage: 15:1060/1065 of query aligns to 395:1446/2225 of P27708
- T456 (= T76) modified: Phosphothreonine; by MAPK1
- Y735 (= Y358) 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
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)
42% identity, 98% coverage: 9:1054/1065 of query aligns to 386:1452/2198 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.
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
40% identity, 99% coverage: 14:1065/1065 of query aligns to 378:1418/1422 of 6w2jA
- active site: Q651 (= Q290), E665 (= E304), N667 (= N306), S673 (= S312), G869 (≠ Q506), A995 (≠ Q632), K1113 (≠ D766), R1249 (≠ H900)
- 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 (= D244), M607 (≠ V246), V615 (≠ M254), P725 (= P364), R726 (= R365), W727 (= W366), D730 (= D369), F732 (= F371), F756 (≠ L399), L760 (≠ V403), C763 (≠ L406), H764 (≠ E407), S795 (≠ D435), R797 (≠ L437), I798 (≠ L438)
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, 98% coverage: 14:1054/1065 of query aligns to 29:1084/1118 of P03965
- L229 (≠ V216) mutation to G: Abolishes ammonia-dependent ATPase activity.
- H262 (= H249) mutation to N: No effect.
- D265 (= D252) mutation D->A,E,N: Reduces ammonia-dependent ATPase activity 17-58 fold.
- I316 (= I303) mutation I->G,S,H: Reduces ammonia-dependent ATPase activity 17-64 fold.
- H807 (= H785) mutation to N: No effect.
- D810 (= D788) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
Query Sequence
>WP_015944958.1 NCBI__GCF_000021925.1:WP_015944958.1
MNAENGNRNTKKWNKVLVIGSGPIVIGQAAEFDYAGTQACRALQEEGVEVVLVNSNPATI
MTDQEVADRIYIEPLTVEFLERIIERERPDGIIATMGGQTGLNLAFQLAEKGILQRCGVQ
LMGTSLDSITKAEDREHFRSLMRELGEPVPPSVIVSDLEEALSFGEEIGYPVIVRPAYTL
GGTGGGIAHNREQLKEIAKSGLQASLIDQILVEKSVAGWKEIEYEVLRDSQGNCITICNM
ENMDPVGVHTGDSMVVAPCQTLTDREVQALRTSSRKIVAALGIEGGCNVQYALHPERLEY
VVIEVNPRLSRSSALASKATGYPIAKVAAKIALGYTLPELTNAVTGKTSACFEPALDYVV
VKIPRWPFDKFSDADRRLGTQMKATGEVMGLGRNLETALQKAVRSLEIKAFGLLLPEFQE
LTDEEILERCQKPDDQLLFILAEGLRRGLSLEQIQKASSWNPYFLTAIERIVRMSETLQF
SPWNGELLLKAKRMGFADRELARLWQTTEKEIYAYRQEKGLQPVFKMVDTCAGEFEALTP
YFYSSYDQEDEGIPTQRRKVVVLGSGPIRIGQGIEFDYCSVHSVLALKKAGVETIIINNN
PETVSTDFDTADRLYFEPLTLEDVSAVLEREQPEGVIVQFGGQTAIGLAKPLAERGYNIL
GTGIEDIDRAEERGQFDEVLHTIGAKRPKGGQASSLAEAVEVAARIGYPLMIRPSFVLGG
RAMEIVYSASELENVVNRAMADFPGQELWMDQYLVGKEVEVDAISDGKNVSLPGIMEHLE
RAGVHSGDSIAVYPPQTLSEPLIQRITLLTTEIARALNVIGLLNIQYVIFQDEVYVIEVN
PRSSRTVPFISKVTGLSIVDYATEVILGKTLTELELPLGLWPLPERVAVKVPVFSFSKLH
RVEPSLGPEMKSTGEVMGVDRTYEKALYKALLAGGFNMSAHGSLLVTLADRDKAEGIPLV
KKFADLGFRILATEGTAKTLREEGIQVAPVAKLHQGSTEITDAIRQGVIQCVLNTTTHNK
KQESDGFAIRRTAVEQGIPCFTSLDTASAWVHVLMSFLPSLMSLK
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