SitesBLAST
Comparing WP_011606327.1 NCBI__GCF_000058485.1:WP_011606327.1 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)
52% identity, 86% coverage: 3:1081/1261 of query aligns to 94:1176/1187 of Q42601
- P149 (= P58) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
- G587 (= G486) mutation to E: In ven3-3; reticulate leaf phenotype.
- A844 (= A734) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P917) 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, 86% coverage: 1:1086/1261 of query aligns to 1:1073/1073 of 1bxrA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ T202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G497), K634 (≠ Q623), R715 (= R708), G721 (= G714), G722 (= G715), S745 (= S738), E761 (= E754), D769 (= D762), Q829 (= Q822), E841 (= E834), N843 (= N836), R848 (= R841), P901 (≠ R909)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), E299 (= E299), R306 (= R306), T376 (= T375), R675 (= R668), V713 (≠ L706), R715 (= R708), L720 (= L713), G721 (= G714), G722 (= G715), M725 (= M718), D753 (= D746), F755 (= F748), L756 (= L749), E761 (= E754), A785 (= A778), G786 (= G779), V787 (= V780), H788 (= H781), Q829 (= Q822), E841 (= E834), N843 (= N836), R848 (= R841)
- binding manganese (ii) ion: E299 (= E299), N301 (= N301), Q829 (= Q822), E841 (= E834), E841 (= E834), N843 (= N836)
- binding L-ornithine: E783 (= E776), D791 (= D784), E892 (= E895), L907 (= L915), D1041 (≠ I1052), T1042 (= T1053)
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, 86% coverage: 1:1086/1261 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 (= 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 (= R708) binding ATP
- H754 (≠ R747) binding ATP
- L756 (= L749) binding ATP
- E761 (= E754) binding ATP
- G786 (= G779) binding ATP
- V787 (= V780) binding ATP
- H788 (= H781) binding ATP
- S789 (= S782) binding ATP
- Q829 (= Q822) binding ATP; binding Mn(2+)
- E841 (= E834) binding ATP; binding Mn(2+); binding Mn(2+)
- N843 (= N836) binding Mn(2+)
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
52% identity, 86% coverage: 1:1086/1261 of query aligns to 1:1058/1058 of 1t36A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ T202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G497), K634 (≠ Q623), R715 (= R708), E746 (= E754), D754 (= D762), Q814 (= Q822), E826 (= E834), N828 (= N836), R833 (= R841), P886 (≠ R909)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), E208 (= E208), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R708), M718 (= M718), F740 (= F748), L741 (= L749), E746 (= E754), A770 (= A778), G771 (= G779), V772 (= V780), H773 (= H781), E826 (= E834), P894 (= P917)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q822), E826 (= E834)
- binding L-ornithine: E768 (= E776), D776 (= D784), E877 (= E895), L892 (= L915), D1026 (≠ I1052), T1027 (= T1053)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
- binding uridine-5'-monophosphate: K939 (= K962), T959 (= T982), G961 (= G984), T962 (= T985), K978 (= K1001), N1000 (= N1026), T1001 (= T1027), T1002 (≠ P1028), S1011 (≠ G1037), I1014 (= I1040)
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
52% identity, 86% coverage: 1:1086/1261 of query aligns to 1:1058/1058 of 1c3oA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ T202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G497), K634 (≠ Q623), R715 (= R708), E746 (= E754), D754 (= D762), Q814 (= Q822), E826 (= E834), N828 (= N836), R833 (= R841), P886 (≠ R909)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R708), M718 (= M718), F740 (= F748), L741 (= L749), E746 (= E754), A770 (= A778), G771 (= G779), V772 (= V780), H773 (= H781), S774 (= S782), E826 (= E834)
- binding glutamine: R528 (≠ T518), A537 (= A527), T538 (≠ S528), N554 (≠ A544)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q822), E826 (= E834)
- binding L-ornithine: E768 (= E776), D776 (= D784), E877 (= E895), L892 (= L915), D1026 (≠ I1052), T1027 (= T1053)
- binding phosphate ion: M174 (≠ L174), 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, 86% coverage: 1:1086/1261 of query aligns to 1:1058/1058 of 1ce8A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ T202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G497), K634 (≠ Q623), R715 (= R708), E746 (= E754), D754 (= D762), Q814 (= Q822), E826 (= E834), N828 (= N836), R833 (= R841), P886 (≠ R909)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ I210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R708), F740 (= F748), L741 (= L749), E746 (= E754), A770 (= A778), G771 (= G779), V772 (= V780), H773 (= H781), S774 (= S782), E826 (= E834)
- binding inosinic acid: S933 (= S956), K939 (= K962), T959 (= T982), G961 (= G984), T962 (= T985), K978 (= K1001), V979 (≠ H1002), I986 (≠ C1012), N1000 (= N1026), T1001 (= T1027), T1002 (≠ P1028), D1010 (= D1036), S1011 (≠ G1037), V1013 (≠ E1039)
- binding manganese (ii) ion: M174 (≠ L174), Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q822), E826 (= E834)
- binding L-ornithine: R528 (≠ T518), A537 (= A527), T538 (≠ S528), E552 (= E542), N554 (≠ A544), E768 (= E776), D776 (= D784), E877 (= E895), L892 (= L915), Y1025 (≠ C1051), D1026 (≠ I1052), T1027 (= T1053)
- binding phosphate ion: M174 (≠ L174), 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, 86% coverage: 1:1086/1261 of query aligns to 1:1058/1058 of 1a9xA
- active site: K202 (≠ T202), D338 (= D338), G507 (= G497), K634 (≠ Q623), D754 (= D762), P886 (≠ R909)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (≠ I210), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T375), R715 (= R708), M718 (= M718), F740 (= F748), L741 (= L749), E746 (= E754), A770 (= A778), G771 (= G779), V772 (= V780), H773 (= H781), E826 (= E834)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q822), E826 (= E834)
- binding L-ornithine: E768 (= E776), D776 (= D784), E877 (= E895), L892 (= L915), Y1025 (≠ C1051), D1026 (≠ I1052), T1027 (= T1053)
- 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)
39% identity, 84% coverage: 6:1065/1261 of query aligns to 473:1517/2244 of Q09794
- S1119 (≠ A658) 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)
39% identity, 86% coverage: 4:1085/1261 of query aligns to 435:1505/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
39% identity, 84% coverage: 4:1066/1261 of query aligns to 419:1478/1500 of Q8C196
- K1291 (≠ L870) 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
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)
40% identity, 85% coverage: 5:1077/1261 of query aligns to 388:1459/2198 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.
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
39% identity, 84% coverage: 4:1066/1261 of query aligns to 419:1478/1500 of P07756
- S537 (≠ N119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S921) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T922) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T982) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T985) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ L999) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N1026) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ W1029) 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)
39% identity, 84% coverage: 4:1066/1261 of query aligns to 419:1478/1500 of P31327
- A438 (= A23) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- K453 (≠ R38) modified: N6-glutaryllysine; alternate
- K458 (≠ R43) 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 (≠ R114) 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 (≠ I135) 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 (≠ T342) 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 (≠ E422) modified: N6-glutaryllysine; alternate
- L843 (≠ T424) 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 (≠ Q437) modified: N6-glutaryllysine; alternate
- K869 (≠ R450) modified: N6-glutaryllysine
- T871 (= T452) 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 (≠ E467) modified: N6-glutaryllysine; alternate
- K892 (≠ A470) modified: N6-glutaryllysine; alternate
- K905 (≠ R480) modified: N6-glutaryllysine
- K908 (= K483) modified: N6-glutaryllysine; alternate
- G911 (= G486) 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 (≠ A488) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- D914 (= D489) 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 (≠ A490) modified: N6-glutaryllysine; alternate
- S918 (≠ A493) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ E494) modified: N6-glutaryllysine; alternate
- R932 (= R507) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (= I512) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (= A524) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (≠ H533) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- Y959 (= Y534) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- Y962 (= Y537) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- G964 (≠ S539) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I561) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G562) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ P653) modified: N6-glutaryllysine; alternate
- K1150 (≠ D729) modified: N6-glutaryllysine
- K1168 (≠ R747) modified: N6-glutaryllysine; alternate
- K1183 (≠ F761) modified: N6-glutaryllysine; alternate
- I1215 (≠ L794) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (≠ R803) modified: N6-glutaryllysine
- I1254 (≠ L833) to F: in CPS1D; uncertain significance
- F1266 (= F845) to S: in dbSNP:rs1047886
- M1283 (= M862) to L: in dbSNP:rs1047887
- K1356 (≠ G946) modified: N6-glutaryllysine; alternate
- K1360 (≠ Y950) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ FVSV 954:957) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ F967) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (≠ I969) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (= L972) to S: in CPS1D; significant loss of protein stability
- T1406 (vs. gap) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ G1000) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (≠ G1032) 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 (= R1041) 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
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)
39% identity, 91% coverage: 8:1154/1261 of query aligns to 394:1538/2225 of P27708
- T456 (= T70) modified: Phosphothreonine; by MAPK1
- Y735 (= Y353) to C: in a colorectal cancer sample; somatic mutation
- S1406 (vs. gap) modified: Phosphoserine; by PKA
- H1471 (= H1082) binding Zn(2+); binding Zn(2+); mutation to A: No zinc-binding and no catalytic activity.; mutation to N: Abolishes dihydroorotase activity.
- H1473 (≠ A1084) binding Zn(2+); mutation to A: No zinc-binding and no catalytic activity.
- R1475 (= R1086) binding (S)-dihydroorotate
- N1505 (≠ S1124) binding (S)-dihydroorotate
- D1512 (= D1131) mutation to N: No change in catalytic activity.
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
- 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)
38% identity, 84% coverage: 7:1068/1261 of query aligns to 404:1452/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
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)
39% identity, 91% coverage: 8:1153/1261 of query aligns to 394:1537/2225 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.
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, 84% coverage: 8:1065/1261 of query aligns to 404:1455/2224 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
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
38% identity, 84% coverage: 4:1066/1261 of query aligns to 377:1419/1430 of 5douD
- active site: R505 (= R129), R545 (= R169), N576 (≠ T202), E589 (= E215), H617 (= H243), N656 (= N283), Q658 (= Q285), E672 (= E299), N674 (= N301), R676 (= R303), S680 (= S307), G880 (= G497), A1006 (≠ P627), R1087 (= R708), E1116 (= E754), K1124 (≠ F761), Q1184 (= Q822), E1196 (= E834), N1198 (= N836), R1203 (= R841), R1260 (= R904)
- binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ V167), R545 (= R169), L550 (= L174), G551 (= G175), G552 (= G176), E581 (= E207), S583 (= S209), V584 (≠ I210), T585 (≠ L211), E589 (= E215), M614 (= M240), G615 (= G241), V616 (= V242), H617 (= H243), Q658 (= Q285), I671 (= I298), E672 (= E299), L1085 (= L706), F1110 (= F748), V1111 (≠ L749), E1116 (= E754), A1140 (= A778), V1142 (= V780), H1143 (= H781), S1144 (= S782), Q1184 (= Q822), L1186 (≠ A824), I1195 (≠ L833), E1196 (= E834)
- binding magnesium ion: Q658 (= Q285), E672 (= E299), E672 (= E299), N674 (= N301)
- binding n-acetyl-l-glutamate: I1307 (≠ V957), Q1308 (≠ A958), T1332 (= T982), A1334 (≠ G984), T1335 (= T985), W1351 (≠ L999), L1379 (≠ T1027), T1384 (≠ G1032), K1385 (≠ P1033), F1386 (≠ R1034), N1390 (≠ G1037)
- binding phosphate ion: L550 (= L174), G551 (= G175), H617 (= H243), E672 (= E299), N674 (= N301), R676 (= R303), R679 (= R306)
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)
40% identity, 79% coverage: 5:995/1261 of query aligns to 26:1010/1118 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 (= 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)
38% identity, 84% coverage: 4:1066/1261 of query aligns to 374:1408/1422 of 6w2jA
- active site: Q651 (= Q285), E665 (= E299), N667 (= N301), S673 (= S307), G869 (= G497), A995 (≠ P627), K1113 (≠ F761), R1249 (= R904)
- 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 (= P359), R726 (= R360), W727 (≠ F361), D730 (≠ E364), F732 (= F366), F756 (≠ L394), L760 (= L398), C763 (≠ M401), H764 (≠ E402), S795 (≠ D429), R797 (= R431), I798 (≠ L432)
Sites not aligning to the query:
Query Sequence
>WP_011606327.1 NCBI__GCF_000058485.1:WP_011606327.1
MPRREDLRSVLVIGSGPIVIGQACEFDYSGTQACRVLRAEGLRVILVNSNPATIMTDPEL
ADATYVEPITPDIVTKIIERERPDAVLATMGGQTALNTAVALHDAGVLDRYGVRLIGANI
DAIRAGEDRQAFKDIVAAVGGETARSAICHTVEECLAAGEEFAYPVVVRPSFTLGGAGSG
FAHDPAELTRMAADGLSASPSTEVLVEESILGWKEFELELMRDRADNVVVVCSIENVDPM
GVHTGDSITVAPAMTLTDREYQTMRDMSIAVMRAVGVDAGGCNIQFAVDPATGRQVVIEM
NPRVSRSSALASKATGFPIAKISAKLALGYTLDEIPNDITRTTPAAFEPTLDYVVVKVPR
FAFEKFPGADPTLTTTMKSVGEAMGVGRSFAEALQKALRSMESAGSVFSFIPPADDAATL
LESTRVPHDGRLRAVQQALLAGADPADVTRVTGIDPWFVDQIVFLNEIAAGVTRTPAGIR
RAKRAGFADAQLAELLGTSEDVVRAFRHRSGIRPVFKTVDTCAAEFASETPYHYSAYDSE
TEVAPSGRPRVIVLGSGPNRIGQGIEFDYACCHAVMALSDAGFETVMVNCNPETVSTDYD
TADRLYVEPLTVEDVLEVVHAEQQAGPLAGVIVQLGGQTPLGIAAALAEAGVPIVGTAPA
AIHLAEDRGLFGRVLADAGLPSPPHGVATSFPEARAVAERIGYPVLVRPSYVLGGRGMEI
VYDDSMLRDYIERATAISPEHPVLVDRFLDDAVEIDVDALFDGETLYLAGVMEHIEEAGV
HSGDSACALPPITLGHADLERIRTSTEAIARGVGVRGLLNVQYALQSDVLYVLEANPRAS
RTVPFVSKATAVPLAKAAARVMLGATVDELRAEGLLPRTGDGATLPLDSHIAVKEAVLPF
GRFRDAVGRGVDTILGPEMKSTGEVMGIDDGFGTAYAKSQAAAYNGLPTYGRVFVSVANR
DKRAMIFPIKRLADLGFVVYATEGTAQVLRRNGVKAVVLGKHRAPTEGLLDCVEMITSGQ
IDLVINTPWGVGPRLDGYEIRTACVSAGVPCITTIQGAAACVQGVEALVRGELGVRPLQE
YHAALREAWGGAAASDTSDTSDALGADPAPFTAAPSPESTDVPSTDAPSTDAPSTDVPST
ELTEAASAEFTGADPGVPFDEQPFEDVEDDQSEDEDFEDEDFEDQPTERLDGLLPGPFED
QPTEHIEELPAGPVTGGAGPDPSTGPDPSTGPPASTRSDASAGPGAVAGLDAGLDPARTV
R
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