SitesBLAST
Comparing WP_053768059.1 NCBI__GCF_001280255.1:WP_053768059.1 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)
56% identity, 93% coverage: 4:965/1030 of query aligns to 95:1076/1187 of Q42601
- P149 (= P58) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
- G587 (= G492) mutation to E: In ven3-3; reticulate leaf phenotype.
- A844 (≠ V736) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P906) mutation to L: In ven3-1; reticulate leaf phenotype.
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
56% identity, 96% coverage: 1:993/1030 of query aligns to 1:1001/1073 of 1bxrA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ H202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G503), K634 (= K629), R715 (= R710), G721 (= G716), G722 (= G717), S745 (≠ L740), E761 (= E757), D769 (= D765), Q829 (= Q825), E841 (= E837), N843 (= N839), R848 (= R844), P901 (= P898)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), E299 (= E299), R306 (= R306), T376 (= T382), R675 (= R670), V713 (≠ L708), R715 (= R710), L720 (= L715), G721 (= G716), G722 (= G717), M725 (= M720), D753 (= D749), F755 (≠ Y751), L756 (= L752), E761 (= E757), A785 (= A781), G786 (= G782), V787 (= V783), H788 (= H784), Q829 (= Q825), E841 (= E837), N843 (= N839), R848 (= R844)
- binding manganese (ii) ion: E299 (= E299), N301 (= N301), Q829 (= Q825), E841 (= E837), E841 (= E837), N843 (= N839)
- binding L-ornithine: E783 (= E779), D791 (= D787), E892 (= E889), L907 (= L904)
Sites not aligning to the query:
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)
56% identity, 96% coverage: 1:993/1030 of query aligns to 1:1001/1073 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 (≠ V210) 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 (= R710) binding ATP
- H754 (≠ R750) binding ATP
- L756 (= L752) binding ATP
- E761 (= E757) binding ATP
- G786 (= G782) binding ATP
- V787 (= V783) binding ATP
- H788 (= H784) binding ATP
- S789 (= S785) binding ATP
- Q829 (= Q825) binding ATP; binding Mn(2+)
- E841 (= E837) binding ATP; binding Mn(2+); binding Mn(2+)
- N843 (= N839) binding Mn(2+)
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
55% identity, 96% coverage: 1:993/1030 of query aligns to 1:986/1058 of 1t36A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ H202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G503), K634 (= K629), R715 (= R710), E746 (= E757), D754 (= D765), Q814 (= Q825), E826 (= E837), N828 (= N839), R833 (= R844), P886 (= P898)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), E208 (= E208), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T382), R715 (= R710), M718 (= M720), F740 (≠ Y751), L741 (= L752), E746 (= E757), A770 (= A781), G771 (= G782), V772 (= V783), H773 (= H784), E826 (= E837), P894 (= P906)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q825), E826 (= E837)
- binding L-ornithine: E768 (= E779), D776 (= D787), E877 (= E889), L892 (= L904)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
- binding uridine-5'-monophosphate: K939 (≠ G948), T959 (≠ S966), G961 (= G968), T962 (≠ E969), K978 (≠ A985)
Sites not aligning to the query:
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
55% identity, 96% coverage: 1:993/1030 of query aligns to 1:986/1058 of 1c3oA
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ H202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G503), K634 (= K629), R715 (= R710), E746 (= E757), D754 (= D765), Q814 (= Q825), E826 (= E837), N828 (= N839), R833 (= R844), P886 (= P898)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T382), R715 (= R710), M718 (= M720), F740 (≠ Y751), L741 (= L752), E746 (= E757), A770 (= A781), G771 (= G782), V772 (= V783), H773 (= H784), S774 (= S785), E826 (= E837)
- binding glutamine: R528 (≠ T524), A537 (≠ E533), T538 (≠ A534), N554 (≠ W550)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q825), E826 (= E837)
- binding L-ornithine: E768 (= E779), D776 (= D787), E877 (= E889), L892 (= L904)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
Sites not aligning to the query:
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
55% identity, 96% coverage: 1:993/1030 of query aligns to 1:986/1058 of 1ce8A
- active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ H202), E215 (= E215), H243 (= H243), N283 (= N283), Q285 (= Q285), E299 (= E299), N301 (= N301), R303 (= R303), S307 (= S307), D338 (= D338), G507 (= G503), K634 (= K629), R715 (= R710), E746 (= E757), D754 (= D765), Q814 (= Q825), E826 (= E837), N828 (= N839), R833 (= R844), P886 (= P898)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ V210), I211 (≠ L211), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T382), R715 (= R710), F740 (≠ Y751), L741 (= L752), E746 (= E757), A770 (= A781), G771 (= G782), V772 (= V783), H773 (= H784), S774 (= S785), E826 (= E837)
- binding inosinic acid: S933 (≠ I945), K939 (≠ G948), T959 (≠ S966), G961 (= G968), T962 (≠ E969), K978 (≠ A985), V979 (= V986), I986 (= I993)
- binding manganese (ii) ion: M174 (≠ L174), Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q825), E826 (= E837)
- binding L-ornithine: R528 (≠ T524), A537 (≠ E533), T538 (≠ A534), E552 (= E548), N554 (≠ W550), E768 (= E779), D776 (= D787), E877 (= E889), L892 (= L904)
- binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
Sites not aligning to the query:
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
55% identity, 96% coverage: 1:993/1030 of query aligns to 1:986/1058 of 1a9xA
- active site: K202 (≠ H202), D338 (= D338), G507 (= G503), K634 (= K629), D754 (= D765), P886 (= P898)
- binding adenosine-5'-diphosphate: R129 (= R129), I167 (≠ V167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (≠ V210), E215 (= E215), M240 (= M240), G241 (= G241), I242 (≠ V242), H243 (= H243), T244 (= T244), Q285 (= Q285), I298 (= I298), E299 (= E299), T376 (= T382), R715 (= R710), M718 (= M720), F740 (≠ Y751), L741 (= L752), E746 (= E757), A770 (= A781), G771 (= G782), V772 (= V783), H773 (= H784), E826 (= E837)
- binding manganese (ii) ion: Q285 (= Q285), E299 (= E299), E299 (= E299), N301 (= N301), Q814 (= Q825), E826 (= E837)
- binding L-ornithine: E768 (= E779), D776 (= D787), E877 (= E889), L892 (= L904)
- binding phosphate ion: G175 (= G175), H243 (= H243), E299 (= E299), N301 (= N301), R303 (= R303), R306 (= R306)
Sites not aligning to the query:
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
41% identity, 92% coverage: 4:949/1030 of query aligns to 419:1379/1500 of P07756
- S537 (≠ N119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S910) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T911) modified: carbohydrate, O-linked (GlcNAc) threonine
Sites not aligning to the query:
- 1391 T→V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- 1394 T→A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- 1410 W→K: 60-fold increase in the activation constant of NAG.
- 1437 N→D: 70-fold increase in the activation constant of NAG.
- 1440 N→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)
41% identity, 92% coverage: 4:949/1030 of query aligns to 419:1379/1500 of Q8C196
- K1291 (≠ L873) 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)
41% identity, 92% coverage: 4:949/1030 of query aligns to 419:1379/1500 of P31327
- A438 (= A23) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- K453 (≠ R38) modified: N6-glutaryllysine; alternate
- K458 (≠ E43) modified: N6-glutaryllysine; alternate
- K527 (= K109) modified: N6-glutaryllysine; alternate
- G530 (= G112) to V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
- K532 (≠ E114) modified: N6-glutaryllysine; alternate
- T544 (≠ 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 (≠ A135) 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 (= K385) modified: N6-glutaryllysine; alternate
- K811 (= K403) modified: N6-glutaryllysine; alternate
- K841 (= K425) modified: N6-glutaryllysine; alternate
- L843 (= L427) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (= R433) 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 (≠ E439) modified: N6-glutaryllysine; alternate
- K869 (≠ Q452) modified: N6-glutaryllysine
- T871 (= T454) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (≠ P458) 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 (≠ A472) modified: N6-glutaryllysine; alternate
- K892 (≠ Q475) modified: N6-glutaryllysine; alternate
- K905 (≠ R486) modified: N6-glutaryllysine
- K908 (= K489) modified: N6-glutaryllysine; alternate
- G911 (= G492) 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 (≠ P494) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- D914 (= D495) 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 (≠ A496) modified: N6-glutaryllysine; alternate
- S918 (≠ G499) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ E500) modified: N6-glutaryllysine; alternate
- R932 (= R513) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (≠ V518) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (= A530) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (≠ H539) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- Y959 (= Y540) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- Y962 (= Y543) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- G964 (≠ L545) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I567) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G568) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ R655) modified: N6-glutaryllysine; alternate
- K1150 (≠ R731) modified: N6-glutaryllysine
- K1168 (≠ R750) modified: N6-glutaryllysine; alternate
- K1183 (≠ D765) modified: N6-glutaryllysine; alternate
- I1215 (≠ L797) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (≠ R806) modified: N6-glutaryllysine
- I1254 (≠ L836) to F: in CPS1D; uncertain significance
- F1266 (= F848) to S: in dbSNP:rs1047886
- M1283 (≠ A865) to L: in dbSNP:rs1047887
- K1356 (≠ R935) modified: N6-glutaryllysine; alternate
- K1360 (≠ S939) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (vs. gap) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (= G946) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (≠ G948) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
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
- 1381 L → S: in CPS1D; significant loss of protein stability
- 1406 T → N: probable risk factor for PHN; dbSNP:rs1047891
- 1411 P → L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- 1443 T → 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
- 1453 R → Q: in CPS1D; the enzyme is inactive; R → W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- 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
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)
41% identity, 94% coverage: 3:973/1030 of query aligns to 434:1400/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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, 93% coverage: 3:958/1030 of query aligns to 470:1418/2244 of Q09794
- S1119 (≠ P660) modified: Phosphoserine
Sites not aligning to the query:
- 1881 modified: Phosphoserine
- 1885 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)
40% identity, 94% coverage: 5:972/1030 of query aligns to 402:1367/2225 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)
42% identity, 91% coverage: 8:946/1030 of query aligns to 394:1320/2225 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)
42% identity, 91% coverage: 8:946/1030 of query aligns to 394:1320/2225 of P27708
- T456 (= T70) modified: Phosphothreonine; by MAPK1
- Y735 (= Y353) to C: in a colorectal cancer sample; somatic mutation
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
- 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
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
40% identity, 92% coverage: 4:949/1030 of query aligns to 377:1320/1430 of 5douD
- active site: R505 (= R129), R545 (= R169), N576 (≠ H202), E589 (= E215), H617 (= H243), N656 (= N283), Q658 (= Q285), E672 (= E299), N674 (= N301), R676 (= R303), S680 (= S307), G880 (= G503), A1006 (≠ K629), R1087 (= R710), E1116 (= E757), K1124 (≠ D765), Q1184 (= Q825), E1196 (= E837), N1198 (= N839), R1203 (= R844), R1260 (≠ P898)
- binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ V167), R545 (= R169), L550 (= L174), G551 (= G175), G552 (= G176), E581 (= E207), S583 (= S209), V584 (= V210), T585 (≠ L211), E589 (= E215), M614 (= M240), G615 (= G241), V616 (= V242), H617 (= H243), Q658 (= Q285), I671 (= I298), E672 (= E299), L1085 (= L708), F1110 (≠ Y751), V1111 (≠ L752), E1116 (= E757), A1140 (= A781), V1142 (= V783), H1143 (= H784), S1144 (= S785), Q1184 (= Q825), L1186 (≠ A827), I1195 (≠ L836), E1196 (= E837)
- binding magnesium ion: Q658 (= Q285), E672 (= E299), E672 (= E299), N674 (= N301)
- binding n-acetyl-l-glutamate: I1307 (vs. gap), Q1308 (vs. gap)
- binding phosphate ion: L550 (= L174), G551 (= G175), H617 (= H243), E672 (= E299), N674 (= N301), R676 (= R303), R679 (= R306)
Sites not aligning to the query:
- active site: 252, 335, 337
- binding n-acetyl-l-glutamate: 1332, 1334, 1335, 1351, 1379, 1384, 1385, 1386, 1390
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, 91% coverage: 8:946/1030 of query aligns to 404:1334/2224 of P05990
- E1167 (= E776) 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
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
39% identity, 92% coverage: 4:949/1030 of query aligns to 374:1309/1422 of 6w2jA
- active site: Q651 (= Q285), E665 (= E299), N667 (= N301), S673 (= S307), G869 (= G503), A995 (≠ K629), K1113 (≠ D765), R1249 (≠ P898)
- 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 (≠ L401), L760 (= L405), C763 (≠ L408), H764 (≠ E409), S795 (≠ P431), R797 (= R433), I798 (= I434)
Sites not aligning to the query:
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, 91% coverage: 5:937/1030 of query aligns to 388:1321/2198 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.
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)
41% identity, 90% coverage: 7:928/1030 of query aligns to 28:953/1118 of P03965
- L229 (≠ V210) mutation to G: Abolishes ammonia-dependent ATPase activity.
- H262 (= H243) mutation to N: No effect.
- D265 (= D246) mutation D->A,E,N: Reduces ammonia-dependent ATPase activity 17-58 fold.
- I316 (= I298) mutation I->G,S,H: Reduces ammonia-dependent ATPase activity 17-64 fold.
- H807 (= H784) mutation to N: No effect.
- D810 (= D787) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
Query Sequence
>WP_053768059.1 NCBI__GCF_001280255.1:WP_053768059.1
MPPRRDLRKILIIGSGPITIGQAAEFDYSGTQAVKALRGAGYEAILVNSNPATIMTDPDL
AERTYVEPLTLEALEKVIAKEAPDALLPTLGGQTALNLSMALHEEGILKRYGVELIGANA
EAIKKGEDREAFQKAMRKIGLEVPRGKMVASVEEGLHFAREVGFPVVVRPSFTLGGTGGG
IAKDEGELKEVLARGLALSPVHTALVEESVLGWKEFELEVMRDHADTVVIITSIENVDPM
GVHTGDSITVAPAQTLSDVEYQRMRDAAKAVIREIGVDTGGSNIQFAVDPKTGRQVVIEM
NPRVSRSSALASKATGFPIAKIAALLAVGYRLDELPNDITRKTPASFEPTIDYVVVKIPR
FAFEKFQDLPNTLGGLKDELGTQMKSVGEVMAMGRTFKEALLKALRGLERDVRALAGVKT
EALEKKLYPNPDRIYAVLELLRRGMGVEELHQATRIDPWFLHQMREIVEAEAWLQDHPPR
DREAWRFYKGLGLPDARIGELLGKKEAEVRAERKALGVVPVYKTVDTCAAEFEAYTPYHY
STYELEDEVWPSKKPKVVILGSGPIRIGQGVEFDYATVHAVWALKEAGYETIMVNSNPET
VSTDYDPADRLYFEPLTLEDVLNLVEHEKPLGVIATLGGQTPLKLAQGLEEAGVRLLGTP
FQAIHQAEDREAFHRLCQRLGIPQPEGRVAKSPEEALELAKEVGFPLLARPSYVLGGRAM
RVLRSQEELKRYLEEVYGPLQEKPSILLDRYLEGALELDVDALSDGEEVLIAGVMEHVER
AGVHSGDSATVLPPVHLSQEALEKVRAYTRRLALALGVRGLLNVQYAVLGEEVYILEANP
RASRTVPFVSKAIGVPLAKLAALIAVGKSLKELGVRDLDPVPPYFAVKEVVIPWLKFPGV
IPVLGPEMRSTGESMGLDEDPYLAYYKAQLGAGQRLPLSGRVRFIGEGEGVEALKKAYRE
AGFALSEGEYDLLISLIPHPELRRAVEAGLPFITTEEGALWSLKAILRAREKPLEVRSLQ
EWHGVYNRAQ
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