SitesBLAST
Comparing 350085 FitnessBrowser__Btheta:350085 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)
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)
59% identity, 98% coverage: 5:1061/1075 of query aligns to 404:1452/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
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)
57% identity, 98% coverage: 6:1059/1075 of query aligns to 475:1518/2244 of Q09794
- S1119 (= S667) 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)
57% identity, 99% coverage: 6:1067/1075 of query aligns to 439:1494/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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)
57% identity, 98% coverage: 6:1058/1075 of query aligns to 394:1440/2225 of P27708
- T456 (= T68) modified: Phosphothreonine; by MAPK1
- Y735 (= Y348) 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 ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding ; H→A: No zinc-binding and no catalytic activity.
- 1475 binding
- 1505 binding
- 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 ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding ; C→S: Reduces dihydroorotase activity.
- 1614 binding ; H→A: Abolishes dihydroorotase activity.
- 1637 binding ; E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding
- 1686 binding ; D→N: Abolishes dihydroorotase activity.
- 1690 binding ; H→N: 3% of wild-type catalytic activity.
- 1702 binding
- 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
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)
56% identity, 98% coverage: 6:1058/1075 of query aligns to 404:1455/2224 of P05990
- E1167 (= E782) 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)
56% identity, 98% coverage: 6:1058/1075 of query aligns to 394:1440/2225 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.
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)
55% identity, 98% coverage: 6:1058/1075 of query aligns to 391:1452/2198 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.
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
53% identity, 100% coverage: 5:1074/1075 of query aligns to 422:1494/1500 of P07756
- S537 (≠ P117) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- S1331 (= S914) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T915) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T975) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T978) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (= W994) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N1017) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ K1020) 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)
53% identity, 100% coverage: 5:1074/1075 of query aligns to 422:1494/1500 of Q8C196
- K1291 (≠ P879) 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)
53% identity, 100% coverage: 5:1074/1075 of query aligns to 422:1494/1500 of P31327
- A438 (= A21) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- K453 (= K36) modified: N6-glutaryllysine; alternate
- K458 (≠ E41) modified: N6-glutaryllysine; alternate
- K527 (≠ E107) modified: N6-glutaryllysine; alternate
- G530 (≠ N110) to V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
- K532 (= K112) modified: N6-glutaryllysine; alternate
- T544 (= T124) 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 (= K133) modified: N6-glutaryllysine; alternate
- Q678 (≠ H258) to P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- K728 (= K308) modified: N6-glutaryllysine
- K757 (≠ T337) modified: N6-glutaryllysine; alternate
- K772 (= K352) modified: N6-glutaryllysine; alternate
- P774 (= P354) to L: in CPS1D; the enzyme is inactive
- K793 (= K373) modified: N6-glutaryllysine; alternate
- K811 (= K391) modified: N6-glutaryllysine; alternate
- K841 (= K416) modified: N6-glutaryllysine; alternate
- L843 (= L418) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- R850 (= R425) 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 (= K431) modified: N6-glutaryllysine; alternate
- K869 (≠ E444) modified: N6-glutaryllysine
- T871 (= T446) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K875 (= K450) 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 (≠ E464) modified: N6-glutaryllysine; alternate
- K892 (≠ H467) modified: N6-glutaryllysine; alternate
- K905 (≠ R485) modified: N6-glutaryllysine
- K908 (= K488) modified: N6-glutaryllysine; alternate
- G911 (= G491) to E: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs1388955593; to V: in CPS1D; significant decrease in protein yield and enzyme activity
- S913 (= S493) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- D914 (= D494) to G: in CPS1D; significant decrease in protein yield and enzyme activity; to H: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs765484849
- K915 (≠ F495) modified: N6-glutaryllysine; alternate
- S918 (≠ A498) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- K919 (≠ R499) modified: N6-glutaryllysine; alternate
- R932 (= R518) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- I937 (= I523) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- A949 (= A535) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- L958 (= L544) to P: in CPS1D; significant decrease in protein yield and enzyme activity
- Y959 (= Y545) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- Y962 (= Y548) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- G964 (= G550) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- I986 (= I574) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G575) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ H662) modified: N6-glutaryllysine; alternate
- K1150 (≠ R738) modified: N6-glutaryllysine
- K1168 (≠ Q756) modified: N6-glutaryllysine; alternate
- K1183 (≠ Q771) modified: N6-glutaryllysine; alternate
- I1215 (≠ L803) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (= K812) modified: N6-glutaryllysine
- I1254 (= I842) to F: in CPS1D; uncertain significance
- F1266 (= F854) to S: in dbSNP:rs1047886
- M1283 (= M871) to L: in dbSNP:rs1047887
- K1356 (≠ R939) modified: N6-glutaryllysine; alternate
- K1360 (= K943) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ LLST 946:949) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ D960) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (= A962) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (= L965) to S: in CPS1D; significant loss of protein stability
- T1406 (= T990) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (= P995) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (= T1023) 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 (= R1034) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- K1479 (vs. gap) modified: N6-glutaryllysine; alternate
- K1486 (≠ I1066) modified: N6-glutaryllysine; alternate
- Y1491 (≠ W1071) 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
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)
53% identity, 100% coverage: 3:1074/1075 of query aligns to 26:1112/1118 of P03965
- L229 (= L206) mutation to G: Abolishes ammonia-dependent ATPase activity.
- H262 (= H239) mutation to N: No effect.
- D265 (≠ E242) mutation D->A,E,N: Reduces ammonia-dependent ATPase activity 17-58 fold.
- I316 (= I293) mutation I->G,S,H: Reduces ammonia-dependent ATPase activity 17-64 fold.
- H807 (= H790) mutation to N: No effect.
- D810 (= D793) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
53% identity, 98% coverage: 5:1057/1075 of query aligns to 380:1417/1430 of 5douD
- active site: R505 (= R127), R545 (= R167), N576 (≠ P198), E589 (= E211), H617 (= H239), N656 (= N278), Q658 (= Q280), E672 (= E294), N674 (= N296), R676 (= R298), S680 (= S302), G880 (= G502), A1006 (≠ N636), R1087 (= R717), E1116 (= E763), K1124 (≠ Q771), Q1184 (= Q831), E1196 (= E843), N1198 (= N845), R1203 (= R850), R1260 (≠ Q902)
- binding adenosine-5'-diphosphate: R505 (= R127), M543 (≠ I165), R545 (= R167), L550 (= L172), G551 (= G173), G552 (= G174), E581 (= E203), S583 (= S205), V584 (≠ L206), T585 (≠ R207), E589 (= E211), M614 (≠ L236), G615 (= G237), V616 (≠ I238), H617 (= H239), Q658 (= Q280), I671 (= I293), E672 (= E294), L1085 (= L715), F1110 (= F757), V1111 (≠ I758), E1116 (= E763), A1140 (= A787), V1142 (= V789), H1143 (= H790), S1144 (= S791), Q1184 (= Q831), L1186 (= L833), I1195 (= I842), E1196 (= E843)
- binding magnesium ion: Q658 (= Q280), E672 (= E294), E672 (= E294), N674 (= N296)
- binding n-acetyl-l-glutamate: I1307 (≠ T949), Q1308 (≠ T951), T1332 (= T975), A1334 (≠ G977), T1335 (= T978), W1351 (= W994), L1379 (≠ I1018), T1384 (= T1023), K1385 (≠ A1024), F1386 (≠ G1025), N1390 (= N1029)
- binding phosphate ion: L550 (= L172), G551 (= G173), H617 (= H239), E672 (= E294), N674 (= N296), R676 (= R298), R679 (= R301)
Sites not aligning to the query:
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
53% identity, 98% coverage: 5:1057/1075 of query aligns to 377:1406/1422 of 6w2jA
- active site: Q651 (= Q280), E665 (= E294), N667 (= N296), S673 (= S302), G869 (= G502), A995 (≠ N636), K1113 (≠ Q771), R1249 (≠ Q902)
- 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 (= D234), M607 (≠ L236), V615 (≠ I244), P725 (= P354), R726 (= R355), W727 (= W356), D730 (≠ G359), F732 (= F361), F756 (≠ I389), L760 (= L393), C763 (≠ I396), H764 (≠ G397), S795 (≠ D423), R797 (= R425), I798 (= I426)
Sites not aligning to the query:
6w2jB Cps1 bound to allosteric inhibitor h3b-374 (see paper)
51% identity, 79% coverage: 204:1057/1075 of query aligns to 517:1348/1364 of 6w2jB
- active site: Q593 (= Q280), E607 (= E294), N609 (= N296), S615 (= S302), G811 (= G502), A937 (≠ N636), K1055 (≠ Q771), R1191 (≠ Q902)
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: D547 (= D234), M549 (≠ L236), V557 (≠ I244), R668 (= R355), W669 (= W356), D672 (≠ G359), R673 (≠ K360), F698 (≠ I389), L702 (= L393), C705 (≠ I396), H706 (≠ G397), S737 (≠ D423), R739 (= R425), I740 (= I426)
Sites not aligning to the query:
6uelA Cps1 bound to allosteric inhibitor h3b-193 (see paper)
46% identity, 98% coverage: 5:1057/1075 of query aligns to 374:1321/1333 of 6uelA
- active site: Q587 (≠ E231), E601 (≠ Q280), N603 (= N296), S609 (= S302), G803 (= G502), A929 (≠ N636), K1032 (≠ Q771), R1168 (≠ Q902)
- binding N~1~-[(4-fluorophenyl)methyl]-N~1~-methyl-N~4~-(4-methyl-1,3-thiazol-2-yl)piperidine-1,4-dicarboxamide: D544 (= D187), V551 (≠ F194), R662 (= R355), W663 (= W356), L665 (= L358), F690 (≠ I389), H698 (≠ G397), I701 (≠ M400), S729 (≠ D423), R731 (= R425), I732 (= I426)
Sites not aligning to the query:
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
40% identity, 99% coverage: 2:1063/1075 of query aligns to 4:1062/1073 of 1bxrA
- active site: R129 (= R127), R169 (= R167), M174 (≠ L172), G176 (= G174), K202 (vs. gap), E215 (= E211), H243 (= H239), N283 (= N278), Q285 (= Q280), E299 (= E294), N301 (= N296), R303 (= R298), S307 (= S302), D338 (≠ S333), G507 (= G502), K634 (≠ N636), R715 (= R717), G721 (≠ S723), G722 (= G724), S745 (= S747), E761 (= E763), D769 (≠ Q771), Q829 (= Q831), E841 (= E843), N843 (= N845), R848 (= R850), P901 (≠ Q902)
- binding phosphoaminophosphonic acid-adenylate ester: R129 (= R127), I167 (= I165), R169 (= R167), M174 (≠ L172), G175 (= G173), G176 (= G174), L210 (= L206), I211 (≠ R207), E215 (= E211), M240 (≠ L236), G241 (= G237), H243 (= H239), T244 (= T240), Q285 (= Q280), E299 (= E294), R306 (= R301), T376 (≠ S370), R675 (= R677), V713 (≠ L715), R715 (= R717), L720 (= L722), G721 (≠ S723), G722 (= G724), M725 (= M727), D753 (≠ S755), F755 (= F757), L756 (≠ I758), E761 (= E763), A785 (= A787), G786 (= G788), V787 (= V789), H788 (= H790), Q829 (= Q831), E841 (= E843), N843 (= N845), R848 (= R850)
- binding manganese (ii) ion: E299 (= E294), N301 (= N296), Q829 (= Q831), E841 (= E843), E841 (= E843), N843 (= N845)
- binding L-ornithine: E783 (= E785), D791 (= D793), E892 (≠ A893), L907 (= L908), D1041 (≠ I1045), T1042 (= T1046)
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)
40% identity, 99% coverage: 2:1063/1075 of query aligns to 4:1062/1073 of P00968
- R129 (= R127) binding
- R169 (= R167) binding
- G175 (= G173) binding
- G176 (= G174) binding
- E208 (≠ K204) binding
- L210 (= L206) binding
- E215 (= E211) binding
- G241 (= G237) binding
- I242 (= I238) binding
- H243 (= H239) binding
- Q285 (= Q280) binding ; binding
- E299 (= E294) binding ; binding ; binding
- N301 (= N296) binding
- R715 (= R717) binding
- H754 (≠ Q756) binding
- L756 (≠ I758) binding
- E761 (= E763) binding
- G786 (= G788) binding
- V787 (= V789) binding
- H788 (= H790) binding
- S789 (= S791) binding
- Q829 (= Q831) binding ; binding
- E841 (= E843) binding ; binding ; binding
- N843 (= N845) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
41% identity, 99% coverage: 2:1069/1075 of query aligns to 95:1169/1187 of Q42601
- P149 (≠ E56) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
- G587 (= G491) mutation to E: In ven3-3; reticulate leaf phenotype.
- A844 (= A743) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (≠ V910) mutation to L: In ven3-1; reticulate leaf phenotype.
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
40% identity, 99% coverage: 2:1063/1075 of query aligns to 4:1047/1058 of 1t36A
- active site: R129 (= R127), R169 (= R167), M174 (≠ L172), G176 (= G174), K202 (vs. gap), E215 (= E211), H243 (= H239), N283 (= N278), Q285 (= Q280), E299 (= E294), N301 (= N296), R303 (= R298), S307 (= S302), D338 (≠ S333), G507 (= G502), K634 (≠ N636), R715 (= R717), E746 (= E763), D754 (≠ Q771), Q814 (= Q831), E826 (= E843), N828 (= N845), R833 (= R850), P886 (≠ Q902)
- binding adenosine-5'-diphosphate: R129 (= R127), I167 (= I165), R169 (= R167), M174 (≠ L172), G175 (= G173), G176 (= G174), E208 (≠ K204), L210 (= L206), I211 (≠ R207), E215 (= E211), M240 (≠ L236), G241 (= G237), I242 (= I238), H243 (= H239), Q285 (= Q280), I298 (= I293), E299 (= E294), T376 (≠ S370), R715 (= R717), M718 (= M727), F740 (= F757), L741 (≠ I758), E746 (= E763), A770 (= A787), G771 (= G788), V772 (= V789), H773 (= H790), E826 (= E843), P894 (≠ V910)
- binding manganese (ii) ion: Q285 (= Q280), E299 (= E294), E299 (= E294), N301 (= N296), Q814 (= Q831), E826 (= E843)
- binding L-ornithine: E768 (= E785), D776 (= D793), E877 (≠ A893), L892 (= L908), D1026 (≠ I1045), T1027 (= T1046)
- binding phosphate ion: M174 (≠ L172), G175 (= G173), H243 (= H239), E299 (= E294), N301 (= N296), R303 (= R298), R306 (= R301)
- binding uridine-5'-monophosphate: K939 (= K955), T959 (= T975), G961 (= G977), T962 (= T978), K978 (≠ P995), N1000 (= N1017), T1001 (≠ I1018), T1002 (≠ P1019), S1011 (≠ G1030), I1014 (= I1033)
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
40% identity, 99% coverage: 2:1063/1075 of query aligns to 4:1047/1058 of 1c3oA
- active site: R129 (= R127), R169 (= R167), M174 (≠ L172), G176 (= G174), K202 (vs. gap), E215 (= E211), H243 (= H239), N283 (= N278), Q285 (= Q280), E299 (= E294), N301 (= N296), R303 (= R298), S307 (= S302), D338 (≠ S333), G507 (= G502), K634 (≠ N636), R715 (= R717), E746 (= E763), D754 (≠ Q771), Q814 (= Q831), E826 (= E843), N828 (= N845), R833 (= R850), P886 (≠ Q902)
- binding adenosine-5'-diphosphate: R129 (= R127), I167 (= I165), R169 (= R167), M174 (≠ L172), G176 (= G174), L210 (= L206), I211 (≠ R207), E215 (= E211), M240 (≠ L236), G241 (= G237), H243 (= H239), T244 (= T240), Q285 (= Q280), I298 (= I293), E299 (= E294), T376 (≠ S370), R715 (= R717), M718 (= M727), F740 (= F757), L741 (≠ I758), E746 (= E763), A770 (= A787), G771 (= G788), V772 (= V789), H773 (= H790), S774 (= S791), E826 (= E843)
- binding glutamine: R528 (≠ Q529), A537 (≠ P538), T538 (≠ A539), N554 (≠ H556)
- binding manganese (ii) ion: Q285 (= Q280), E299 (= E294), E299 (= E294), N301 (= N296), Q814 (= Q831), E826 (= E843)
- binding L-ornithine: E768 (= E785), D776 (= D793), E877 (≠ A893), L892 (= L908), D1026 (≠ I1045), T1027 (= T1046)
- binding phosphate ion: M174 (≠ L172), G175 (= G173), H243 (= H239), E299 (= E294), N301 (= N296), R303 (= R298), R306 (= R301)
Query Sequence
>350085 FitnessBrowser__Btheta:350085
MKENIKKVLLLGSGALKIGEAGEFDYSGSQALKALKEEGIETILINPNIATVQTSEGVAD
QIYFLPVTPYFVEKVIQKEKPEGIMLAFGGQTALNCGVALYKEGILEKYNVKVLGTPVQA
IMDTEDRELFVQKLNEINVKTIKSEAVENAEDARRAAKELGYPVIVRAAYALGGLGSGFC
DNEEQLDVLVEKAFSFSPQVLVEKSLRGWKEVEYEVVRDRFDNCITVCNMENFDPLGIHT
GESIVIAPSQTLTNSEYHKLRELAIRIIRHIGIVGECNVQYAFDPESEDYRVIEVNARLS
RSSALASKATGYPLAFVAAKLGLGYGLFDLKNSVTKTTSAFFEPALDYVVCKIPRWDLGK
FHGVDKELGSSMKSVGEVMAIGRTFEEAIQKGLRMIGQGMHGFVENKELVIPDIDKALRE
PTDKRIFVISKAFRAGYTIDQVHELTKIDKWFLQKLMNIMKTSEEMHEWGNNHKQIADLP
VELLRKAKVQGFSDFQIARAIGYEGDMENGSLYVRKYRKAAGILPVVKQIDTLAAEYPAQ
TNYLYLTYSGVANDVHYLGDHKSIVVLGSGAYRIGSSVEFDWCGVQALNTIRKEGWRSVM
INYNPETVSTDYDMCDRLYFDELTFERVMDILELENPHGVIVSTGGQIPNNLALRLDAQN
IHILGTSAQSIDNAEDREKFSAMLDRIGVDQPRWRELTSLEDINEFVDEVGFPVLVRPSY
VLSGAAMNVCSNQEELERFLKLAANVSKKHPVVVSQFIEHAKEVEMDAVAQNGEIIAYAI
SEHIEFAGVHSGDATIQFPPQKLYVETVRRIKRISREIAKALNISGPFNIQYLAKDNDIK
VIECNLRASRSFPFVSKVLKINFIELATKVMLGLPVEKPEKNLFELDYVGIKASQFSFNR
LQKADPVLGVDMASTGEVGCIGSDTSCAVLKAMLSVGYRIPKKNILLSTGTMKQKADMMD
AARMLVNKGYKLFATGGTHKTFAENGIESTLVYWPSEEGHPQALEMLHNKEIDMVVNIPK
NLTAGELDNGYKIRRAAIDLNVPLITNARLASAFINAFCTMTVDDIAIKSWEEYK
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