SitesBLAST
Comparing WP_010936889.1 NCBI__GCF_000011905.1:WP_010936889.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
40% identity, 90% coverage: 24:321/331 of query aligns to 2:284/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 90% coverage: 24:321/331 of query aligns to 2:284/290 of 3r7lA
- active site: R49 (= R76), T50 (= T77), K77 (= K104), R99 (= R126), H127 (= H154), Q130 (= Q157), L210 (= L245), P249 (= P286), G277 (= G314)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S74), T48 (= T75), R49 (= R76), T50 (= T77), S74 (= S101), K77 (= K104), R99 (= R126), H127 (= H154), R160 (= R187), R211 (= R246), Q213 (= Q248), A250 (≠ G287)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 90% coverage: 24:321/331 of query aligns to 2:284/291 of 3r7fA
- active site: R49 (= R76), T50 (= T77), K77 (= K104), R99 (= R126), H127 (= H154), Q130 (= Q157), L210 (= L245), P249 (= P286), G277 (= G314)
- binding phosphoric acid mono(formamide)ester: S47 (= S74), T48 (= T75), R49 (= R76), T50 (= T77), R99 (= R126), H127 (= H154), Q130 (= Q157), P249 (= P286), A250 (≠ G287)
- binding phosphate ion: S11 (= S33), T12 (≠ R34), Q23 (≠ G45), K26 (≠ R53), E140 (≠ R167), R171 (≠ K198), K241 (= K278), H243 (≠ D280), K272 (≠ E309), K272 (≠ E309), K275 (= K312)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 90% coverage: 24:321/331 of query aligns to 2:284/291 of 3r7dA
- active site: R49 (= R76), T50 (= T77), K77 (= K104), R99 (= R126), H127 (= H154), Q130 (= Q157), L210 (= L245), P249 (= P286), G277 (= G314)
- binding phosphate ion: S11 (= S33), T12 (≠ R34), T73 (≠ S100), S74 (= S101), K77 (= K104), R171 (≠ K198)
4bjhB Crystal structure of the aquifex reactor complex formed by dihydroorotase (h180a, h232a) with dihydroorotate and aspartate transcarbamoylase with n-(phosphonacetyl)-l-aspartate (pala) (see paper)
41% identity, 88% coverage: 31:322/331 of query aligns to 9:286/291 of 4bjhB
- active site: R47 (= R76), T48 (= T77), K75 (= K104), R97 (= R126), H126 (= H154), Q129 (= Q157)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S74), T46 (= T75), R47 (= R76), T48 (= T77), R97 (= R126), H126 (= H154), R159 (= R187), V160 (= V188), R213 (= R246), Q215 (= Q248), G251 (= G287)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
41% identity, 88% coverage: 31:322/331 of query aligns to 9:286/291 of 3d6nB
- active site: R47 (= R76), T48 (= T77), K75 (= K104), R97 (= R126), H126 (= H154), Q129 (= Q157)
- binding citrate anion: T48 (= T77), R97 (= R126), H126 (= H154), R159 (= R187), V160 (= V188), R213 (= R246), G251 (= G287)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
38% identity, 90% coverage: 25:321/331 of query aligns to 3:287/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S74), T49 (= T75), R50 (= R76), T51 (= T77), S75 (= S101), K78 (= K104), R100 (= R126), H127 (= H154), R160 (= R187), R210 (= R246), Q212 (= Q248), A253 (≠ G287)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
38% identity, 93% coverage: 21:327/331 of query aligns to 2:305/307 of 1ml4A
- active site: R56 (= R76), T57 (= T77), K85 (= K104), R106 (= R126), H134 (= H154), Q137 (= Q157), T227 (≠ L245), P266 (= P286), G292 (= G314)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S74), T55 (= T75), R56 (= R76), T57 (= T77), R106 (= R126), H134 (= H154), R167 (= R187), T168 (≠ V188), R228 (= R246), L267 (≠ G287)
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
38% identity, 90% coverage: 24:322/331 of query aligns to 3:285/292 of 5g1pA
- active site: R54 (= R76), T55 (= T77), K82 (= K104), R103 (= R126), H131 (= H154), Q134 (= Q157), T223 (≠ L245), P251 (= P286), G277 (= G314)
- binding phosphoric acid mono(formamide)ester: S52 (= S74), T53 (= T75), R54 (= R76), T55 (= T77), R103 (= R126), Q134 (= Q157), M252 (≠ G287)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
37% identity, 90% coverage: 24:322/331 of query aligns to 6:300/307 of 5g1nE
- active site: R57 (= R76), T58 (= T77), K85 (= K104), R106 (= R126), H134 (= H154), Q137 (= Q157), T227 (≠ L245), P266 (= P286), G292 (= G314)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S74), T56 (= T75), R57 (= R76), T58 (= T77), S82 (= S101), K85 (= K104), R106 (= R126), H134 (= H154), R167 (= R187), R228 (= R246), Q230 (= Q248), M267 (≠ G287)
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)
37% identity, 95% coverage: 10:322/331 of query aligns to 1913:2218/2225 of P08955
Sites not aligning to the query:
- 1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.
P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
37% identity, 95% coverage: 10:322/331 of query aligns to 1913:2218/2225 of P27708
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
- 177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
- 456 modified: Phosphothreonine; by MAPK1
- 735 Y → C: in a colorectal cancer sample; somatic mutation
- 1406 modified: Phosphoserine; by PKA
- 1471 binding Zn(2+); binding Zn(2+); H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding Zn(2+); H→A: No zinc-binding and no catalytic activity.
- 1475 binding (S)-dihydroorotate
- 1505 binding (S)-dihydroorotate
- 1512 D→N: No change in catalytic activity.
- 1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
- 1562 T→A: Abolishes dihydroorotase activity.
- 1563 F→A: Abolishes dihydroorotase activity.
- 1590 binding Zn(2+); H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding Zn(2+); C→S: Reduces dihydroorotase activity.
- 1614 binding Zn(2+); H→A: Abolishes dihydroorotase activity.
- 1637 binding Zn(2+); E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding (S)-dihydroorotate
- 1686 binding Zn(2+); D→N: Abolishes dihydroorotase activity.
- 1690 binding (S)-dihydroorotate; H→N: 3% of wild-type catalytic activity.
- 1702 binding (S)-dihydroorotate
- 1789:2225 natural variant: Missing (in DEE50; uncertain significance)
- 1859 modified: Phosphoserine; by RPS6KB1 and PKA
- 1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
- 1900 modified: Phosphoserine
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
34% identity, 95% coverage: 12:324/331 of query aligns to 4:313/316 of 8bplA
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)
36% identity, 92% coverage: 24:328/331 of query aligns to 1923:2223/2225 of P20054