SitesBLAST
Comparing WP_066551284.1 NCBI__GCF_001636925.1:WP_066551284.1 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)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
42% identity, 90% coverage: 22:316/327 of query aligns to 2:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 90% coverage: 22:316/327 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R74), T50 (= T75), K77 (= K102), R99 (= R124), H127 (= H152), Q130 (= Q155), L210 (= L238), P249 (= P279), G277 (= G308)
- binding phosphoric acid mono(formamide)ester: S47 (= S72), T48 (= T73), R49 (= R74), T50 (= T75), R99 (= R124), H127 (= H152), Q130 (= Q155), P249 (= P279), A250 (≠ G280)
- binding phosphate ion: S11 (≠ D31), T12 (≠ P32), Q23 (≠ D43), K26 (≠ Q51), E140 (≠ R165), R171 (≠ M196), K241 (≠ N271), H243 (≠ C273), K272 (≠ D303), K272 (≠ D303), K275 (≠ E306)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 90% coverage: 22:316/327 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R74), T50 (= T75), K77 (= K102), R99 (= R124), H127 (= H152), Q130 (= Q155), L210 (= L238), P249 (= P279), G277 (= G308)
- binding phosphate ion: S11 (≠ D31), T12 (≠ P32), T73 (≠ S98), S74 (= S99), K77 (= K102), R171 (≠ M196)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 90% coverage: 22:316/327 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R74), T50 (= T75), K77 (= K102), R99 (= R124), H127 (= H152), Q130 (= Q155), L210 (= L238), P249 (= P279), G277 (= G308)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S72), T48 (= T73), R49 (= R74), T50 (= T75), S74 (= S99), K77 (= K102), R99 (= R124), H127 (= H152), R160 (= R185), R211 (= R239), Q213 (= Q241), A250 (≠ G280)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
39% identity, 91% coverage: 23:319/327 of query aligns to 3:291/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S72), T49 (= T73), R50 (= R74), T51 (= T75), S75 (= S99), K78 (= K102), R100 (= R124), H127 (= H152), R160 (= R185), R210 (= R239), Q212 (= Q241), A253 (≠ G280)
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)
37% identity, 90% coverage: 25:319/327 of query aligns to 5:289/291 of 4bjhB
- active site: R47 (= R74), T48 (= T75), K75 (= K102), R97 (= R124), H126 (= H152), Q129 (= Q155)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S72), T46 (= T73), R47 (= R74), T48 (= T75), R97 (= R124), H126 (= H152), R159 (= R185), V160 (= V186), R213 (= R239), Q215 (= Q241), G251 (= G280)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
37% identity, 90% coverage: 25:319/327 of query aligns to 5:289/291 of 3d6nB
- active site: R47 (= R74), T48 (= T75), K75 (= K102), R97 (= R124), H126 (= H152), Q129 (= Q155)
- binding citrate anion: T48 (= T75), R97 (= R124), H126 (= H152), R159 (= R185), V160 (= V186), R213 (= R239), G251 (= G280)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
37% identity, 83% coverage: 51:323/327 of query aligns to 34:307/307 of 5g1nE
- active site: R57 (= R74), T58 (= T75), K85 (= K102), R106 (= R124), H134 (= H152), Q137 (= Q155), T227 (≠ L238), P266 (= P279), G292 (= G308)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S72), T56 (= T73), R57 (= R74), T58 (= T75), S82 (= S99), K85 (= K102), R106 (= R124), H134 (= H152), R167 (= R185), R228 (= R239), Q230 (= Q241), M267 (≠ G280)
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, 83% coverage: 51:323/327 of query aligns to 1952:2225/2225 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
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)
38% identity, 83% coverage: 51:323/327 of query aligns to 1952:2225/2225 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.
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
37% identity, 83% coverage: 51:323/327 of query aligns to 31:292/292 of 5g1pA
- active site: R54 (= R74), T55 (= T75), K82 (= K102), R103 (= R124), H131 (= H152), Q134 (= Q155), T223 (≠ L238), P251 (= P279), G277 (= G308)
- binding phosphoric acid mono(formamide)ester: S52 (= S72), T53 (= T73), R54 (= R74), T55 (= T75), R103 (= R124), Q134 (= Q155), M252 (≠ G280)
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
36% identity, 82% coverage: 51:317/327 of query aligns to 44:312/316 of 8bplA
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)
37% identity, 80% coverage: 56:317/327 of query aligns to 1944:2207/2214 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)
37% identity, 80% coverage: 56:317/327 of query aligns to 1970:2234/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
37% identity, 80% coverage: 56:317/327 of query aligns to 38:301/307 of 1ml4A