SitesBLAST
Comparing WP_089322409.1 NCBI__GCF_900188395.1:WP_089322409.1 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)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
44% identity, 95% coverage: 1:296/312 of query aligns to 1:285/290 of 3r7lA
- active site: R49 (= R54), T50 (= T55), K77 (= K82), R99 (= R104), H127 (= H132), Q130 (= Q135), L210 (= L218), P249 (= P260), G277 (= G288)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S52), T48 (= T53), R49 (= R54), T50 (= T55), S74 (= S79), K77 (= K82), R99 (= R104), H127 (= H132), R160 (= R165), R211 (= R219), Q213 (= Q221), A250 (≠ G261)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
44% identity, 95% coverage: 1:296/312 of query aligns to 1:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
44% identity, 95% coverage: 1:296/312 of query aligns to 1:285/291 of 3r7fA
- active site: R49 (= R54), T50 (= T55), K77 (= K82), R99 (= R104), H127 (= H132), Q130 (= Q135), L210 (= L218), P249 (= P260), G277 (= G288)
- binding phosphoric acid mono(formamide)ester: S47 (= S52), T48 (= T53), R49 (= R54), T50 (= T55), R99 (= R104), H127 (= H132), Q130 (= Q135), P249 (= P260), A250 (≠ G261)
- binding phosphate ion: S11 (≠ T11), T12 (≠ K12), Q23 (≠ E27), K26 (≠ R30), E140 (= E145), R171 (≠ K176), K241 (= K252), H243 (≠ D254), K272 (≠ E283), K272 (≠ E283), K275 (≠ E286)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
44% identity, 95% coverage: 1:296/312 of query aligns to 1:285/291 of 3r7dA
- active site: R49 (= R54), T50 (= T55), K77 (= K82), R99 (= R104), H127 (= H132), Q130 (= Q135), L210 (= L218), P249 (= P260), G277 (= G288)
- binding phosphate ion: S11 (≠ T11), T12 (≠ K12), T73 (≠ S78), S74 (= S79), K77 (= K82), R171 (≠ K176)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
41% identity, 96% coverage: 1:299/312 of query aligns to 1:291/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S52), T49 (= T53), R50 (= R54), T51 (= T55), S75 (= S79), K78 (= K82), R100 (= R104), H127 (= H132), R160 (= R165), R210 (= R219), Q212 (= Q221), A253 (≠ G261)
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)
39% identity, 96% coverage: 1:301/312 of query aligns to 1:291/291 of 4bjhB
- active site: R47 (= R54), T48 (= T55), K75 (= K82), R97 (= R104), H126 (= H132), Q129 (= Q135)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S52), T46 (= T53), R47 (= R54), T48 (= T55), R97 (= R104), H126 (= H132), R159 (= R165), V160 (= V166), R213 (= R219), Q215 (= Q221), G251 (= G261)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
39% identity, 96% coverage: 1:301/312 of query aligns to 1:291/291 of 3d6nB
- active site: R47 (= R54), T48 (= T55), K75 (= K82), R97 (= R104), H126 (= H132), Q129 (= Q135)
- binding citrate anion: T48 (= T55), R97 (= R104), H126 (= H132), R159 (= R165), V160 (= V166), R213 (= R219), G251 (= G261)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
36% identity, 96% coverage: 2:302/312 of query aligns to 6:306/307 of 5g1nE
- active site: R57 (= R54), T58 (= T55), K85 (= K82), R106 (= R104), H134 (= H132), Q137 (= Q135), T227 (≠ L218), P266 (= P260), G292 (= G288)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S52), T56 (= T53), R57 (= R54), T58 (= T55), S82 (= S79), K85 (= K82), R106 (= R104), H134 (= H132), R167 (= R165), R228 (= R219), Q230 (= Q221), M267 (≠ G261)
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)
36% identity, 96% coverage: 2:302/312 of query aligns to 1924:2224/2225 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)
36% identity, 96% coverage: 2:302/312 of query aligns to 1924:2224/2225 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
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
36% identity, 96% coverage: 2:302/312 of query aligns to 3:291/292 of 5g1pA
- active site: R54 (= R54), T55 (= T55), K82 (= K82), R103 (= R104), H131 (= H132), Q134 (= Q135), T223 (≠ L218), P251 (= P260), G277 (= G288)
- binding phosphoric acid mono(formamide)ester: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R103 (= R104), Q134 (= Q135), M252 (≠ G261)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
37% identity, 95% coverage: 2:296/312 of query aligns to 5:300/307 of 1ml4A
- active site: R56 (= R54), T57 (= T55), K85 (= K82), R106 (= R104), H134 (= H132), Q137 (= Q135), T227 (≠ L218), P266 (= P260), G292 (= G288)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S52), T55 (= T53), R56 (= R54), T57 (= T55), R106 (= R104), H134 (= H132), R167 (= R165), T168 (≠ V166), R228 (= R219), L267 (≠ G261)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
36% identity, 97% coverage: 1:304/312 of query aligns to 1:304/304 of 4eknB
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)
34% identity, 95% coverage: 2:296/312 of query aligns to 1923:2217/2225 of P20054