SitesBLAST
Comparing WP_011390938.1 NCBI__GCF_000013085.1:WP_011390938.1 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)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
43% identity, 93% coverage: 12:307/319 of query aligns to 2:286/291 of 3r7fA
- active site: R49 (= R64), T50 (= T65), K77 (= K92), R99 (= R114), H127 (= H142), Q130 (= Q145), L210 (= L228), P249 (= P269), G277 (= G298)
- binding phosphoric acid mono(formamide)ester: S47 (= S62), T48 (= T63), R49 (= R64), T50 (= T65), R99 (= R114), H127 (= H142), Q130 (= Q145), P249 (= P269), A250 (≠ G270)
- binding phosphate ion: S11 (≠ V21), T12 (≠ P22), Q23 (≠ E33), K26 (≠ S41), E140 (≠ R155), R171 (≠ L186), K241 (= K261), H243 (≠ D263), K272 (≠ E293), K272 (≠ E293), K275 (≠ E296)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
43% identity, 93% coverage: 12:307/319 of query aligns to 2:286/291 of 3r7dA
- active site: R49 (= R64), T50 (= T65), K77 (= K92), R99 (= R114), H127 (= H142), Q130 (= Q145), L210 (= L228), P249 (= P269), G277 (= G298)
- binding phosphate ion: S11 (≠ V21), T12 (≠ P22), T73 (≠ S88), S74 (= S89), K77 (= K92), R171 (≠ L186)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
43% identity, 93% coverage: 12:307/319 of query aligns to 2:286/290 of 3r7lA
- active site: R49 (= R64), T50 (= T65), K77 (= K92), R99 (= R114), H127 (= H142), Q130 (= Q145), L210 (= L228), P249 (= P269), G277 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S62), T48 (= T63), R49 (= R64), T50 (= T65), S74 (= S89), K77 (= K92), R99 (= R114), H127 (= H142), R160 (= R175), R211 (= R229), Q213 (= Q231), A250 (≠ G270)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
42% identity, 97% coverage: 12:319/319 of query aligns to 2:299/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
41% identity, 93% coverage: 13:309/319 of query aligns to 3:291/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S62), T49 (= T63), R50 (= R64), T51 (= T65), S75 (= S89), K78 (= K92), R100 (= R114), H127 (= H142), R160 (= R175), R210 (= R229), Q212 (= Q231), A253 (≠ G270)
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)
42% identity, 79% coverage: 57:309/319 of query aligns to 39:289/291 of 4bjhB
- active site: R47 (= R64), T48 (= T65), K75 (= K92), R97 (= R114), H126 (= H142), Q129 (= Q145)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S62), T46 (= T63), R47 (= R64), T48 (= T65), R97 (= R114), H126 (= H142), R159 (= R175), V160 (= V176), R213 (= R229), Q215 (= Q231), G251 (= G270)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
42% identity, 79% coverage: 57:309/319 of query aligns to 39:289/291 of 3d6nB
- active site: R47 (= R64), T48 (= T65), K75 (= K92), R97 (= R114), H126 (= H142), Q129 (= Q145)
- binding citrate anion: T48 (= T65), R97 (= R114), H126 (= H142), R159 (= R175), V160 (= V176), R213 (= R229), G251 (= G270)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 95% coverage: 12:313/319 of query aligns to 6:307/307 of 5g1nE
- active site: R57 (= R64), T58 (= T65), K85 (= K92), R106 (= R114), H134 (= H142), Q137 (= Q145), T227 (≠ L228), P266 (= P269), G292 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S62), T56 (= T63), R57 (= R64), T58 (= T65), S82 (= S89), K85 (= K92), R106 (= R114), H134 (= H142), R167 (= R175), R228 (= R229), Q230 (= Q231), M267 (≠ G270)
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
34% identity, 95% coverage: 12:313/319 of query aligns to 3:292/292 of 5g1pA
- active site: R54 (= R64), T55 (= T65), K82 (= K92), R103 (= R114), H131 (= H142), Q134 (= Q145), T223 (≠ L228), P251 (= P269), G277 (= G298)
- binding phosphoric acid mono(formamide)ester: S52 (= S62), T53 (= T63), R54 (= R64), T55 (= T65), R103 (= R114), Q134 (= Q145), M252 (≠ G270)
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)
35% identity, 95% coverage: 12:313/319 of query aligns to 1924:2225/2225 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.
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)
35% identity, 95% coverage: 12:313/319 of query aligns to 1924:2225/2225 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
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
36% identity, 82% coverage: 45:306/319 of query aligns to 48:311/316 of 8bplA
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
35% identity, 93% coverage: 12:309/319 of query aligns to 2:299/304 of 4eknB
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, 94% coverage: 12:311/319 of query aligns to 1911:2211/2214 of P07259