SitesBLAST
Comparing WP_010933460.1 NCBI__GCF_000006985.1:WP_010933460.1 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)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
38% identity, 99% coverage: 1:306/308 of query aligns to 1:292/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S53), T49 (= T54), R50 (= R55), T51 (= T56), S75 (= S80), K78 (= K83), R100 (= R105), H127 (= H133), R160 (= R166), R210 (= R220), Q212 (= Q222), 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)
40% identity, 100% coverage: 1:307/308 of query aligns to 1:291/291 of 4bjhB
- active site: R47 (= R55), T48 (= T56), K75 (= K83), R97 (= R105), H126 (= H133), Q129 (= Q136)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S53), T46 (= T54), R47 (= R55), T48 (= T56), R97 (= R105), H126 (= H133), R159 (= R166), V160 (= V167), R213 (= R220), Q215 (= Q222), G251 (= G261)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
40% identity, 100% coverage: 1:307/308 of query aligns to 1:291/291 of 3d6nB
- active site: R47 (= R55), T48 (= T56), K75 (= K83), R97 (= R105), H126 (= H133), Q129 (= Q136)
- binding citrate anion: T48 (= T56), R97 (= R105), H126 (= H133), R159 (= R166), V160 (= V167), R213 (= R220), G251 (= G261)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 99% coverage: 1:306/308 of query aligns to 1:289/290 of 3r7lA
- active site: R49 (= R55), T50 (= T56), K77 (= K83), R99 (= R105), H127 (= H133), Q130 (= Q136), L210 (= L219), P249 (= P260), G277 (= G294)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S53), T48 (= T54), R49 (= R55), T50 (= T56), S74 (= S80), K77 (= K83), R99 (= R105), H127 (= H133), R160 (= R166), R211 (= R220), Q213 (= Q222), A250 (≠ G261)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 99% coverage: 1:306/308 of query aligns to 1:289/291 of 3r7fA
- active site: R49 (= R55), T50 (= T56), K77 (= K83), R99 (= R105), H127 (= H133), Q130 (= Q136), L210 (= L219), P249 (= P260), G277 (= G294)
- binding phosphoric acid mono(formamide)ester: S47 (= S53), T48 (= T54), R49 (= R55), T50 (= T56), R99 (= R105), H127 (= H133), Q130 (= Q136), P249 (= P260), A250 (≠ G261)
- binding phosphate ion: S11 (≠ P11), T12 (≠ A12), Q23 (≠ T23), K26 (≠ R26), E140 (= E146), R171 (≠ T177), K241 (= K252), H243 (≠ L254), K272 (≠ E289), K272 (≠ E289), K275 (≠ T292)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 99% coverage: 1:306/308 of query aligns to 1:289/291 of 3r7dA
- active site: R49 (= R55), T50 (= T56), K77 (= K83), R99 (= R105), H127 (= H133), Q130 (= Q136), L210 (= L219), P249 (= P260), G277 (= G294)
- binding phosphate ion: S11 (≠ P11), T12 (≠ A12), T73 (≠ S79), S74 (= S80), K77 (= K83), R171 (≠ T177)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
40% identity, 99% coverage: 1:306/308 of query aligns to 1:289/304 of P05654
Sites not aligning to the query:
- 303 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, 88% coverage: 39:308/308 of query aligns to 1959:2224/2225 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.
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 100% coverage: 2:308/308 of query aligns to 6:306/307 of 5g1nE
- active site: R57 (= R55), T58 (= T56), K85 (= K83), R106 (= R105), H134 (= H133), Q137 (= Q136), T227 (≠ L219), P266 (= P260), G292 (= G294)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S53), T56 (= T54), R57 (= R55), T58 (= T56), S82 (= S80), K85 (= K83), R106 (= R105), H134 (= H133), R167 (= R166), R228 (= R220), Q230 (= Q222), M267 (≠ G261)
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)
38% identity, 88% coverage: 39:308/308 of query aligns to 1959:2224/2225 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
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
39% identity, 84% coverage: 45:302/308 of query aligns to 46:300/307 of 1ml4A
- active site: R56 (= R55), T57 (= T56), K85 (= K83), R106 (= R105), H134 (= H133), Q137 (= Q136), T227 (≠ L219), P266 (= P260), G292 (= G294)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S53), T55 (= T54), R56 (= R55), T57 (= T56), R106 (= R105), H134 (= H133), R167 (= R166), T168 (≠ V167), R228 (= R220), L267 (≠ G261)
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)
37% identity, 86% coverage: 39:302/308 of query aligns to 1958:2217/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
34% identity, 100% coverage: 2:308/308 of query aligns to 3:291/292 of 5g1pA
- active site: R54 (= R55), T55 (= T56), K82 (= K83), R103 (= R105), H131 (= H133), Q134 (= Q136), T223 (≠ L219), P251 (= P260), G277 (= G294)
- binding phosphoric acid mono(formamide)ester: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R103 (= R105), Q134 (= Q136), M252 (≠ G261)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
36% identity, 99% coverage: 1:306/308 of query aligns to 1:300/304 of 4eknB
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
35% identity, 93% coverage: 18:302/308 of query aligns to 32:311/316 of 8bplA
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)
37% identity, 86% coverage: 39:302/308 of query aligns to 1954:2213/2224 of P05990
Sites not aligning to the query:
- 1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
- 1883 modified: Phosphoserine
- 1885 modified: Phosphoserine
- 1892 modified: Phosphoserine
- 1894 modified: Phosphoserine
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
36% identity, 92% coverage: 21:302/308 of query aligns to 24:300/310 of 2hseA
- active site: R54 (= R55), T55 (= T56), K84 (= K83), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (≠ L219), P266 (= P260), G292 (= G294)
- binding aspartic acid: R54 (= R55), T55 (= T56), S58 (= S59), R105 (= R105), H134 (= H133), Q137 (= Q136), R167 (= R166), R229 (= R220), Q231 (= Q222), L267 (≠ G261), P268 (= P262), A289 (≠ V291), R296 (= R298)
- binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), L267 (≠ G261)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
36% identity, 92% coverage: 21:302/308 of query aligns to 24:300/310 of 2a0fA
- active site: R54 (= R55), T55 (= T56), K84 (= K83), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (≠ L219), P266 (= P260), G292 (= G294)
- binding phosphonoacetamide: R54 (= R55), T55 (= T56), H134 (= H133), Q137 (= Q136), L267 (≠ G261)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 92% coverage: 21:302/308 of query aligns to 25:301/311 of P0A786
- R55 (= R55) binding carbamoyl phosphate
- T56 (= T56) binding carbamoyl phosphate
- R106 (= R105) binding carbamoyl phosphate
- H135 (= H133) binding carbamoyl phosphate
- Q138 (= Q136) binding carbamoyl phosphate
- L268 (≠ G261) binding carbamoyl phosphate
- P269 (= P262) binding carbamoyl phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
36% identity, 92% coverage: 21:302/308 of query aligns to 24:300/310 of 2ipoA
- active site: R54 (= R55), T55 (= T56), K84 (= K83), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (≠ L219), P266 (= P260), G292 (= G294)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), H134 (= H133), R167 (= R166), T168 (≠ V167), R229 (= R220), L267 (≠ G261)
Query Sequence
>WP_010933460.1 NCBI__GCF_000006985.1:WP_010933460.1
MNHLTGLFGLPASTLVELLDLATGYREGLNREPETFAPLLSNRRIALVFFENSTRTRFSF
ELAARHLGAGTLSFTAASSSVSKGETLSDTIRNLEAMKVDAFVLRHPSSGAAEFVASITK
RPVINAGDGTHEHPTQALLDLLTLREYFGKIEGLKIMILGDILHSRVARSNIIGLKTLGA
EIAVCAPTTLLPGRIDQLGVRVFTGIDEALAWADAAIVLRLQLERATGGYIPSLEEYSAS
YGLTDEKLDRLKRLMPVLHPGPINREIEISNLVADRIQPPGYSSSMLMEQVTNGVAVRMA
VLHRLLAK
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