SitesBLAST
Comparing WP_013451026.1 NCBI__GCF_000183405.1:WP_013451026.1 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)
46% identity, 99% coverage: 5:311/311 of query aligns to 2:297/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
46% identity, 95% coverage: 5:298/311 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R57), T50 (= T58), K77 (= K85), R99 (= R107), H127 (= H135), Q130 (= Q138), L210 (= L221), P249 (= P262), G277 (= G290)
- binding phosphoric acid mono(formamide)ester: S47 (= S55), T48 (= T56), R49 (= R57), T50 (= T58), R99 (= R107), H127 (= H135), Q130 (= Q138), P249 (= P262), A250 (≠ G263)
- binding phosphate ion: S11 (≠ T14), T12 (≠ K15), Q23 (≠ E26), K26 (= K29), E140 (= E148), R171 (≠ K179), K241 (= K254), H243 (≠ D256), K272 (≠ T285), K272 (≠ T285), K275 (≠ E288)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
46% identity, 95% coverage: 5:298/311 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R57), T50 (= T58), K77 (= K85), R99 (= R107), H127 (= H135), Q130 (= Q138), L210 (= L221), P249 (= P262), G277 (= G290)
- binding phosphate ion: S11 (≠ T14), T12 (≠ K15), T73 (≠ S81), S74 (= S82), K77 (= K85), R171 (≠ K179)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
46% identity, 95% coverage: 5:298/311 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R57), T50 (= T58), K77 (= K85), R99 (= R107), H127 (= H135), Q130 (= Q138), L210 (= L221), P249 (= P262), G277 (= G290)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S55), T48 (= T56), R49 (= R57), T50 (= T58), S74 (= S82), K77 (= K85), R99 (= R107), H127 (= H135), R160 (= R168), R211 (= R222), Q213 (= Q224), A250 (≠ G263)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
44% identity, 94% coverage: 7:298/311 of query aligns to 4:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S55), T49 (= T56), R50 (= R57), T51 (= T58), S75 (= S82), K78 (= K85), R100 (= R107), H127 (= H135), R160 (= R168), R210 (= R222), Q212 (= Q224), A253 (≠ G263)
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, 95% coverage: 5:301/311 of query aligns to 2:289/291 of 4bjhB
- active site: R47 (= R57), T48 (= T58), K75 (= K85), R97 (= R107), H126 (= H135), Q129 (= Q138)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S55), T46 (= T56), R47 (= R57), T48 (= T58), R97 (= R107), H126 (= H135), R159 (= R168), V160 (= V169), R213 (= R222), Q215 (= Q224), G251 (= G263)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
41% identity, 95% coverage: 5:301/311 of query aligns to 2:289/291 of 3d6nB
- active site: R47 (= R57), T48 (= T58), K75 (= K85), R97 (= R107), H126 (= H135), Q129 (= Q138)
- binding citrate anion: T48 (= T58), R97 (= R107), H126 (= H135), R159 (= R168), V160 (= V169), R213 (= R222), G251 (= G263)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
41% identity, 95% coverage: 5:301/311 of query aligns to 5:303/307 of 1ml4A
- active site: R56 (= R57), T57 (= T58), K85 (= K85), R106 (= R107), H134 (= H135), Q137 (= Q138), T227 (≠ L221), P266 (= P262), G292 (= G290)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S55), T55 (= T56), R56 (= R57), T57 (= T58), R106 (= R107), H134 (= H135), R167 (= R168), T168 (≠ V169), R228 (= R222), L267 (≠ G263)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
37% identity, 92% coverage: 14:298/311 of query aligns to 15:300/307 of 5g1nE
- active site: R57 (= R57), T58 (= T58), K85 (= K85), R106 (= R107), H134 (= H135), Q137 (= Q138), T227 (≠ L221), P266 (= P262), G292 (= G290)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S55), T56 (= T56), R57 (= R57), T58 (= T58), S82 (= S82), K85 (= K85), R106 (= R107), H134 (= H135), R167 (= R168), R228 (= R222), Q230 (= Q224), M267 (≠ G263)
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, 92% coverage: 14:298/311 of query aligns to 1933:2218/2225 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, 92% coverage: 14:298/311 of query aligns to 1933:2218/2225 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
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
39% identity, 95% coverage: 5:298/311 of query aligns to 2:296/304 of 4eknB
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
35% identity, 92% coverage: 14:298/311 of query aligns to 12:285/292 of 5g1pA
- active site: R54 (= R57), T55 (= T58), K82 (= K85), R103 (= R107), H131 (= H135), Q134 (= Q138), T223 (≠ L221), P251 (= P262), G277 (= G290)
- binding phosphoric acid mono(formamide)ester: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R103 (= R107), Q134 (= Q138), M252 (≠ G263)
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
39% identity, 96% coverage: 2:301/311 of query aligns to 15:308/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
39% identity, 96% coverage: 2:301/311 of query aligns to 15:308/312 of 6ypoA
- active site: R109 (= R107), H137 (= H135), Q140 (= Q138), T231 (≠ L221), P271 (= P262), G297 (= G290)
- binding uridine-5'-monophosphate: R58 (= R57), T59 (= T58), R109 (= R107), H137 (= H135), R170 (= R168), T171 (≠ V169), R232 (= R222), H270 (= H261), P271 (= P262), L272 (≠ G263)
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
39% identity, 96% coverage: 2:301/311 of query aligns to 27:320/324 of 6yvbC
- active site: R121 (= R107), H149 (= H135), Q152 (= Q138), T243 (≠ L221), P283 (= P262), G309 (= G290)
- binding phosphoric acid mono(formamide)ester: S68 (= S55), T69 (= T56), R70 (= R57), T71 (= T58), R121 (= R107), H149 (= H135), Q152 (= Q138), P283 (= P262)
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
39% identity, 96% coverage: 2:301/311 of query aligns to 93:386/390 of P49077
- R136 (= R57) binding UMP
- T137 (= T58) binding UMP
- R187 (= R107) binding UMP
- H215 (= H135) binding UMP
- R248 (= R168) binding UMP
- R310 (= R222) binding UMP
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
35% identity, 96% coverage: 2:301/311 of query aligns to 4:303/310 of 2hseA
- active site: R54 (= R57), T55 (= T58), K84 (= K85), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (≠ L221), P266 (= P262), G292 (= G290)
- binding aspartic acid: R54 (= R57), T55 (= T58), S58 (= S61), R105 (= R107), H134 (= H135), Q137 (= Q138), R167 (= R168), R229 (= R222), Q231 (= Q224), L267 (≠ G263), P268 (= P264), A289 (≠ V287), R296 (= R294)
- binding phosphonoacetamide: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), L267 (≠ G263)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
35% identity, 96% coverage: 2:301/311 of query aligns to 4:303/310 of 2a0fA
- active site: R54 (= R57), T55 (= T58), K84 (= K85), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (≠ L221), P266 (= P262), G292 (= G290)
- binding phosphonoacetamide: R54 (= R57), T55 (= T58), H134 (= H135), Q137 (= Q138), L267 (≠ G263)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
35% identity, 96% coverage: 2:301/311 of query aligns to 5:304/311 of P0A786
- R55 (= R57) binding carbamoyl phosphate
- T56 (= T58) binding carbamoyl phosphate
- R106 (= R107) binding carbamoyl phosphate
- H135 (= H135) binding carbamoyl phosphate
- Q138 (= Q138) binding carbamoyl phosphate
- L268 (≠ G263) binding carbamoyl phosphate
- P269 (= P264) binding carbamoyl phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_013451026.1 NCBI__GCF_000183405.1:WP_013451026.1
MLNRKDLTGLVDVTKEEILEILDTAEKFKEINSREIKKVPALKGKTIANLFFEPSTRTRT
SFEIAGKRLSADVINFTASASSTTKGETLIDTVKNIESMGVDMFVVRHYYSGSVRFIAQN
TKAHVINAGDGTNEHPTQSLLDLYTIKEQKGKLEGLKVAIIGDITHSRVARSNAWAMKKL
GIDLRLYGPKTMIPRDYLPFGCKVCNSMEEALEDCDVVMMLRIQLERQGIALLPSLKEYS
KLFGLNKNRLDLAKKDAIIMHPGPINRGVELPSYLADCDKSVILTQVENGVAVRMAVMYL
LAMQQNTKLGE
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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