SitesBLAST
Comparing WP_011736388.1 NCBI__GCF_000015045.1:WP_011736388.1 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)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 95% coverage: 7:301/310 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R59), T50 (= T60), K77 (= K87), R99 (= R109), H127 (= H137), Q130 (= Q140), L210 (= L224), P249 (= P265), G277 (= G293)
- binding phosphoric acid mono(formamide)ester: S47 (= S57), T48 (= T58), R49 (= R59), T50 (= T60), R99 (= R109), H127 (= H137), Q130 (= Q140), P249 (= P265), A250 (≠ G266)
- binding phosphate ion: S11 (≠ T16), T12 (≠ K17), Q23 (≠ E28), K26 (≠ R31), E140 (≠ D150), R171 (≠ K181), K241 (= K257), H243 (≠ D259), K272 (= K288), K272 (= K288), K275 (≠ E291)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 95% coverage: 7:301/310 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R59), T50 (= T60), K77 (= K87), R99 (= R109), H127 (= H137), Q130 (= Q140), L210 (= L224), P249 (= P265), G277 (= G293)
- binding phosphate ion: S11 (≠ T16), T12 (≠ K17), T73 (≠ S83), S74 (= S84), K77 (= K87), R171 (≠ K181)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 95% coverage: 7:301/310 of query aligns to 2:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 95% coverage: 7:301/310 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R59), T50 (= T60), K77 (= K87), R99 (= R109), H127 (= H137), Q130 (= Q140), L210 (= L224), P249 (= P265), G277 (= G293)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S57), T48 (= T58), R49 (= R59), T50 (= T60), S74 (= S84), K77 (= K87), R99 (= R109), H127 (= H137), R160 (= R170), R211 (= R225), Q213 (= Q227), A250 (≠ G266)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
37% identity, 95% coverage: 9:301/310 of query aligns to 4:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S57), T49 (= T58), R50 (= R59), T51 (= T60), S75 (= S84), K78 (= K87), R100 (= R109), H127 (= H137), R160 (= R170), R210 (= R225), Q212 (= Q227), A253 (≠ G266)
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, 95% coverage: 7:300/310 of query aligns to 2:285/291 of 4bjhB
- active site: R47 (= R59), T48 (= T60), K75 (= K87), R97 (= R109), H126 (= H137), Q129 (= Q140)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S57), T46 (= T58), R47 (= R59), T48 (= T60), R97 (= R109), H126 (= H137), R159 (= R170), V160 (= V171), R213 (= R225), Q215 (= Q227), G251 (= G266)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
40% identity, 95% coverage: 7:300/310 of query aligns to 2:285/291 of 3d6nB
- active site: R47 (= R59), T48 (= T60), K75 (= K87), R97 (= R109), H126 (= H137), Q129 (= Q140)
- binding citrate anion: T48 (= T60), R97 (= R109), H126 (= H137), R159 (= R170), V160 (= V171), R213 (= R225), G251 (= G266)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
36% identity, 96% coverage: 3:301/310 of query aligns to 1:300/307 of 1ml4A
- active site: R56 (= R59), T57 (= T60), K85 (= K87), R106 (= R109), H134 (= H137), Q137 (= Q140), T227 (≠ L224), P266 (= P265), G292 (= G293)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S57), T55 (= T58), R56 (= R59), T57 (= T60), R106 (= R109), H134 (= H137), R167 (= R170), T168 (≠ V171), R228 (= R225), L267 (≠ G266)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 95% coverage: 7:301/310 of query aligns to 6:300/307 of 5g1nE
- active site: R57 (= R59), T58 (= T60), K85 (= K87), R106 (= R109), H134 (= H137), Q137 (= Q140), T227 (≠ L224), P266 (= P265), G292 (= G293)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S57), T56 (= T58), R57 (= R59), T58 (= T60), S82 (= S84), K85 (= K87), R106 (= R109), H134 (= H137), R167 (= R170), R228 (= R225), Q230 (= Q227), M267 (≠ G266)
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, 96% coverage: 7:304/310 of query aligns to 1924:2221/2225 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)
35% identity, 96% coverage: 7:304/310 of query aligns to 1924:2221/2225 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)
33% identity, 95% coverage: 7:301/310 of query aligns to 3:285/292 of 5g1pA
- active site: R54 (= R59), T55 (= T60), K82 (= K87), R103 (= R109), H131 (= H137), Q134 (= Q140), T223 (≠ L224), P251 (= P265), G277 (= G293)
- binding phosphoric acid mono(formamide)ester: S52 (= S57), T53 (= T58), R54 (= R59), T55 (= T60), R103 (= R109), Q134 (= Q140), M252 (≠ G266)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
35% identity, 100% coverage: 1:309/310 of query aligns to 1:309/311 of P0A786
- M1 (= M1) modified: Initiator methionine, Removed
- R55 (= R59) binding carbamoyl phosphate
- T56 (= T60) binding carbamoyl phosphate
- R106 (= R109) binding carbamoyl phosphate
- H135 (= H137) binding carbamoyl phosphate
- Q138 (= Q140) binding carbamoyl phosphate
- L268 (≠ G266) binding carbamoyl phosphate
- P269 (= P267) binding carbamoyl phosphate
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
36% identity, 98% coverage: 7:309/310 of query aligns to 7:308/310 of 2hseA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L224), P266 (= P265), G292 (= G293)
- binding aspartic acid: R54 (= R59), T55 (= T60), S58 (= S63), R105 (= R109), H134 (= H137), Q137 (= Q140), R167 (= R170), R229 (= R225), Q231 (= Q227), L267 (≠ G266), P268 (= P267), A289 (≠ V290), R296 (= R297)
- binding phosphonoacetamide: S52 (= S57), T53 (= T58), R54 (= R59), T55 (= T60), R105 (= R109), L267 (≠ G266)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
36% identity, 98% coverage: 7:309/310 of query aligns to 7:308/310 of 2a0fA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L224), P266 (= P265), G292 (= G293)
- binding phosphonoacetamide: R54 (= R59), T55 (= T60), H134 (= H137), Q137 (= Q140), L267 (≠ G266)
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
35% identity, 98% coverage: 7:309/310 of query aligns to 7:308/310 of 2ipoA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L224), P266 (= P265), G292 (= G293)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S57), T53 (= T58), R54 (= R59), T55 (= T60), R105 (= R109), H134 (= H137), R167 (= R170), T168 (≠ V171), R229 (= R225), L267 (≠ G266)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
35% identity, 98% coverage: 7:309/310 of query aligns to 7:308/310 of 2h3eA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L224), P266 (= P265), G292 (= G293)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S57), T53 (= T58), R54 (= R59), T55 (= T60), R105 (= R109), H134 (= H137), R167 (= R170), R229 (= R225), L267 (≠ G266)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
35% identity, 98% coverage: 7:309/310 of query aligns to 7:308/310 of 2fzkA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L224), P266 (= P265), G292 (= G293)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T60), H134 (= H137), Q137 (= Q140), T168 (≠ V171), R229 (= R225), P266 (= P265), L267 (≠ G266), R296 (= R297)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
35% identity, 98% coverage: 7:309/310 of query aligns to 7:308/310 of 2fzgA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L224), P266 (= P265), G292 (= G293)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S57), R54 (= R59), T55 (= T60), R105 (= R109), H134 (= H137), R167 (= R170), T168 (≠ V171), R229 (= R225), P266 (= P265), L267 (≠ G266)
2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
35% identity, 98% coverage: 7:309/310 of query aligns to 7:308/310 of 2fzcA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L224), P266 (= P265), G292 (= G293)
- binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S57), R54 (= R59), T55 (= T60), R105 (= R109), R167 (= R170), T168 (≠ V171), P266 (= P265), L267 (≠ G266)
Query Sequence
>WP_011736388.1 NCBI__GCF_000015045.1:WP_011736388.1
MANFKHKDIIALQDLTKQEIELLLSTAESMREINNRDIKKVPTLRGKTIVNLFYESSTRT
RTSFELAAKRLSADTVNISPSTSSATKGETLADTALNLLAMKPDIIVMRHSVSGSHYFLS
KKLPCSIVNAGDGVHEHPSQGLLDMLTMKDRFGRLDGLKVAIVGDISHSRVARSNIQGLT
KLGSQVFLAGPPTMMPPGVERLGNVTVCDSLREAIQDADVVMMLRIQQERQGKTLMPNAR
EYARYFGLNPENLKLAKPDAMVMHPGPINRGVEMASSVVDGDQSWILKQVENGVAVRMSM
LYHVCEGELE
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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