SitesBLAST
Comparing WP_035255368.1 NCBI__GCF_000422285.1:WP_035255368.1 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)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
45% identity, 94% coverage: 1:289/308 of query aligns to 7:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
45% identity, 94% coverage: 1:289/308 of query aligns to 7:285/290 of 3r7lA
- active site: R49 (= R48), T50 (= T49), K77 (= K76), R99 (= R98), H127 (= H126), Q130 (= Q129), L210 (= L212), P249 (= P253), G277 (= G281)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S46), T48 (= T47), R49 (= R48), T50 (= T49), S74 (= S73), K77 (= K76), R99 (= R98), H127 (= H126), R160 (= R159), R211 (= R213), Q213 (= Q215), A250 (≠ G254)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
45% identity, 94% coverage: 1:289/308 of query aligns to 7:285/291 of 3r7fA
- active site: R49 (= R48), T50 (= T49), K77 (= K76), R99 (= R98), H127 (= H126), Q130 (= Q129), L210 (= L212), P249 (= P253), G277 (= G281)
- binding phosphoric acid mono(formamide)ester: S47 (= S46), T48 (= T47), R49 (= R48), T50 (= T49), R99 (= R98), H127 (= H126), Q130 (= Q129), P249 (= P253), A250 (≠ G254)
- binding phosphate ion: S11 (= S5), T12 (≠ V6), Q23 (≠ D17), K26 (= K20), E140 (= E139), R171 (≠ K170), K241 (= K245), H243 (≠ D247), K272 (≠ D276), K272 (≠ D276), K275 (≠ A279)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
45% identity, 94% coverage: 1:289/308 of query aligns to 7:285/291 of 3r7dA
- active site: R49 (= R48), T50 (= T49), K77 (= K76), R99 (= R98), H127 (= H126), Q130 (= Q129), L210 (= L212), P249 (= P253), G277 (= G281)
- binding phosphate ion: S11 (= S5), T12 (≠ V6), T73 (≠ S72), S74 (= S73), K77 (= K76), R171 (≠ K170)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
41% identity, 94% coverage: 1:289/308 of query aligns to 7:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S46), T49 (= T47), R50 (= R48), T51 (= T49), S75 (= S73), K78 (= K76), R100 (= R98), H127 (= H126), R160 (= R159), R210 (= R213), Q212 (= Q215), A253 (≠ G254)
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, 94% coverage: 4:292/308 of query aligns to 10:289/291 of 4bjhB
- active site: R47 (= R48), T48 (= T49), K75 (= K76), R97 (= R98), H126 (= H126), Q129 (= Q129)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S46), T46 (= T47), R47 (= R48), T48 (= T49), R97 (= R98), H126 (= H126), R159 (= R159), V160 (= V160), R213 (= R213), Q215 (= Q215), G251 (= G254)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
41% identity, 94% coverage: 4:292/308 of query aligns to 10:289/291 of 3d6nB
- active site: R47 (= R48), T48 (= T49), K75 (= K76), R97 (= R98), H126 (= H126), Q129 (= Q129)
- binding citrate anion: T48 (= T49), R97 (= R98), H126 (= H126), R159 (= R159), V160 (= V160), R213 (= R213), G251 (= G254)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
38% identity, 95% coverage: 3:294/308 of query aligns to 13:305/307 of 5g1nE
- active site: R57 (= R48), T58 (= T49), K85 (= K76), R106 (= R98), H134 (= H126), Q137 (= Q129), T227 (≠ L212), P266 (= P253), G292 (= G281)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S46), T56 (= T47), R57 (= R48), T58 (= T49), S82 (= S73), K85 (= K76), R106 (= R98), H134 (= H126), R167 (= R159), R228 (= R213), Q230 (= Q215), M267 (≠ G254)
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, 95% coverage: 3:294/308 of query aligns to 1931:2223/2225 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 ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding ; H→A: No zinc-binding and no catalytic activity.
- 1475 binding
- 1505 binding
- 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 ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding ; C→S: Reduces dihydroorotase activity.
- 1614 binding ; H→A: Abolishes dihydroorotase activity.
- 1637 binding ; E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding
- 1686 binding ; D→N: Abolishes dihydroorotase activity.
- 1690 binding ; H→N: 3% of wild-type catalytic activity.
- 1702 binding
- 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)
37% identity, 95% coverage: 3:294/308 of query aligns to 1931:2223/2225 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)
36% identity, 95% coverage: 3:294/308 of query aligns to 10:290/292 of 5g1pA
- active site: R54 (= R48), T55 (= T49), K82 (= K76), R103 (= R98), H131 (= H126), Q134 (= Q129), T223 (≠ L212), P251 (= P253), G277 (= G281)
- binding phosphoric acid mono(formamide)ester: S52 (= S46), T53 (= T47), R54 (= R48), T55 (= T49), R103 (= R98), Q134 (= Q129), M252 (≠ G254)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
39% identity, 94% coverage: 4:294/308 of query aligns to 13:305/307 of 1ml4A
- active site: R56 (= R48), T57 (= T49), K85 (= K76), R106 (= R98), H134 (= H126), Q137 (= Q129), T227 (≠ L212), P266 (= P253), G292 (= G281)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S46), T55 (= T47), R56 (= R48), T57 (= T49), R106 (= R98), H134 (= H126), R167 (= R159), T168 (≠ V160), R228 (= R213), L267 (≠ G254)
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
36% identity, 95% coverage: 3:294/308 of query aligns to 23:316/316 of 8bplA
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
36% identity, 95% coverage: 1:294/308 of query aligns to 12:305/310 of 2hseA
- active site: R54 (= R48), T55 (= T49), K84 (= K76), R105 (= R98), H134 (= H126), Q137 (= Q129), T228 (≠ L212), P266 (= P253), G292 (= G281)
- binding aspartic acid: R54 (= R48), T55 (= T49), S58 (= S52), R105 (= R98), H134 (= H126), Q137 (= Q129), R167 (= R159), R229 (= R213), Q231 (= Q215), L267 (≠ G254), P268 (= P255), A289 (≠ V278), R296 (= R285)
- binding phosphonoacetamide: S52 (= S46), T53 (= T47), R54 (= R48), T55 (= T49), R105 (= R98), L267 (≠ G254)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
36% identity, 95% coverage: 1:294/308 of query aligns to 12:305/310 of 2a0fA
- active site: R54 (= R48), T55 (= T49), K84 (= K76), R105 (= R98), H134 (= H126), Q137 (= Q129), T228 (≠ L212), P266 (= P253), G292 (= G281)
- binding phosphonoacetamide: R54 (= R48), T55 (= T49), H134 (= H126), Q137 (= Q129), L267 (≠ G254)
Q09794 Multifunctional protein ura1; 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 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 96% coverage: 3:297/308 of query aligns to 1944:2241/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
36% identity, 95% coverage: 1:294/308 of query aligns to 12:305/310 of 2ipoA
- active site: R54 (= R48), T55 (= T49), K84 (= K76), R105 (= R98), H134 (= H126), Q137 (= Q129), T228 (≠ L212), P266 (= P253), G292 (= G281)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S46), T53 (= T47), R54 (= R48), T55 (= T49), R105 (= R98), H134 (= H126), R167 (= R159), T168 (≠ V160), R229 (= R213), L267 (≠ G254)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
36% identity, 95% coverage: 1:294/308 of query aligns to 12:305/310 of 2h3eA
- active site: R54 (= R48), T55 (= T49), K84 (= K76), R105 (= R98), H134 (= H126), Q137 (= Q129), T228 (≠ L212), P266 (= P253), G292 (= G281)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S46), T53 (= T47), R54 (= R48), T55 (= T49), R105 (= R98), H134 (= H126), R167 (= R159), R229 (= R213), L267 (≠ G254)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
36% identity, 95% coverage: 1:294/308 of query aligns to 12:305/310 of 2fzkA
- active site: R54 (= R48), T55 (= T49), K84 (= K76), R105 (= R98), H134 (= H126), Q137 (= Q129), T228 (≠ L212), P266 (= P253), G292 (= G281)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T49), H134 (= H126), Q137 (= Q129), T168 (≠ V160), R229 (= R213), P266 (= P253), L267 (≠ G254), R296 (= R285)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
36% identity, 95% coverage: 1:294/308 of query aligns to 12:305/310 of 2fzgA
- active site: R54 (= R48), T55 (= T49), K84 (= K76), R105 (= R98), H134 (= H126), Q137 (= Q129), T228 (≠ L212), P266 (= P253), G292 (= G281)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S46), R54 (= R48), T55 (= T49), R105 (= R98), H134 (= H126), R167 (= R159), T168 (≠ V160), R229 (= R213), P266 (= P253), L267 (≠ G254)
Query Sequence
>WP_035255368.1 NCBI__GCF_000422285.1:WP_035255368.1
MGQLSVDDIQLILDTADSFKDISSREIKKVPTLRGKSIVNFFYEASTRTRTSFEVAAKRL
SADTFSLSASTSSMVKGETLIDTGRNLQAMSPDVIVIRHSSSGAPHLLAKGVKACVVNAG
DGINEHPTQALLDLYTIRERKGRIRGLNIAIIGDIAHSRVARSNMIGLTKMGARVTIGGP
PTMIPLGMEAFGVEVVPDPREAIGDKDVVMMLRIQLERQRRTLFPSLREYSAAFGLDSEA
LKSAKPDCVIMHPGPINRGVEISSELADSPASLILDQVANGVAVRMAILYLLIGGSKADA
VDKERAAG
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