SitesBLAST
Comparing 18270 FitnessBrowser__Keio:18270 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)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
100% identity, 100% coverage: 1:311/311 of query aligns to 1:311/311 of P0A786
- M1 (= M1) modified: Initiator methionine, Removed
- R55 (= R55) binding
- T56 (= T56) binding
- R106 (= R106) binding
- H135 (= H135) binding
- Q138 (= Q138) binding
- L268 (= L268) binding
- P269 (= P269) binding
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2ipoA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), R167 (= R168), T168 (= T169), R229 (= R230), L267 (= L268)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2h3eA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), R167 (= R168), R229 (= R230), L267 (= L268)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2fzkA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T56), H134 (= H135), Q137 (= Q138), T168 (= T169), R229 (= R230), P266 (= P267), L267 (= L268), 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)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2fzgA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S53), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), R167 (= R168), T168 (= T169), R229 (= R230), P266 (= P267), L267 (= L268)
2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2fzcA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S53), R54 (= R55), T55 (= T56), R105 (= R106), R167 (= R168), T168 (= T169), P266 (= P267), L267 (= L268)
2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2airA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S53), T53 (= T54), R54 (= R55), R105 (= R106)
- binding phosphoric acid mono(formamide)ester: R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135)
1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1za2A
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding phosphoric acid mono(formamide)ester: T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), R167 (= R168), T168 (= T169), L267 (= L268)
1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1r0cA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding n-carbamoyl-l-aspartate: S52 (= S53), R54 (= R55), R105 (= R106)
- binding phosphate ion: R105 (= R106), H134 (= H135), Q137 (= Q138)
1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1r0bA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding citrate anion: H134 (= H135), R167 (= R168), R229 (= R230), Q231 (= Q232), P266 (= P267), P268 (= P269)
- binding phosphate ion: S80 (= S81), K84 (= K85)
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2hseA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding aspartic acid: R54 (= R55), T55 (= T56), S58 (= S59), R105 (= R106), H134 (= H135), Q137 (= Q138), R167 (= R168), R229 (= R230), Q231 (= Q232), L267 (= L268), P268 (= P269), A289 (= A290), R296 (= R297)
- binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), L267 (= L268)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
100% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2a0fA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding phosphonoacetamide: R54 (= R55), T55 (= T56), H134 (= H135), Q137 (= Q138), L267 (= L268)
5vmqC Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution (see paper)
100% identity, 99% coverage: 2:310/311 of query aligns to 1:309/309 of 5vmqC
2at1A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral ph (see paper)
99% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2at1A
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding alpha-D-glucopyranose: R167 (= R168), R229 (= R230)
- binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), Q137 (= Q138)
1at1A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral p H (see paper)
99% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1at1A
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding malonate ion: H134 (= H135), R167 (= R168), R229 (= R230), Q231 (= Q232)
- binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), Q137 (= Q138)
1acmA Arginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, nmr and x-ray crystallography study (see paper)
98% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1acmA
- active site: A54 (≠ R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding n-(phosphonacetyl)-l-aspartic acid: S52 (= S53), T53 (= T54), T55 (= T56), R105 (= R106), H134 (= H135), R167 (= R168), R229 (= R230), L267 (= L268), P268 (= P269)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
53% identity, 96% coverage: 8:306/311 of query aligns to 5:305/307 of 1ml4A
- active site: R56 (= R55), T57 (= T56), K85 (= K85), R106 (= R106), H134 (= H135), Q137 (= Q138), T227 (= T229), P266 (= P267), G292 (= G293)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S53), T55 (= T54), R56 (= R55), T57 (= T56), R106 (= R106), H134 (= H135), R167 (= R168), T168 (= T169), R228 (= R230), L267 (= L268)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
49% identity, 95% coverage: 8:301/311 of query aligns to 2:296/304 of 4eknB
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)
45% identity, 97% coverage: 5:307/311 of query aligns to 1921:2224/2225 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)
44% identity, 97% coverage: 5:307/311 of query aligns to 3:306/307 of 5g1nE
- active site: R57 (= R55), T58 (= T56), K85 (= K85), R106 (= R106), H134 (= H135), Q137 (= Q138), T227 (= T229), P266 (= P267), G292 (= G293)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S53), T56 (= T54), R57 (= R55), T58 (= T56), S82 (≠ L82), K85 (= K85), R106 (= R106), H134 (= H135), R167 (= R168), R228 (= R230), Q230 (= Q232), M267 (≠ L268)
Query Sequence
>18270 FitnessBrowser__Keio:18270
MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSF
ETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFS
GNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKF
DGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSE
YANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQAL
LALVLNRDLVL
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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