SitesBLAST
Comparing WP_013683809.1 NCBI__GCF_000194625.1:WP_013683809.1 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)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
60% identity, 98% coverage: 5:299/300 of query aligns to 5:304/307 of 1ml4A
- active site: R56 (= R56), T57 (= T57), K85 (= K85), R106 (= R106), H134 (= H134), Q137 (= Q137), T227 (= T222), P266 (= P261), G292 (= G287)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S54), T55 (= T55), R56 (= R56), T57 (= T57), R106 (= R106), H134 (= H134), R167 (= R166), T168 (= T167), R228 (= R223), L267 (= L262)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
60% identity, 99% coverage: 4:299/300 of query aligns to 1:300/304 of 4eknB
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)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2at1A
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding alpha-D-glucopyranose: R167 (= R166), R229 (= R223)
- binding phosphonoacetamide: S52 (= S54), T53 (= T55), R54 (= R56), T55 (= T57), R105 (= R106), H134 (= H134), Q137 (= Q137)
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)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 1at1A
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding malonate ion: H134 (= H134), R167 (= R166), R229 (= R223), Q231 (= Q225)
- binding phosphonoacetamide: S52 (= S54), T53 (= T55), R54 (= R56), T55 (= T57), R105 (= R106), H134 (= H134), Q137 (= Q137)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
49% identity, 98% coverage: 5:299/300 of query aligns to 8:305/311 of P0A786
- R55 (= R56) binding carbamoyl phosphate
- T56 (= T57) binding carbamoyl phosphate
- R106 (= R106) binding carbamoyl phosphate
- H135 (= H134) binding carbamoyl phosphate
- Q138 (= Q137) binding carbamoyl phosphate
- L268 (= L262) binding carbamoyl phosphate
- P269 (= P263) 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)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2ipoA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S54), T53 (= T55), R54 (= R56), T55 (= T57), R105 (= R106), H134 (= H134), R167 (= R166), T168 (= T167), R229 (= R223), L267 (= L262)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2h3eA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S54), T53 (= T55), R54 (= R56), T55 (= T57), R105 (= R106), H134 (= H134), R167 (= R166), R229 (= R223), L267 (= L262)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2fzkA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T57), H134 (= H134), Q137 (= Q137), T168 (= T167), R229 (= R223), P266 (= P261), L267 (= L262), R296 (= R291)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2fzgA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S54), R54 (= R56), T55 (= T57), R105 (= R106), H134 (= H134), R167 (= R166), T168 (= T167), R229 (= R223), P266 (= P261), L267 (= L262)
2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2fzcA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S54), R54 (= R56), T55 (= T57), R105 (= R106), R167 (= R166), T168 (= T167), P266 (= P261), L267 (= L262)
2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2airA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S54), T53 (= T55), R54 (= R56), R105 (= R106)
- binding phosphoric acid mono(formamide)ester: R54 (= R56), T55 (= T57), R105 (= R106), H134 (= H134)
1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 1za2A
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding phosphoric acid mono(formamide)ester: T53 (= T55), R54 (= R56), T55 (= T57), R105 (= R106), R167 (= R166), T168 (= T167), L267 (= L262)
1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 1r0cA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding n-carbamoyl-l-aspartate: S52 (= S54), R54 (= R56), R105 (= R106)
- binding phosphate ion: R105 (= R106), H134 (= H134), Q137 (= Q137)
1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 1r0bA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding citrate anion: H134 (= H134), R167 (= R166), R229 (= R223), Q231 (= Q225), P266 (= P261), P268 (= P263)
- binding phosphate ion: S80 (= S82), K84 (vs. gap)
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)
49% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 1acmA
- active site: A54 (≠ R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding n-(phosphonacetyl)-l-aspartic acid: S52 (= S54), T53 (= T55), T55 (= T57), R105 (= R106), H134 (= H134), R167 (= R166), R229 (= R223), L267 (= L262), P268 (= P263)
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
48% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2hseA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding aspartic acid: R54 (= R56), T55 (= T57), S58 (= S60), R105 (= R106), H134 (= H134), Q137 (= Q137), R167 (= R166), R229 (= R223), Q231 (= Q225), L267 (= L262), P268 (= P263), A289 (= A284), R296 (= R291)
- binding phosphonoacetamide: S52 (= S54), T53 (= T55), R54 (= R56), T55 (= T57), R105 (= R106), L267 (= L262)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
48% identity, 98% coverage: 5:299/300 of query aligns to 7:304/310 of 2a0fA
- active site: R54 (= R56), T55 (= T57), K84 (vs. gap), R105 (= R106), H134 (= H134), Q137 (= Q137), T228 (= T222), P266 (= P261), G292 (= G287)
- binding phosphonoacetamide: R54 (= R56), T55 (= T57), H134 (= H134), Q137 (= Q137), L267 (= L262)
5vmqC Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution (see paper)
48% identity, 98% coverage: 5:299/300 of query aligns to 7:304/309 of 5vmqC
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)
49% identity, 98% coverage: 5:299/300 of query aligns to 1937:2237/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
44% identity, 98% coverage: 5:299/300 of query aligns to 6:304/307 of 5g1nE
- active site: R57 (= R56), T58 (= T57), K85 (= K85), R106 (= R106), H134 (= H134), Q137 (= Q137), T227 (= T222), P266 (= P261), G292 (= G287)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S54), T56 (= T55), R57 (= R56), T58 (= T57), S82 (= S82), K85 (= K85), R106 (= R106), H134 (= H134), R167 (= R166), R228 (= R223), Q230 (= Q225), M267 (≠ L262)
Query Sequence
>WP_013683809.1 NCBI__GCF_000194625.1:WP_013683809.1
MTRFRHLISIDDLSKDDILYILDKAEEFEEIARGKTKSRTLEGKLLANLFFEPSTRTRMS
FEAAMKRLGGDVINMTAQEASSVAKGETLADTIRVVGKYADAIVLRHPLEGAARFAAEHS
EVPVINAGDGAGQHPTQTLLDLYTIRKESSLDELKIALMGDLKYSRTVHSLIKALTLFDA
EIYLVSPPSLALPEEFLEGIGGKITTAELDEILEEIDVLYVTRIQKERFPDEEEYRKVAG
SYKVDAETLKRAKDSLIVMHPLPRVDEIDVSVDATKHAKYFQQAFYGVPVRMAILSEVML
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