SitesBLAST
Comparing WP_055068652.1 NCBI__GCF_001406815.1:WP_055068652.1 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)
51% identity, 99% coverage: 2:303/306 of query aligns to 5:306/307 of 1ml4A
- active site: R56 (= R51), T57 (= T52), K85 (= K80), R106 (= R101), H134 (= H129), Q137 (= Q132), T227 (= T224), P266 (= P263), G292 (= G289)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S49), T55 (= T50), R56 (= R51), T57 (= T52), R106 (= R101), H134 (= H129), R167 (= R162), T168 (= T163), R228 (= R225), L267 (= L264)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
51% identity, 98% coverage: 1:301/306 of query aligns to 1:300/304 of 4eknB
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
46% identity, 98% coverage: 2:302/306 of query aligns to 8:306/311 of P0A786
- R55 (= R51) binding carbamoyl phosphate
- T56 (= T52) binding carbamoyl phosphate
- R106 (= R101) binding carbamoyl phosphate
- H135 (= H129) binding carbamoyl phosphate
- Q138 (= Q132) binding carbamoyl phosphate
- L268 (= L264) binding carbamoyl phosphate
- P269 (= P265) binding carbamoyl phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2hseA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding aspartic acid: R54 (= R51), T55 (= T52), S58 (= S55), R105 (= R101), H134 (= H129), Q137 (= Q132), R167 (= R162), R229 (= R225), Q231 (= Q227), L267 (= L264), P268 (= P265), A289 (≠ V286), R296 (= R293)
- binding phosphonoacetamide: S52 (= S49), T53 (= T50), R54 (= R51), T55 (= T52), R105 (= R101), L267 (= L264)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2a0fA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding phosphonoacetamide: R54 (= R51), T55 (= T52), H134 (= H129), Q137 (= Q132), L267 (= L264)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
47% identity, 98% coverage: 2:302/306 of query aligns to 6:305/307 of 5g1nE
- active site: R57 (= R51), T58 (= T52), K85 (= K80), R106 (= R101), H134 (= H129), Q137 (= Q132), T227 (= T224), P266 (= P263), G292 (= G289)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S49), T56 (= T50), R57 (= R51), T58 (= T52), S82 (= S77), K85 (= K80), R106 (= R101), H134 (= H129), R167 (= R162), R228 (= R225), Q230 (= Q227), M267 (≠ L264)
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2ipoA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S49), T53 (= T50), R54 (= R51), T55 (= T52), R105 (= R101), H134 (= H129), R167 (= R162), T168 (= T163), R229 (= R225), L267 (= L264)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2h3eA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S49), T53 (= T50), R54 (= R51), T55 (= T52), R105 (= R101), H134 (= H129), R167 (= R162), R229 (= R225), L267 (= L264)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2fzkA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T52), H134 (= H129), Q137 (= Q132), T168 (= T163), R229 (= R225), P266 (= P263), L267 (= L264), R296 (= R293)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2fzgA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S49), R54 (= R51), T55 (= T52), R105 (= R101), H134 (= H129), R167 (= R162), T168 (= T163), R229 (= R225), P266 (= P263), L267 (= L264)
2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2fzcA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S49), R54 (= R51), T55 (= T52), R105 (= R101), R167 (= R162), T168 (= T163), P266 (= P263), L267 (= L264)
2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2airA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S49), T53 (= T50), R54 (= R51), R105 (= R101)
- binding phosphoric acid mono(formamide)ester: R54 (= R51), T55 (= T52), R105 (= R101), H134 (= H129)
1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 1za2A
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding phosphoric acid mono(formamide)ester: T53 (= T50), R54 (= R51), T55 (= T52), R105 (= R101), R167 (= R162), T168 (= T163), L267 (= L264)
1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 1r0cA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding n-carbamoyl-l-aspartate: S52 (= S49), R54 (= R51), R105 (= R101)
- binding phosphate ion: R105 (= R101), H134 (= H129), Q137 (= Q132)
1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
46% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 1r0bA
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding citrate anion: H134 (= H129), R167 (= R162), R229 (= R225), Q231 (= Q227), P266 (= P263), P268 (= P265)
- binding phosphate ion: S80 (= S76), K84 (= K80)
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)
45% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 2at1A
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding alpha-D-glucopyranose: R167 (= R162), R229 (= R225)
- binding phosphonoacetamide: S52 (= S49), T53 (= T50), R54 (= R51), T55 (= T52), R105 (= R101), H134 (= H129), Q137 (= Q132)
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)
45% identity, 98% coverage: 2:302/306 of query aligns to 7:305/310 of 1at1A
- active site: R54 (= R51), T55 (= T52), K84 (= K80), R105 (= R101), H134 (= H129), Q137 (= Q132), T228 (= T224), P266 (= P263), G292 (= G289)
- binding malonate ion: H134 (= H129), R167 (= R162), R229 (= R225), Q231 (= Q227)
- binding phosphonoacetamide: S52 (= S49), T53 (= T50), R54 (= R51), T55 (= T52), R105 (= R101), H134 (= H129), Q137 (= Q132)
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)
47% identity, 98% coverage: 2:302/306 of query aligns to 1924:2223/2225 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 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
5vmqC Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution (see paper)
45% identity, 98% coverage: 2:302/306 of query aligns to 7:305/309 of 5vmqC
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)
47% identity, 98% coverage: 2:302/306 of query aligns to 1924:2223/2225 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.
Query Sequence
>WP_055068652.1 NCBI__GCF_001406815.1:WP_055068652.1
MRHLMSPLDFSVEELDQLLDLASDIEKHPKKYAHACDGKKLATCFYEPSTRTRLSFEAAM
LNLGGSVLGFASADSSSASKGESISDTIRVISCYADICAMRHPKEGAALVASQKSRIPVI
NAGDGGHQHPTQTLTDLMTIRSLKGRLGNITIGLCGDLKFGRTVHSLINALIRYENVKFI
LISPEELKIPDYIREDVLQANHVEFEEVERLEDAMSQLDVLYMTRVQRERFFNEEDYIRL
KDFYILTKEKMELAKDDMIVLHPLPRVNEISVEVDDDPRAAYFTQVQNGVYVRMALILTL
LGIEVE
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