SitesBLAST
Comparing WP_057508242.1 NCBI__GCF_001431535.1:WP_057508242.1 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)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
39% identity, 95% coverage: 12:312/316 of query aligns to 1:286/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 95% coverage: 12:312/316 of query aligns to 1:286/290 of 3r7lA
- active site: R49 (= R66), T50 (= T67), K77 (= K94), R99 (= R116), H127 (= H146), Q130 (= Q149), L210 (= L234), P249 (= P275), G277 (= G303)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S64), T48 (= T65), R49 (= R66), T50 (= T67), S74 (= S91), K77 (= K94), R99 (= R116), H127 (= H146), R160 (= R180), R211 (= R235), Q213 (= Q237), A250 (≠ G276)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 95% coverage: 12:312/316 of query aligns to 1:286/291 of 3r7fA
- active site: R49 (= R66), T50 (= T67), K77 (= K94), R99 (= R116), H127 (= H146), Q130 (= Q149), L210 (= L234), P249 (= P275), G277 (= G303)
- binding phosphoric acid mono(formamide)ester: S47 (= S64), T48 (= T65), R49 (= R66), T50 (= T67), R99 (= R116), H127 (= H146), Q130 (= Q149), P249 (= P275), A250 (≠ G276)
- binding phosphate ion: S11 (≠ P22), T12 (≠ R23), Q23 (≠ G34), K26 (≠ R37), E140 (≠ Q159), R171 (≠ T191), K241 (≠ G267), H243 (≠ D269), K272 (≠ R298), K272 (≠ R298), K275 (≠ A301)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 95% coverage: 12:312/316 of query aligns to 1:286/291 of 3r7dA
- active site: R49 (= R66), T50 (= T67), K77 (= K94), R99 (= R116), H127 (= H146), Q130 (= Q149), L210 (= L234), P249 (= P275), G277 (= G303)
- binding phosphate ion: S11 (≠ P22), T12 (≠ R23), T73 (≠ S90), S74 (= S91), K77 (= K94), R171 (≠ T191)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
37% identity, 96% coverage: 12:315/316 of query aligns to 1:292/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S64), T49 (= T65), R50 (= R66), T51 (= T67), S75 (= S91), K78 (= K94), R100 (= R116), H127 (= H146), R160 (= R180), R210 (= R235), Q212 (= Q237), A253 (≠ G276)
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)
36% identity, 96% coverage: 12:315/316 of query aligns to 1:290/291 of 4bjhB
- active site: R47 (= R66), T48 (= T67), K75 (= K94), R97 (≠ H117), H126 (= H146), Q129 (= Q149)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S64), T46 (= T65), R47 (= R66), T48 (= T67), R97 (≠ H117), H126 (= H146), R159 (= R180), V160 (= V181), R213 (= R235), Q215 (= Q237), G251 (= G276)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
36% identity, 96% coverage: 12:315/316 of query aligns to 1:290/291 of 3d6nB
- active site: R47 (= R66), T48 (= T67), K75 (= K94), R97 (≠ H117), H126 (= H146), Q129 (= Q149)
- binding citrate anion: T48 (= T67), R97 (≠ H117), H126 (= H146), R159 (= R180), V160 (= V181), R213 (= R235), G251 (= G276)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 96% coverage: 13:316/316 of query aligns to 6:305/307 of 5g1nE
- active site: R57 (= R66), T58 (= T67), K85 (= K94), R106 (= R116), H134 (= H146), Q137 (= Q149), T227 (≠ L234), P266 (= P275), G292 (= G303)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S64), T56 (= T65), R57 (= R66), T58 (= T67), S82 (= S91), K85 (= K94), R106 (= R116), H134 (= H146), R167 (= R180), R228 (= R235), Q230 (= Q237), M267 (≠ G276)
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
35% identity, 96% coverage: 13:316/316 of query aligns to 3:290/292 of 5g1pA
- active site: R54 (= R66), T55 (= T67), K82 (= K94), R103 (= R116), H131 (= H146), Q134 (= Q149), T223 (≠ L234), P251 (= P275), G277 (= G303)
- binding phosphoric acid mono(formamide)ester: S52 (= S64), T53 (= T65), R54 (= R66), T55 (= T67), R103 (= R116), Q134 (= Q149), M252 (≠ G276)
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: 13:316/316 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 ; 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
P20054 Multifunctional protein pyr1-3; 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 Dictyostelium discoideum (Social amoeba)
33% identity, 98% coverage: 7:316/316 of query aligns to 1917:2222/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
34% identity, 96% coverage: 12:315/316 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)
32% identity, 96% coverage: 13:316/316 of query aligns to 7:305/310 of 2at1A
- active site: R54 (= R66), T55 (= T67), K84 (= K94), R105 (= R116), H134 (= H146), Q137 (= Q149), T228 (≠ L234), P266 (= P275), G292 (= G303)
- binding alpha-D-glucopyranose: R167 (= R180), R229 (= R235)
- binding phosphonoacetamide: S52 (= S64), T53 (= T65), R54 (= R66), T55 (= T67), R105 (= R116), H134 (= H146), Q137 (= Q149)
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)
32% identity, 96% coverage: 13:316/316 of query aligns to 7:305/310 of 1at1A
- active site: R54 (= R66), T55 (= T67), K84 (= K94), R105 (= R116), H134 (= H146), Q137 (= Q149), T228 (≠ L234), P266 (= P275), G292 (= G303)
- binding malonate ion: H134 (= H146), R167 (= R180), R229 (= R235), Q231 (= Q237)
- binding phosphonoacetamide: S52 (= S64), T53 (= T65), R54 (= R66), T55 (= T67), R105 (= R116), H134 (= H146), Q137 (= Q149)
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: 13:316/316 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.
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)
32% identity, 96% coverage: 13:316/316 of query aligns to 7:305/310 of 1acmA
- active site: A54 (≠ R66), T55 (= T67), K84 (= K94), R105 (= R116), H134 (= H146), Q137 (= Q149), T228 (≠ L234), P266 (= P275), G292 (= G303)
- binding n-(phosphonacetyl)-l-aspartic acid: S52 (= S64), T53 (= T65), T55 (= T67), R105 (= R116), H134 (= H146), R167 (= R180), R229 (= R235), L267 (≠ G276), P268 (= P277)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
37% identity, 84% coverage: 53:316/316 of query aligns to 43:305/307 of 1ml4A
- active site: R56 (= R66), T57 (= T67), K85 (= K94), R106 (= R116), H134 (= H146), Q137 (= Q149), T227 (≠ L234), P266 (= P275), G292 (= G303)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S64), T55 (= T65), R56 (= R66), T57 (= T67), R106 (= R116), H134 (= H146), R167 (= R180), T168 (≠ V181), R228 (= R235), L267 (≠ G276)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 96% coverage: 13:316/316 of query aligns to 8:306/311 of P0A786
- R55 (= R66) binding
- T56 (= T67) binding
- R106 (= R116) binding
- H135 (= H146) binding
- Q138 (= Q149) binding
- L268 (≠ G276) binding
- P269 (= P277) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
31% identity, 96% coverage: 13:316/316 of query aligns to 7:305/310 of 2ipoA
- active site: R54 (= R66), T55 (= T67), K84 (= K94), R105 (= R116), H134 (= H146), Q137 (= Q149), T228 (≠ L234), P266 (= P275), G292 (= G303)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S64), T53 (= T65), R54 (= R66), T55 (= T67), R105 (= R116), H134 (= H146), R167 (= R180), T168 (≠ V181), R229 (= R235), L267 (≠ G276)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
31% identity, 96% coverage: 13:316/316 of query aligns to 7:305/310 of 2h3eA
- active site: R54 (= R66), T55 (= T67), K84 (= K94), R105 (= R116), H134 (= H146), Q137 (= Q149), T228 (≠ L234), P266 (= P275), G292 (= G303)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S64), T53 (= T65), R54 (= R66), T55 (= T67), R105 (= R116), H134 (= H146), R167 (= R180), R229 (= R235), L267 (≠ G276)
Query Sequence
>WP_057508242.1 NCBI__GCF_001431535.1:WP_057508242.1
MTASQLDSSGRLRHLLTLQGLPRETLLQLLDRAGQIRDAAVGRVGNKRAVLAGSAVCTLF
FEPSTRTRSSFQLAAQRLGADVLNFDASTSSTRKGETATDTLRNLEAMGVRGFVVRHPDD
GAVAALAAAAGEGTALINAGDGRSSHPTQGLLDMLTLRQAKGSDFSKMKVVIVGDVKHSR
VARTDLHALRTLGVGEIRVCGPQSLLPDDDTLKGCVVGQDFDEMLEGADALMMLRLQRER
MEEGLVPSLEQYHQQYGLHAARLARAGKDAAVLHPGPINRGVEVTDEVADGPQSWVLRQV
ANGVAVRMAVLETLLG
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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