SitesBLAST
Comparing H281DRAFT_04817 H281DRAFT_04817 aspartate carbamoyltransferase 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)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 87% coverage: 36:333/341 of query aligns to 1:285/291 of 3r7fA
- active site: R49 (= R89), T50 (= T90), K77 (= K117), R99 (= R139), H127 (= H169), Q130 (= Q172), L210 (= L256), P249 (= P297), G277 (= G325)
- binding phosphoric acid mono(formamide)ester: S47 (= S87), T48 (= T88), R49 (= R89), T50 (= T90), R99 (= R139), H127 (= H169), Q130 (= Q172), P249 (= P297), A250 (≠ G298)
- binding phosphate ion: S11 (≠ P46), T12 (≠ K47), Q23 (≠ S58), K26 (≠ V61), E140 (≠ H182), R171 (≠ T213), K241 (= K289), H243 (≠ D291), K272 (≠ N320), K272 (≠ N320), K275 (≠ T323)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 87% coverage: 36:333/341 of query aligns to 1:285/291 of 3r7dA
- active site: R49 (= R89), T50 (= T90), K77 (= K117), R99 (= R139), H127 (= H169), Q130 (= Q172), L210 (= L256), P249 (= P297), G277 (= G325)
- binding phosphate ion: S11 (≠ P46), T12 (≠ K47), T73 (≠ S113), S74 (= S114), K77 (= K117), R171 (≠ T213)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 87% coverage: 36:333/341 of query aligns to 1:285/290 of 3r7lA
- active site: R49 (= R89), T50 (= T90), K77 (= K117), R99 (= R139), H127 (= H169), Q130 (= Q172), L210 (= L256), P249 (= P297), G277 (= G325)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S87), T48 (= T88), R49 (= R89), T50 (= T90), S74 (= S114), K77 (= K117), R99 (= R139), H127 (= H169), R160 (= R202), R211 (= R257), Q213 (= Q259), A250 (≠ G298)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 87% coverage: 36:333/341 of query aligns to 1:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
39% identity, 87% coverage: 36:333/341 of query aligns to 1:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S87), T49 (= T88), R50 (= R89), T51 (= T90), S75 (= S114), K78 (= K117), R100 (= R139), H127 (= H169), R160 (= R202), R210 (= R257), Q212 (= Q259), A253 (≠ G298)
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)
39% identity, 87% coverage: 36:332/341 of query aligns to 1:285/291 of 4bjhB
- active site: R47 (= R89), T48 (= T90), K75 (= K117), R97 (= R139), H126 (= H169), Q129 (= Q172)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S87), T46 (= T88), R47 (= R89), T48 (= T90), R97 (= R139), H126 (= H169), R159 (= R202), V160 (= V203), R213 (= R257), Q215 (= Q259), G251 (= G298)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
39% identity, 87% coverage: 36:332/341 of query aligns to 1:285/291 of 3d6nB
- active site: R47 (= R89), T48 (= T90), K75 (= K117), R97 (= R139), H126 (= H169), Q129 (= Q172)
- binding citrate anion: T48 (= T90), R97 (= R139), H126 (= H169), R159 (= R202), V160 (= V203), R213 (= R257), G251 (= G298)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 89% coverage: 37:339/341 of query aligns to 6:306/307 of 5g1nE
- active site: R57 (= R89), T58 (= T90), K85 (= K117), R106 (= R139), H134 (= H169), Q137 (= Q172), T227 (≠ L256), P266 (= P297), G292 (= G325)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S87), T56 (= T88), R57 (= R89), T58 (= T90), S82 (= S114), K85 (= K117), R106 (= R139), H134 (= H169), R167 (= R202), R228 (= R257), Q230 (= Q259), M267 (≠ G298)
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)
36% identity, 89% coverage: 37:338/341 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
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)
36% identity, 89% coverage: 37:338/341 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.
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
34% identity, 89% coverage: 37:339/341 of query aligns to 3:291/292 of 5g1pA
- active site: R54 (= R89), T55 (= T90), K82 (= K117), R103 (= R139), H131 (= H169), Q134 (= Q172), T223 (≠ L256), P251 (= P297), G277 (= G325)
- binding phosphoric acid mono(formamide)ester: S52 (= S87), T53 (= T88), R54 (= R89), T55 (= T90), R103 (= R139), Q134 (= Q172), M252 (≠ G298)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
37% identity, 90% coverage: 36:341/341 of query aligns to 1:304/304 of 4eknB
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
35% identity, 89% coverage: 37:338/341 of query aligns to 5:305/307 of 1ml4A
- active site: R56 (= R89), T57 (= T90), K85 (= K117), R106 (= R139), H134 (= H169), Q137 (= Q172), T227 (≠ L256), P266 (= P297), G292 (= G325)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S87), T55 (= T88), R56 (= R89), T57 (= T90), R106 (= R139), H134 (= H169), R167 (= R202), T168 (≠ V203), R228 (= R257), L267 (≠ G298)
P05990 Multifunctional protein r; Protein rudimentary; 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 Drosophila melanogaster (Fruit fly) (see 2 papers)
34% identity, 89% coverage: 37:341/341 of query aligns to 1918:2221/2224 of P05990
Sites not aligning to the query:
- 1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
- 1883 modified: Phosphoserine
- 1885 modified: Phosphoserine
- 1892 modified: Phosphoserine
- 1894 modified: Phosphoserine
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
32% identity, 88% coverage: 38:336/341 of query aligns to 17:314/316 of 8bplA
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
34% identity, 88% coverage: 37:336/341 of query aligns to 7:303/310 of 2hseA
- active site: R54 (= R89), T55 (= T90), K84 (= K117), R105 (= R139), H134 (= H169), Q137 (= Q172), T228 (≠ L256), P266 (= P297), G292 (= G325)
- binding aspartic acid: R54 (= R89), T55 (= T90), S58 (≠ T93), R105 (= R139), H134 (= H169), Q137 (= Q172), R167 (= R202), R229 (= R257), Q231 (= Q259), L267 (≠ G298), P268 (= P299), A289 (≠ V322), R296 (= R329)
- binding phosphonoacetamide: S52 (= S87), T53 (= T88), R54 (= R89), T55 (= T90), R105 (= R139), L267 (≠ G298)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
34% identity, 88% coverage: 37:336/341 of query aligns to 7:303/310 of 2a0fA
- active site: R54 (= R89), T55 (= T90), K84 (= K117), R105 (= R139), H134 (= H169), Q137 (= Q172), T228 (≠ L256), P266 (= P297), G292 (= G325)
- binding phosphonoacetamide: R54 (= R89), T55 (= T90), H134 (= H169), Q137 (= Q172), L267 (≠ G298)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 88% coverage: 37:336/341 of query aligns to 8:304/311 of P0A786
- R55 (= R89) binding
- T56 (= T90) binding
- R106 (= R139) binding
- H135 (= H169) binding
- Q138 (= Q172) binding
- L268 (≠ G298) binding
- P269 (= P299) 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)
34% identity, 88% coverage: 37:336/341 of query aligns to 7:303/310 of 2ipoA
- active site: R54 (= R89), T55 (= T90), K84 (= K117), R105 (= R139), H134 (= H169), Q137 (= Q172), T228 (≠ L256), P266 (= P297), G292 (= G325)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S87), T53 (= T88), R54 (= R89), T55 (= T90), R105 (= R139), H134 (= H169), R167 (= R202), T168 (≠ V203), R229 (= R257), L267 (≠ G298)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
34% identity, 88% coverage: 37:336/341 of query aligns to 7:303/310 of 2h3eA
- active site: R54 (= R89), T55 (= T90), K84 (= K117), R105 (= R139), H134 (= H169), Q137 (= Q172), T228 (≠ L256), P266 (= P297), G292 (= G325)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S87), T53 (= T88), R54 (= R89), T55 (= T90), R105 (= R139), H134 (= H169), R167 (= R202), R229 (= R257), L267 (≠ G298)
Query Sequence
>H281DRAFT_04817 H281DRAFT_04817 aspartate carbamoyltransferase
MNTANQASHDQADSATERFRYGFLKGNPQLTKNGELKHLLSIEGLPKAIVNHILDTASQF
VSVTDREVKKVPLLRGKSVFNLFFENSTRTRTTFEIAATRLSADVLNLNINASSTSKGES
LLDTINNLSAMHADMFVVRHASSGAPYLIAQHCAPHVHVINAGDGRHAHPTQGLLDMYTI
RHYKKDFTNLRVAIVGDILHSRVARSDIHALTTLGVPEVRAIGPRTLLPGGLEQMGVRVF
HNLDEGLKDVDVIIMLRLQNERMSGALLPSAQEYFKSWGLTPERLALAKPDAIVMHPGPM
NRGVEIDSQVADGPQSVILNQVTFGIAVRMAVMGIVAGNND
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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