SitesBLAST
Comparing WP_028996415.1 NCBI__GCF_000430725.1:WP_028996415.1 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)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 93% coverage: 17:312/320 of query aligns to 3:285/290 of 3r7lA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H148), Q130 (= Q151), L210 (= L235), P249 (= P276), G277 (= G304)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S66), T48 (= T67), R49 (= R68), T50 (= T69), S74 (= S93), K77 (= K96), R99 (= R118), H127 (= H148), R160 (= R181), R211 (= R236), Q213 (= Q238), A250 (≠ G277)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 93% coverage: 17:312/320 of query aligns to 3:285/291 of 3r7fA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H148), Q130 (= Q151), L210 (= L235), P249 (= P276), G277 (= G304)
- binding phosphoric acid mono(formamide)ester: S47 (= S66), T48 (= T67), R49 (= R68), T50 (= T69), R99 (= R118), H127 (= H148), Q130 (= Q151), P249 (= P276), A250 (≠ G277)
- binding phosphate ion: S11 (≠ P25), T12 (≠ R26), Q23 (≠ S37), K26 (≠ A41), E140 (≠ H161), R171 (≠ T192), K241 (= K268), H243 (≠ D270), K272 (≠ P299), K272 (≠ P299), K275 (≠ T302)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 93% coverage: 17:312/320 of query aligns to 3:285/291 of 3r7dA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H148), Q130 (= Q151), L210 (= L235), P249 (= P276), G277 (= G304)
- binding phosphate ion: S11 (≠ P25), T12 (≠ R26), T73 (≠ S92), S74 (= S93), K77 (= K96), R171 (≠ T192)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
42% identity, 93% coverage: 17:312/320 of query aligns to 3:285/304 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, 93% coverage: 17:312/320 of query aligns to 3:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S66), T49 (= T67), R50 (= R68), T51 (= T69), S75 (= S93), K78 (= K96), R100 (= R118), H127 (= H148), R160 (= R181), R210 (= R236), Q212 (= Q238), A253 (≠ G277)
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, 93% coverage: 18:315/320 of query aligns to 4:289/291 of 4bjhB
- active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H148), Q129 (= Q151)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S66), T46 (= T67), R47 (= R68), T48 (= T69), R97 (= R118), H126 (= H148), R159 (= R181), V160 (= V182), R213 (= R236), Q215 (= Q238), G251 (= G277)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
39% identity, 93% coverage: 18:315/320 of query aligns to 4:289/291 of 3d6nB
- active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H148), Q129 (= Q151)
- binding citrate anion: T48 (= T69), R97 (= R118), H126 (= H148), R159 (= R181), V160 (= V182), R213 (= R236), G251 (= G277)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 94% coverage: 17:317/320 of query aligns to 7:305/307 of 5g1nE
- active site: R57 (= R68), T58 (= T69), K85 (= K96), R106 (= R118), H134 (= H148), Q137 (= Q151), T227 (≠ L235), P266 (= P276), G292 (= G304)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S66), T56 (= T67), R57 (= R68), T58 (= T69), S82 (= S93), K85 (= K96), R106 (= R118), H134 (= H148), R167 (= R181), R228 (= R236), Q230 (= Q238), M267 (≠ G277)
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, 94% coverage: 17:317/320 of query aligns to 1925:2223/2225 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
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, 94% coverage: 17:317/320 of query aligns to 1925:2223/2225 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, 94% coverage: 17:317/320 of query aligns to 4:290/292 of 5g1pA
- active site: R54 (= R68), T55 (= T69), K82 (= K96), R103 (= R118), H131 (= H148), Q134 (= Q151), T223 (≠ L235), P251 (= P276), G277 (= G304)
- binding phosphoric acid mono(formamide)ester: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R103 (= R118), Q134 (= Q151), M252 (≠ G277)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
36% identity, 86% coverage: 44:317/320 of query aligns to 29:305/307 of 1ml4A
- active site: R56 (= R68), T57 (= T69), K85 (= K96), R106 (= R118), H134 (= H148), Q137 (= Q151), T227 (≠ L235), P266 (= P276), G292 (= G304)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S66), T55 (= T67), R56 (= R68), T57 (= T69), R106 (= R118), H134 (= H148), R167 (= R181), T168 (≠ V182), R228 (= R236), L267 (≠ G277)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
34% identity, 95% coverage: 17:319/320 of query aligns to 3:304/304 of 4eknB
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, 94% coverage: 17:317/320 of query aligns to 1919:2218/2224 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
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 94% coverage: 14:315/320 of query aligns to 83:386/390 of P49077
- R136 (= R68) binding UMP
- T137 (= T69) binding UMP
- R187 (= R118) binding UMP
- H215 (= H148) binding UMP
- R248 (= R181) binding UMP
- R310 (= R236) binding UMP
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
33% identity, 94% coverage: 14:315/320 of query aligns to 5:308/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
33% identity, 94% coverage: 14:315/320 of query aligns to 5:308/312 of 6ypoA
- active site: R109 (= R118), H137 (= H148), Q140 (= Q151), T231 (≠ L235), P271 (= P276), G297 (= G304)
- binding uridine-5'-monophosphate: R58 (= R68), T59 (= T69), R109 (= R118), H137 (= H148), R170 (= R181), T171 (≠ V182), R232 (= R236), H270 (= H275), P271 (= P276), L272 (≠ G277)
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
33% identity, 94% coverage: 14:315/320 of query aligns to 17:320/324 of 6yvbC
- active site: R121 (= R118), H149 (= H148), Q152 (= Q151), T243 (≠ L235), P283 (= P276), G309 (= G304)
- binding phosphoric acid mono(formamide)ester: S68 (= S66), T69 (= T67), R70 (= R68), T71 (= T69), R121 (= R118), H149 (= H148), Q152 (= Q151), P283 (= P276)
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
32% identity, 93% coverage: 17:315/320 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
35% identity, 95% coverage: 17:319/320 of query aligns to 8:307/310 of 2hseA
- active site: R54 (= R68), T55 (= T69), K84 (vs. gap), R105 (= R118), H134 (= H148), Q137 (= Q151), T228 (≠ L235), P266 (= P276), G292 (= G304)
- binding aspartic acid: R54 (= R68), T55 (= T69), S58 (≠ T72), R105 (= R118), H134 (= H148), Q137 (= Q151), R167 (= R181), R229 (= R236), Q231 (= Q238), L267 (≠ G277), P268 (= P278), A289 (≠ V301), R296 (= R308)
- binding phosphonoacetamide: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R105 (= R118), L267 (≠ G277)
Query Sequence
>WP_028996415.1 NCBI__GCF_000430725.1:WP_028996415.1
MLSRRNPQLNSHGELIHLLSTEGLPRAVLTQILDTASTFLAVGEREIKKVPLLRGKSVFN
LFFENSTRTRTTFEIAAKRLSADVINLDIARSSTAKGESLLDTIANLSAMQADMFVVRHS
ESGAPYLIAQHCAPHVHVVNAGDGRHAHPTQGLLDMYTIRHFKKDFTNLTVAIVGDIVHS
RVARSDIHALTTLGVPEIRAVGPTTLVPDNLREMGVRVCRDMAEGIRDADVIIMLRLQNE
RMGSALLPSAGEFFKHYGLTPEKLALAKPDAIVMHPGPINRGVEIDSAVADGRHSVILPQ
VTFGIAVRMAVMSIIAGNDA
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