SitesBLAST
Comparing WP_072910073.1 NCBI__GCF_900142125.1:WP_072910073.1 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)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 96% coverage: 6:302/310 of query aligns to 2:288/291 of 3r7fA
- active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L222), P249 (= P263), G277 (= G291)
- binding phosphoric acid mono(formamide)ester: S47 (= S56), T48 (= T57), R49 (= R58), T50 (= T59), R99 (= R108), H127 (= H136), Q130 (= Q139), P249 (= P263), A250 (≠ G264)
- binding phosphate ion: S11 (≠ T15), T12 (≠ P16), Q23 (≠ I27), K26 (= K30), E140 (= E149), R171 (≠ K180), K241 (= K255), H243 (≠ D257), K272 (≠ D286), K272 (≠ D286), K275 (≠ E289)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 96% coverage: 6:302/310 of query aligns to 2:288/291 of 3r7dA
- active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L222), P249 (= P263), G277 (= G291)
- binding phosphate ion: S11 (≠ T15), T12 (≠ P16), T73 (≠ S82), S74 (= S83), K77 (= K86), R171 (≠ K180)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 96% coverage: 6:302/310 of query aligns to 2:288/290 of 3r7lA
- active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L222), P249 (= P263), G277 (= G291)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S56), T48 (= T57), R49 (= R58), T50 (= T59), S74 (= S83), K77 (= K86), R99 (= R108), H127 (= H136), R160 (= R169), R211 (= R223), Q213 (= Q225), A250 (≠ G264)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
42% identity, 96% coverage: 6:302/310 of query aligns to 2:288/304 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.
42% identity, 95% coverage: 7:299/310 of query aligns to 3:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S56), T49 (= T57), R50 (= R58), T51 (= T59), S75 (= S83), K78 (= K86), R100 (= R108), H127 (= H136), R160 (= R169), R210 (= R223), Q212 (= Q225), A253 (≠ G264)
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)
40% identity, 95% coverage: 6:298/310 of query aligns to 2:285/291 of 4bjhB
- active site: R47 (= R58), T48 (= T59), K75 (= K86), R97 (≠ M107), H126 (= H136), Q129 (= Q139)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S56), T46 (= T57), R47 (= R58), T48 (= T59), R97 (≠ M107), H126 (= H136), R159 (= R169), V160 (= V170), R213 (= R223), Q215 (= Q225), G251 (= G264)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
40% identity, 95% coverage: 6:298/310 of query aligns to 2:285/291 of 3d6nB
- active site: R47 (= R58), T48 (= T59), K75 (= K86), R97 (≠ M107), H126 (= H136), Q129 (= Q139)
- binding citrate anion: T48 (= T59), R97 (≠ M107), H126 (= H136), R159 (= R169), V160 (= V170), R213 (= R223), G251 (= G264)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
36% identity, 96% coverage: 6:304/310 of query aligns to 6:305/307 of 5g1nE
- active site: R57 (= R58), T58 (= T59), K85 (= K86), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (≠ L222), P266 (= P263), G292 (= G291)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S56), T56 (= T57), R57 (= R58), T58 (= T59), S82 (= S83), K85 (= K86), R106 (= R108), H134 (= H136), R167 (= R169), R228 (= R223), Q230 (= Q225), M267 (≠ G264)
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, 96% coverage: 6:304/310 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.
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, 96% coverage: 6:304/310 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
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
34% identity, 96% coverage: 6:304/310 of query aligns to 3:290/292 of 5g1pA
- active site: R54 (= R58), T55 (= T59), K82 (= K86), R103 (= R108), H131 (= H136), Q134 (= Q139), T223 (≠ L222), P251 (= P263), G277 (= G291)
- binding phosphoric acid mono(formamide)ester: S52 (= S56), T53 (= T57), R54 (= R58), T55 (= T59), R103 (= R108), Q134 (= Q139), M252 (≠ G264)
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)
35% identity, 97% coverage: 6:305/310 of query aligns to 1923:2223/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
34% identity, 97% coverage: 2:301/310 of query aligns to 12:313/316 of 8bplA
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
37% identity, 97% coverage: 3:304/310 of query aligns to 2:305/307 of 1ml4A
- active site: R56 (= R58), T57 (= T59), K85 (= K86), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (≠ L222), P266 (= P263), G292 (= G291)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S56), T55 (= T57), R56 (= R58), T57 (= T59), R106 (= R108), H134 (= H136), R167 (= R169), T168 (≠ V170), R228 (= R223), L267 (≠ G264)
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)
35% identity, 97% coverage: 6:305/310 of query aligns to 1918:2219/2224 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
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
36% identity, 98% coverage: 3:305/310 of query aligns to 16:323/324 of 6yvbC
- active site: R121 (= R108), H149 (= H136), Q152 (= Q139), T243 (≠ L222), P283 (= P263), G309 (= G291)
- binding phosphoric acid mono(formamide)ester: S68 (= S56), T69 (= T57), R70 (= R58), T71 (= T59), R121 (= R108), H149 (= H136), Q152 (= Q139), P283 (= P263)
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
36% identity, 98% coverage: 3:305/310 of query aligns to 4:311/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
36% identity, 98% coverage: 3:305/310 of query aligns to 4:311/312 of 6ypoA
- active site: R109 (= R108), H137 (= H136), Q140 (= Q139), T231 (≠ L222), P271 (= P263), G297 (= G291)
- binding uridine-5'-monophosphate: R58 (= R58), T59 (= T59), R109 (= R108), H137 (= H136), R170 (= R169), T171 (≠ V170), R232 (= R223), H270 (= H262), P271 (= P263), L272 (≠ G264)
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 98% coverage: 3:305/310 of query aligns to 82:389/390 of P49077
- R136 (= R58) binding UMP
- T137 (= T59) binding UMP
- R187 (= R108) binding UMP
- H215 (= H136) binding UMP
- R248 (= R169) binding UMP
- R310 (= R223) binding UMP
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
35% identity, 96% coverage: 5:301/310 of query aligns to 6:302/310 of 2hseA
- active site: R54 (= R58), T55 (= T59), K84 (= K86), R105 (= R108), H134 (= H136), Q137 (= Q139), T228 (≠ L222), P266 (= P263), G292 (= G291)
- binding aspartic acid: R54 (= R58), T55 (= T59), S58 (= S62), R105 (= R108), H134 (= H136), Q137 (= Q139), R167 (= R169), R229 (= R223), Q231 (= Q225), L267 (≠ G264), P268 (= P265), A289 (≠ V288), R296 (= R295)
- binding phosphonoacetamide: S52 (= S56), T53 (= T57), R54 (= R58), T55 (= T59), R105 (= R108), L267 (≠ G264)
Query Sequence
>WP_072910073.1 NCBI__GCF_900142125.1:WP_072910073.1
MTFNHKHIIGIKDLTPEELTFILDTSISFKEINRRDIKKVPTLRGKTIINLFFEASTRTR
TSFEIAGKRLSADTINISASGSSVVKGETLEDTAKNIEAMNPDAIVMRHNASGACEYLAK
RLDCAIINAGDGMHEHPSQALLDAYTIREAKGKIEGLTVAIIGDITHSRVVRSNIYCLTK
LGAKVRVAGPGTMLPPGIERLGCEAYKNIDDAIKGSDVVMMLRIQRERQGAPLIPSVREY
SKFFGLTHARMKLAKEDAIVMHPGPINRGVELPTSIADGPQNVILDQVENGVAVRMALLY
LACGGEKLQD
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