SitesBLAST
Comparing BWI76_RS03010 FitnessBrowser__Koxy:BWI76_RS03010 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)
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
90% identity, 100% coverage: 1:334/334 of query aligns to 1:334/334 of P04391
- M1 (= M1) modified: Initiator methionine, Removed
- S56 (= S56) mutation to H: Much less active than the wild-type.
- STRT 56:59 (= STRT 56:59) binding carbamoyl phosphate
- R58 (= R58) mutation to G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate.
- Q83 (= Q83) binding carbamoyl phosphate
- K87 (= K87) mutation to Q: Much less active than the wild-type.
- R107 (= R107) binding carbamoyl phosphate
- HPTQ 134:137 (= HPTQ 134:137) binding carbamoyl phosphate
- N168 (= N168) binding L-ornithine
- D232 (= D232) binding L-ornithine
- SM 236:237 (= SM 236:237) binding L-ornithine
- C274 (= C274) binding Zn(2+); mutation to A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization.
- CL 274:275 (= CL 274:275) binding carbamoyl phosphate
- R320 (= R320) binding carbamoyl phosphate; mutation to A: Much less active than the wild-type.
- A326 (= A326) mutation to G: Activity greater than the wild-type and Km for ornithwinas increases about twofold.
1duvG Crystal structure of e. Coli ornithine transcarbamoylase complexed with ndelta-l-ornithine-diaminophosphinyl-n-sulphonic acid (psorn) (see paper)
89% identity, 100% coverage: 2:334/334 of query aligns to 1:333/333 of 1duvG
- binding ndelta-(n'-sulphodiaminophosphinyl)-l-ornithine: S55 (= S56), T56 (= T57), R57 (= R58), T58 (= T59), R106 (= R107), L128 (= L129), H133 (= H134), N167 (= N168), D231 (= D232), S235 (= S236), M236 (= M237), C273 (= C274), L274 (= L275), R319 (= R320)
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
89% identity, 100% coverage: 2:334/334 of query aligns to 1:333/333 of 2otcA
- active site: R57 (= R58), T58 (= T59), H85 (= H86), R106 (= R107), H133 (= H134), Q136 (= Q137), D231 (= D232), C273 (= C274), R319 (= R320)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S56), T56 (= T57), R57 (= R58), T58 (= T59), R106 (= R107), H133 (= H134), N167 (= N168), D231 (= D232), S235 (= S236), M236 (= M237), L274 (= L275), R319 (= R320)
4jfrB Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate
67% identity, 98% coverage: 7:333/334 of query aligns to 14:339/340 of 4jfrB
- active site: R65 (= R58), T66 (= T59), D93 (≠ H86), R114 (= R107), H141 (= H134), Q144 (= Q137), D239 (= D232), C281 (= C274), R326 (= R320)
- binding phosphoric acid mono(formamide)ester: S63 (= S56), T64 (= T57), R65 (= R58), T66 (= T59), R114 (= R107), H141 (= H134), Q144 (= Q137), C281 (= C274), R326 (= R320)
4jqoA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with citrulline and inorganic phosphate
67% identity, 98% coverage: 7:333/334 of query aligns to 12:337/338 of 4jqoA
- active site: R63 (= R58), T64 (= T59), D91 (≠ H86), R112 (= R107), H139 (= H134), Q142 (= Q137), D237 (= D232), C279 (= C274), R324 (= R320)
- binding citrulline: H139 (= H134), Q142 (= Q137), N173 (= N168), D237 (= D232), S241 (= S236), M242 (= M237), C279 (= C274), L280 (= L275), R324 (= R320)
4jhxA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoylphosphate and arginine
67% identity, 98% coverage: 7:333/334 of query aligns to 10:335/336 of 4jhxA
- active site: R61 (= R58), T62 (= T59), D89 (≠ H86), R110 (= R107), H137 (= H134), Q140 (= Q137), D235 (= D232), C277 (= C274), R322 (= R320)
- binding arginine: L132 (= L129), N171 (= N168), D235 (= D232), S239 (= S236), M240 (= M237), P279 (= P276)
- binding phosphoric acid mono(formamide)ester: S59 (= S56), T60 (= T57), R61 (= R58), T62 (= T59), R110 (= R107), H137 (= H134), C277 (= C274), L278 (= L275), R322 (= R320)
Q8DCF5 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Vibrio vulnificus (strain CMCP6)
67% identity, 98% coverage: 7:333/334 of query aligns to 8:333/334 of Q8DCF5
- STRT 57:60 (= STRT 56:59) binding carbamoyl phosphate
- Q84 (= Q83) binding carbamoyl phosphate
- R108 (= R107) binding carbamoyl phosphate
- HPTQ 135:138 (= HPTQ 134:137) binding carbamoyl phosphate
- N169 (= N168) binding L-ornithine
- D233 (= D232) binding L-ornithine
- SM 237:238 (= SM 236:237) binding L-ornithine
- CL 275:276 (= CL 274:275) binding carbamoyl phosphate
- R320 (= R320) binding carbamoyl phosphate
4h31A Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate and l-norvaline
67% identity, 98% coverage: 7:333/334 of query aligns to 10:335/335 of 4h31A
- active site: R61 (= R58), T62 (= T59), D89 (≠ H86), R110 (= R107), H137 (= H134), Q140 (= Q137), D235 (= D232), C277 (= C274), R322 (= R320)
- binding phosphoric acid mono(formamide)ester: S59 (= S56), T60 (= T57), R61 (= R58), T62 (= T59), R110 (= R107), H137 (= H134), Q140 (= Q137), C277 (= C274), L278 (= L275), R322 (= R320)
- binding norvaline: L132 (= L129), N171 (= N168), D235 (= D232), S239 (= S236), M240 (= M237)
P08308 Ornithine carbamoyltransferase, catabolic; OTCase; EC 2.1.3.3 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 4 papers)
59% identity, 99% coverage: 5:333/334 of query aligns to 6:334/336 of P08308
- E106 (≠ Q105) mutation E->A,G: Loss of homotropic cooperativity; gain of anabolic activity. Conformational change which modifies the catalytic site. This mutant is blocked in the active R (relaxed) state.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q8G998 Ornithine carbamoyltransferase, catabolic; OTCase; EC 2.1.3.3 from Lentilactobacillus hilgardii (Lactobacillus hilgardii) (see paper)
49% identity, 99% coverage: 2:333/334 of query aligns to 8:336/343 of Q8G998
- H79 (≠ R73) binding Ni(2+)
Sites not aligning to the query:
- 337:343 mutation Missing: It generates a metastable mutant that behaves as a mixture of monomeric and trimeric species with only the latter exhibiting OTC activity.
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
40% identity, 98% coverage: 7:333/334 of query aligns to 8:311/315 of Q51742
- W22 (≠ T21) mutation to A: Decreased heat stability.
- E26 (= E25) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ R29) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ D33) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y230) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ K243) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E300) mutation to G: Becomes active at low temperatures; when associated with C-228 or D-241.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
38% identity, 97% coverage: 7:330/334 of query aligns to 12:307/316 of Q81M99
- STRT 57:60 (= STRT 56:59) binding carbamoyl phosphate
- Q84 (= Q83) binding carbamoyl phosphate
- R108 (= R107) binding carbamoyl phosphate
- HPCQ 135:138 (≠ HPTQ 134:137) binding carbamoyl phosphate
- N166 (= N168) binding L-ornithine
- D230 (= D232) binding L-ornithine
- SM 234:235 (= SM 236:237) binding L-ornithine
- CL 269:270 (= CL 274:275) binding carbamoyl phosphate
- R297 (= R320) binding carbamoyl phosphate
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
38% identity, 97% coverage: 7:329/334 of query aligns to 4:302/308 of 7nouA
- active site: R102 (= R107), H129 (= H134), Q132 (= Q137), D225 (= D232), C265 (= C274), R293 (= R320)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (= I51), T52 (= T57), R53 (= R58), R53 (= R58), F56 (≠ C61), F56 (≠ C61), L79 (≠ I84), D82 (≠ K87), E83 (= E88), V91 (= V96), Y95 (≠ M100), L266 (= L275), R293 (= R320)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
38% identity, 97% coverage: 7:329/334 of query aligns to 4:302/308 of 7nosA