SitesBLAST
Comparing PfGW456L13_1873 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1873 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)
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)
89% identity, 100% coverage: 1:336/336 of query aligns to 1:336/336 of P08308
- M1 (= M1) modified: Initiator methionine, Removed
- E106 (= E106) 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.
4jqoA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with citrulline and inorganic phosphate
63% identity, 99% coverage: 1:334/336 of query aligns to 5:337/338 of 4jqoA
- active site: R63 (= R59), T64 (= T60), D91 (≠ H87), R112 (= R108), H139 (= H135), Q142 (= Q138), D237 (= D232), C279 (= C274), R324 (= R321)
- binding citrulline: H139 (= H135), Q142 (= Q138), N173 (= N168), D237 (= D232), S241 (= S236), M242 (= M237), C279 (= C274), L280 (= L275), R324 (= R321)
4jhxA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoylphosphate and arginine
63% identity, 99% coverage: 1:334/336 of query aligns to 3:335/336 of 4jhxA
- active site: R61 (= R59), T62 (= T60), D89 (≠ H87), R110 (= R108), H137 (= H135), Q140 (= Q138), D235 (= D232), C277 (= C274), R322 (= R321)
- binding arginine: L132 (= L130), N171 (= N168), D235 (= D232), S239 (= S236), M240 (= M237), P279 (= P276)
- binding phosphoric acid mono(formamide)ester: S59 (= S57), T60 (= T58), R61 (= R59), T62 (= T60), R110 (= R108), H137 (= H135), C277 (= C274), L278 (= L275), R322 (= R321)
Q8DCF5 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Vibrio vulnificus (strain CMCP6)
63% identity, 99% coverage: 1:334/336 of query aligns to 1:333/334 of Q8DCF5
- STRT 57:60 (= STRT 57:60) binding carbamoyl phosphate
- Q84 (= Q84) binding carbamoyl phosphate
- R108 (= R108) binding carbamoyl phosphate
- HPTQ 135:138 (= HPTQ 135:138) 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 (= R321) binding carbamoyl phosphate
4h31A Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate and l-norvaline
63% identity, 99% coverage: 1:334/336 of query aligns to 3:335/335 of 4h31A
- active site: R61 (= R59), T62 (= T60), D89 (≠ H87), R110 (= R108), H137 (= H135), Q140 (= Q138), D235 (= D232), C277 (= C274), R322 (= R321)
- binding phosphoric acid mono(formamide)ester: S59 (= S57), T60 (= T58), R61 (= R59), T62 (= T60), R110 (= R108), H137 (= H135), Q140 (= Q138), C277 (= C274), L278 (= L275), R322 (= R321)
- binding norvaline: L132 (= L130), N171 (= N168), D235 (= D232), S239 (= S236), M240 (= M237)
4jfrB Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate
63% identity, 99% coverage: 1:334/336 of query aligns to 7:339/340 of 4jfrB
- active site: R65 (= R59), T66 (= T60), D93 (≠ H87), R114 (= R108), H141 (= H135), Q144 (= Q138), D239 (= D232), C281 (= C274), R326 (= R321)
- binding phosphoric acid mono(formamide)ester: S63 (= S57), T64 (= T58), R65 (= R59), T66 (= T60), R114 (= R108), H141 (= H135), Q144 (= Q138), C281 (= C274), R326 (= R321)
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
60% identity, 99% coverage: 4:334/336 of query aligns to 3:333/334 of P04391
- S56 (= S57) mutation to H: Much less active than the wild-type.
- STRT 56:59 (= STRT 57:60) binding carbamoyl phosphate
- R58 (= R59) mutation to G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate.
- Q83 (= Q84) binding carbamoyl phosphate
- K87 (= K88) mutation to Q: Much less active than the wild-type.
- R107 (= R108) binding carbamoyl phosphate
- HPTQ 134:137 (= HPTQ 135:138) 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 (= R321) binding carbamoyl phosphate; mutation to A: Much less active than the wild-type.
- A326 (= A327) mutation to G: Activity greater than the wild-type and Km for ornithwinas increases about twofold.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1duvG Crystal structure of e. Coli ornithine transcarbamoylase complexed with ndelta-l-ornithine-diaminophosphinyl-n-sulphonic acid (psorn) (see paper)
60% identity, 99% coverage: 4:334/336 of query aligns to 2:332/333 of 1duvG
- binding ndelta-(n'-sulphodiaminophosphinyl)-l-ornithine: S55 (= S57), T56 (= T58), R57 (= R59), T58 (= T60), R106 (= R108), L128 (= L130), H133 (= H135), N167 (= N168), D231 (= D232), S235 (= S236), M236 (= M237), C273 (= C274), L274 (= L275), R319 (= R321)
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
60% identity, 99% coverage: 4:334/336 of query aligns to 2:332/333 of 2otcA
- active site: R57 (= R59), T58 (= T60), H85 (= H87), R106 (= R108), H133 (= H135), Q136 (= Q138), D231 (= D232), C273 (= C274), R319 (= R321)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S57), T56 (= T58), R57 (= R59), T58 (= T60), R106 (= R108), H133 (= H135), N167 (= N168), D231 (= D232), S235 (= S236), M236 (= M237), L274 (= L275), R319 (= R321)
Q8G998 Ornithine carbamoyltransferase, catabolic; OTCase; EC 2.1.3.3 from Lentilactobacillus hilgardii (Lactobacillus hilgardii) (see paper)
50% identity, 99% coverage: 5:336/336 of query aligns to 10:338/343 of Q8G998
- H79 (≠ N74) 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)
39% identity, 100% coverage: 1:336/336 of query aligns to 1:313/315 of Q51742
- M1 (= M1) modified: Initiator methionine, Removed
- W22 (≠ R22) mutation to A: Decreased heat stability.
- E26 (≠ D26) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ D30) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ A34) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (≠ H230) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (= A243) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E301) mutation to G: Becomes active at low temperatures; when associated with C-228 or D-241.
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 99% coverage: 4:335/336 of query aligns to 36:344/354 of P00481
- R92 (= R59) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C274) mutation to S: Increases KM for ornithine 5-fold and decreases kcat 20-fold.
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
37% identity, 99% coverage: 5:336/336 of query aligns to 9:312/316 of Q81M99
- STRT 57:60 (= STRT 57:60) binding carbamoyl phosphate
- Q84 (= Q84) binding carbamoyl phosphate
- R108 (= R108) binding carbamoyl phosphate
- HPCQ 135:138 (≠ HPTQ 135:138) 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 (= R321) binding carbamoyl phosphate
P00480 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Homo sapiens (Human) (see 31 papers)
37% identity, 99% coverage: 5:335/336 of query aligns to 37:344/354 of P00480