SitesBLAST
Comparing Echvi_3849 FitnessBrowser__Cola:Echvi_3849 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)
1js1X Crystal structure of a new transcarbamylase from the anaerobic bacterium bacteroides fragilis at 2.0 a resolution (see paper)
46% identity, 100% coverage: 1:313/313 of query aligns to 1:315/324 of 1js1X
E1WKT5 N-succinylornithine carbamoyltransferase; N-succinyl-L-ornithine transcarbamylase; SOTCase; EC 2.1.3.11 from Bacteroides fragilis (strain 638R) (see 2 papers)
46% identity, 100% coverage: 1:313/313 of query aligns to 1:315/318 of E1WKT5
- SLRT 47:50 (= SLRT 47:50) binding in other chain
- W75 (= W75) binding carbamoyl phosphate
- P90 (≠ A90) Key residue in conferring substrate specificity for N-succinyl-L-ornithine versus N-acetyl-L-ornithine; mutation to E: Generates an enzyme capable of carbamoylation of N-acetyl-L-ornithine at a rate 7-times greater than N-succinyl-L-ornithine, thus practically converting it from a N-succinylornithine transcarbamylase (SOTCase) to a N-acetylornithine transcarbamylase (AOTCase).
- R110 (= R110) binding in other chain
- HPLQ 147:150 (= HPLQ 147:150) binding in other chain
- CL 274:275 (= CL 272:273) binding in other chain
- R302 (= R300) binding in other chain
2g7mC Crystal structure of b. Fragilis n-succinylornithine transcarbamylase p90e mutant complexed with carbamoyl phosphate and n-acetylnorvaline (see paper)
46% identity, 100% coverage: 1:313/313 of query aligns to 3:317/320 of 2g7mC
- active site: R112 (= R110), H149 (= H147), Q152 (= Q150), K238 (= K236), C276 (= C272), R304 (= R300)
- binding n-acetyl-l-norvaline: W77 (= W75), E92 (≠ A90), F114 (= F112), E144 (= E142), L182 (≠ I180), P183 (= P181), K238 (= K236)
- binding phosphoric acid mono(formamide)ester: S49 (= S47), L50 (= L48), R51 (= R49), T52 (= T50), R112 (= R110), L277 (= L273), R304 (= R300)
2fg7C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with carbamoyl phosphate and n-succinyl-l-norvaline (see paper)
46% identity, 100% coverage: 1:313/313 of query aligns to 3:317/320 of 2fg7C
- active site: R112 (= R110), H149 (= H147), Q152 (= Q150), K238 (= K236), C276 (= C272), R304 (= R300)
- binding phosphoric acid mono(formamide)ester: S49 (= S47), L50 (= L48), R51 (= R49), T52 (= T50), R112 (= R110), L277 (= L273), R304 (= R300)
- binding n-(3-carboxypropanoyl)-l-norvaline: W77 (= W75), P92 (≠ A90), F114 (= F112), E144 (= E142), H178 (= H176), R180 (≠ K178), L182 (≠ I180), P183 (= P181), K238 (= K236), R280 (= R276)
2fg6C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with sulfate and n-succinyl-l-norvaline (see paper)
46% identity, 100% coverage: 1:313/313 of query aligns to 4:318/321 of 2fg6C
- active site: R113 (= R110), H150 (= H147), Q153 (= Q150), K239 (= K236), C277 (= C272), R305 (= R300)
- binding n-(3-carboxypropanoyl)-l-norvaline: F115 (= F112), E145 (= E142), H179 (= H176), R181 (≠ K178), L183 (≠ I180), P184 (= P181), K239 (= K236), R281 (= R276)
- binding sulfate ion: S50 (= S47), L51 (= L48), R52 (= R49), R113 (= R110)
3l02A Crystal structure of n-acetyl-l-ornithine transcarbamylase e92a mutant complexed with carbamyl phosphate and n-succinyl-l-norvaline (see paper)
36% identity, 98% coverage: 5:312/313 of query aligns to 7:332/332 of 3l02A
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C272), R320 (= R300)
- binding phosphoric acid mono(formamide)ester: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), Q149 (= Q150), C292 (= C272), L293 (= L273), R320 (= R300)
- binding n-(3-carboxypropanoyl)-l-norvaline: F112 (= F112), E142 (= E142), H178 (= H176), K250 (= K236), C292 (= C272), R296 (= R276)
Q8P8J2 N-acetylornithine carbamoyltransferase; N-acetyl-L-ornithine transcarbamylase; AOTCase; Acetylornithine transcarbamylase; EC 2.1.3.9 from Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) (see 3 papers)
36% identity, 98% coverage: 5:312/313 of query aligns to 9:334/339 of Q8P8J2
- SMRT 49:52 (≠ SLRT 47:50) binding in other chain
- W77 (= W75) binding carbamoyl phosphate
- E92 (≠ A90) Key residue in conferring substrate specificity for N-acetyl-L-ornithine versus N-succinyl-L-ornithine; mutation E->A,P,S,V: Generates an enzyme capable of carbamoylation of N-succinyl-L-ornithine while losing its ability to use N-acetyl-L-ornithine as substrate, thus converting it from a N-acetylornithine transcarbamylase (AOTCase) to a N-succinylornithine transcarbamylase (SOTCase).
- R112 (= R110) binding in other chain
- E144 (= E142) binding N(2)-acetyl-L-ornithine
- HPCQ 148:151 (≠ HPLQ 147:150) binding in other chain
- K252 (= K236) binding N(2)-acetyl-L-ornithine
- CL 294:295 (= CL 272:273) binding in other chain
- L295 (= L273) binding N(2)-acetyl-L-ornithine
- K302 (≠ E280) modified: N6-carboxylysine; mutation K->A,E,R: Significant decrease in enzymatic activity.
- R322 (= R300) binding in other chain
3kzkA Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline (see paper)
36% identity, 98% coverage: 5:312/313 of query aligns to 7:332/334 of 3kzkA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C272), R320 (= R300)
- binding (s)-2-acetamido-5-ureidopentanoic acid: R110 (= R110), E142 (= E142), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C272), L293 (= L273), R320 (= R300)
3m4jA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with palao (see paper)
36% identity, 98% coverage: 5:312/313 of query aligns to 7:332/332 of 3m4jA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C272), R320 (= R300)
- binding N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), E142 (= E142), H146 (= H147), L182 (≠ I180), K250 (= K236), L293 (= L273)
3kzoA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate and n-acetyl-l-norvaline (see paper)
36% identity, 98% coverage: 5:312/313 of query aligns to 7:332/332 of 3kzoA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C272), R320 (= R300)
- binding n-acetyl-l-norvaline: E142 (= E142), L182 (≠ I180), K250 (= K236)
- binding phosphoric acid mono(formamide)ester: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), R320 (= R300)
3kznA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with n-acetyl-l-ornirthine (see paper)
36% identity, 98% coverage: 5:312/313 of query aligns to 7:332/332 of 3kznA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C272), R320 (= R300)
- binding n~2~-acetyl-l-ornithine: F112 (= F112), E142 (= E142), L182 (≠ I180), K250 (= K236), C292 (= C272), L293 (= L273)
3kzmA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate (see paper)
36% identity, 98% coverage: 5:312/313 of query aligns to 7:332/332 of 3kzmA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C272), R320 (= R300)
- binding phosphoric acid mono(formamide)ester: M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), C292 (= C272), L293 (= L273), R320 (= R300)
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
32% identity, 90% coverage: 31:312/313 of query aligns to 41:310/315 of Q51742
- Y228 (= Y234) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (vs. gap) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E280) 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
- 22 W→A: Decreased heat stability.
- 26 E→Q: Increased dissociation of dodecamers into trimers.
- 30 M→A: Increased dissociation of dodecamers into trimers.
- 34 W→A: Increased dissociation of dodecamers into trimers.
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
30% identity, 95% coverage: 16:313/313 of query aligns to 28:310/316 of Q81M99