SitesBLAST
Comparing N515DRAFT_3763 FitnessBrowser__Dyella79:N515DRAFT_3763 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)
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)
80% identity, 100% coverage: 1:334/335 of query aligns to 1:336/339 of Q8P8J2
- SMRT 49:52 (= SMRT 49:52) binding in other chain
- W77 (= W77) binding
- E92 (= E92) 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 (= R112) binding in other chain
- E144 (= E144) binding
- HPCQ 148:151 (= HPCQ 148:151) binding in other chain
- K252 (= K250) binding
- CL 294:295 (= CL 292:293) binding in other chain
- L295 (= L293) binding
- K302 (= K300) modified: N6-carboxylysine; mutation K->A,E,R: Significant decrease in enzymatic activity.
- R322 (= R320) binding in other chain
3kzkA Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline (see paper)
81% identity, 99% coverage: 3:334/335 of query aligns to 1:334/334 of 3kzkA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K250), C292 (= C292), R320 (= R320)
- binding (s)-2-acetamido-5-ureidopentanoic acid: R110 (= R112), E142 (= E144), H146 (= H148), Q149 (= Q151), K250 (= K250), C292 (= C292), L293 (= L293), R320 (= R320)
3m4jA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with palao (see paper)
80% identity, 99% coverage: 3:332/335 of query aligns to 1:332/332 of 3m4jA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K250), C292 (= C292), R320 (= R320)
- binding N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine: S47 (= S49), M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), E142 (= E144), H146 (= H148), L182 (= L182), K250 (= K250), L293 (= L293)
3kzoA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate and n-acetyl-l-norvaline (see paper)
80% identity, 99% coverage: 3:332/335 of query aligns to 1:332/332 of 3kzoA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K250), C292 (= C292), R320 (= R320)
- binding n-acetyl-l-norvaline: E142 (= E144), L182 (= L182), K250 (= K250)
- binding phosphoric acid mono(formamide)ester: S47 (= S49), M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), R320 (= R320)
3kznA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with n-acetyl-l-ornirthine (see paper)
80% identity, 99% coverage: 3:332/335 of query aligns to 1:332/332 of 3kznA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K250), C292 (= C292), R320 (= R320)
- binding n~2~-acetyl-l-ornithine: F112 (= F114), E142 (= E144), L182 (= L182), K250 (= K250), C292 (= C292), L293 (= L293)
3kzmA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate (see paper)
80% identity, 99% coverage: 3:332/335 of query aligns to 1:332/332 of 3kzmA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K250), C292 (= C292), R320 (= R320)
- binding phosphoric acid mono(formamide)ester: M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), C292 (= C292), L293 (= L293), R320 (= R320)
3l02A Crystal structure of n-acetyl-l-ornithine transcarbamylase e92a mutant complexed with carbamyl phosphate and n-succinyl-l-norvaline (see paper)
80% identity, 99% coverage: 3:332/335 of query aligns to 1:332/332 of 3l02A
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K250), C292 (= C292), R320 (= R320)
- binding phosphoric acid mono(formamide)ester: S47 (= S49), M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), Q149 (= Q151), C292 (= C292), L293 (= L293), R320 (= R320)
- binding n-(3-carboxypropanoyl)-l-norvaline: F112 (= F114), E142 (= E144), H178 (= H178), K250 (= K250), C292 (= C292), R296 (= R296)
2g7mC Crystal structure of b. Fragilis n-succinylornithine transcarbamylase p90e mutant complexed with carbamoyl phosphate and n-acetylnorvaline (see paper)
37% identity, 88% coverage: 38:332/335 of query aligns to 38:316/320 of 2g7mC
- active site: R112 (= R112), H149 (= H148), Q152 (= Q151), K238 (= K250), C276 (= C292), R304 (= R320)
- binding n-acetyl-l-norvaline: W77 (= W77), E92 (= E92), F114 (= F114), E144 (= E144), L182 (= L182), P183 (≠ N183), K238 (= K250)
- binding phosphoric acid mono(formamide)ester: S49 (= S49), L50 (≠ M50), R51 (= R51), T52 (= T52), R112 (= R112), L277 (= L293), R304 (= R320)
2fg6C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with sulfate and n-succinyl-l-norvaline (see paper)
36% identity, 88% coverage: 38:332/335 of query aligns to 39:317/321 of 2fg6C
- active site: R113 (= R112), H150 (= H148), Q153 (= Q151), K239 (= K250), C277 (= C292), R305 (= R320)
- binding n-(3-carboxypropanoyl)-l-norvaline: F115 (= F114), E145 (= E144), H179 (= H178), R181 (≠ K180), L183 (= L182), P184 (≠ N183), K239 (= K250), R281 (= R296)
- binding sulfate ion: S50 (= S49), L51 (≠ M50), R52 (= R51), R113 (= R112)
2fg7C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with carbamoyl phosphate and n-succinyl-l-norvaline (see paper)
36% identity, 88% coverage: 38:332/335 of query aligns to 38:316/320 of 2fg7C
- active site: R112 (= R112), H149 (= H148), Q152 (= Q151), K238 (= K250), C276 (= C292), R304 (= R320)
- binding phosphoric acid mono(formamide)ester: S49 (= S49), L50 (≠ M50), R51 (= R51), T52 (= T52), R112 (= R112), L277 (= L293), R304 (= R320)
- binding n-(3-carboxypropanoyl)-l-norvaline: W77 (= W77), P92 (≠ E92), F114 (= F114), E144 (= E144), H178 (= H178), R180 (≠ K180), L182 (= L182), P183 (≠ N183), K238 (= K250), R280 (= R296)
1js1X Crystal structure of a new transcarbamylase from the anaerobic bacterium bacteroides fragilis at 2.0 a resolution (see paper)
36% identity, 88% coverage: 38:332/335 of query aligns to 36:314/324 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)
36% identity, 88% coverage: 38:332/335 of query aligns to 36:314/318 of E1WKT5
- SLRT 47:50 (≠ SMRT 49:52) binding in other chain
- W75 (= W77) binding
- P90 (≠ E92) 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 (= R112) binding in other chain
- HPLQ 147:150 (≠ HPCQ 148:151) binding in other chain
- CL 274:275 (= CL 292:293) binding in other chain
- R302 (= R320) binding in other chain
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
36% identity, 99% coverage: 4:333/335 of query aligns to 8:311/315 of Q51742
- W22 (≠ D18) mutation to A: Decreased heat stability.
- E26 (= E22) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ A26) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ S30) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y248) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ E264) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (≠ K300) 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
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
36% identity, 99% coverage: 3:333/335 of query aligns to 1:303/304 of 8qeuA
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
36% identity, 99% coverage: 3:333/335 of query aligns to 1:296/297 of 8qevA
2i6uA Crystal structure of ornithine carbamoyltransferase complexed with carbamoyl phosphate and l-norvaline from mycobacterium tuberculosis (rv1656) at 2.2 a (see paper)
36% identity, 99% coverage: 3:332/335 of query aligns to 2:304/307 of 2i6uA
- active site: R52 (= R51), T53 (= T52), R80 (≠ T91), R101 (= R112), H128 (= H148), Q131 (= Q151), D224 (≠ K250), C264 (= C292), R292 (= R320)
- binding phosphoric acid mono(formamide)ester: S50 (= S49), T51 (≠ M50), R52 (= R51), T53 (= T52), R101 (= R112), C264 (= C292), L265 (= L293), R292 (= R320)
- binding norvaline: L123 (≠ M143), N160 (≠ T184), D224 (≠ K250), S228 (≠ A254), M229 (≠ L255)
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
36% identity, 99% coverage: 3:332/335 of query aligns to 3:305/308 of 7nouA
- active site: R102 (= R112), H129 (= H148), Q132 (= Q151), D225 (≠ K250), C265 (= C292), R293 (= R320)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (≠ L44), T52 (≠ M50), R53 (= R51), R53 (= R51), F56 (≠ T54), F56 (≠ T54), L79 (≠ D88), D82 (≠ E92), E83 (= E93), V91 (= V101), Y95 (= Y105), L266 (= L293), R293 (= R320)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
36% identity, 99% coverage: 3:332/335 of query aligns to 3:305/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
36% identity, 99% coverage: 3:332/335 of query aligns to 3:305/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
36% identity, 99% coverage: 3:332/335 of query aligns to 3:305/308 of 7nnyA
- active site: R102 (= R112), H129 (= H148), Q132 (= Q151), D225 (≠ K250), C265 (= C292), R293 (= R320)
- binding 1-naphthol: T52 (≠ M50), R53 (= R51), F56 (≠ T54), E83 (= E93), V91 (= V101), Y95 (= Y105)
Query Sequence
>N515DRAFT_3763 FitnessBrowser__Dyella79:N515DRAFT_3763
MTLRHFLTTQDYSRAEIDALLEQAAAFKRSPRGQQLAGKSVALLFFNPSMRTRTSFELGA
FHLGGHAIVLAPGKDAWPIEFDVGTVMDGDTEEHIAEVARVLSRYVDLIAVRAFPKFQDW
TVDREDRVIKAFAQYASVPVINMETITHPCQELAHALAMQEHLGSLQNKKYVLTWTYHPK
PLNTAVANSALLIATKMGMDVTLLCPTPDYVLDDRYMQAGYANAQANGGSLRISHDIDEA
YSGADVVYAKSWGALPFFGRWEQEKPIRDAHKHFIVDERKMALTNNGLFSHCLPLRRNVK
ATDAVMDAPYCIAIDEAENRLHVQKAVMATLLGQR
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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