SitesBLAST
Comparing WP_057687254.1 NCBI__GCF_001431535.1:WP_057687254.1 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)
93% identity, 100% coverage: 1:336/336 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 (= K252) binding
- CL 294:295 (= CL 294:295) binding in other chain
- L295 (= L295) binding
- K302 (= K302) modified: N6-carboxylysine; mutation K->A,E,R: Significant decrease in enzymatic activity.
- R322 (= R322) binding in other chain
3kzkA Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline (see paper)
93% identity, 99% coverage: 3:336/336 of query aligns to 1:334/334 of 3kzkA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K252), C292 (= C294), R320 (= R322)
- binding (s)-2-acetamido-5-ureidopentanoic acid: R110 (= R112), E142 (= E144), H146 (= H148), Q149 (= Q151), K250 (= K252), C292 (= C294), L293 (= L295), R320 (= R322)
3m4jA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with palao (see paper)
94% identity, 99% coverage: 3:333/336 of query aligns to 1:331/332 of 3m4jA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K252), C292 (= C294), R320 (= R322)
- binding N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine: S47 (= S49), M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), E142 (= E144), H146 (= H148), L182 (= L184), K250 (= K252), L293 (= L295)
3kzoA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate and n-acetyl-l-norvaline (see paper)
94% identity, 99% coverage: 3:333/336 of query aligns to 1:331/332 of 3kzoA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K252), C292 (= C294), R320 (= R322)
- binding n-acetyl-l-norvaline: E142 (= E144), L182 (= L184), K250 (= K252)
- binding phosphoric acid mono(formamide)ester: S47 (= S49), M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), R320 (= R322)
3kznA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with n-acetyl-l-ornirthine (see paper)
94% identity, 99% coverage: 3:333/336 of query aligns to 1:331/332 of 3kznA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K252), C292 (= C294), R320 (= R322)
- binding n~2~-acetyl-l-ornithine: F112 (= F114), E142 (= E144), L182 (= L184), K250 (= K252), C292 (= C294), L293 (= L295)
3kzmA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate (see paper)
94% identity, 99% coverage: 3:333/336 of query aligns to 1:331/332 of 3kzmA
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K252), C292 (= C294), R320 (= R322)
- binding phosphoric acid mono(formamide)ester: M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), C292 (= C294), L293 (= L295), R320 (= R322)
3l02A Crystal structure of n-acetyl-l-ornithine transcarbamylase e92a mutant complexed with carbamyl phosphate and n-succinyl-l-norvaline (see paper)
93% identity, 99% coverage: 3:333/336 of query aligns to 1:331/332 of 3l02A
- active site: R110 (= R112), H146 (= H148), Q149 (= Q151), K250 (= K252), C292 (= C294), R320 (= R322)
- binding phosphoric acid mono(formamide)ester: S47 (= S49), M48 (= M50), R49 (= R51), T50 (= T52), R110 (= R112), Q149 (= Q151), C292 (= C294), L293 (= L295), R320 (= R322)
- binding n-(3-carboxypropanoyl)-l-norvaline: F112 (= F114), E142 (= E144), H178 (= H180), K250 (= K252), C292 (= C294), R296 (= R298)
2g7mC Crystal structure of b. Fragilis n-succinylornithine transcarbamylase p90e mutant complexed with carbamoyl phosphate and n-acetylnorvaline (see paper)
35% identity, 95% coverage: 3:322/336 of query aligns to 3:304/320 of 2g7mC
- active site: R112 (= R112), H149 (= H148), Q152 (= Q151), K238 (= K252), C276 (= C294), R304 (= R322)
- binding n-acetyl-l-norvaline: W77 (= W77), E92 (= E92), F114 (= F114), E144 (= E144), L182 (= L184), P183 (≠ N185), K238 (= K252)
- binding phosphoric acid mono(formamide)ester: S49 (= S49), L50 (≠ M50), R51 (= R51), T52 (= T52), R112 (= R112), L277 (= L295), R304 (= R322)
2fg6C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with sulfate and n-succinyl-l-norvaline (see paper)
35% identity, 95% coverage: 3:322/336 of query aligns to 4:305/321 of 2fg6C
- active site: R113 (= R112), H150 (= H148), Q153 (= Q151), K239 (= K252), C277 (= C294), R305 (= R322)
- binding n-(3-carboxypropanoyl)-l-norvaline: F115 (= F114), E145 (= E144), H179 (= H180), R181 (≠ K182), L183 (= L184), P184 (≠ N185), K239 (= K252), R281 (= R298)
- 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)
35% identity, 95% coverage: 3:322/336 of query aligns to 3:304/320 of 2fg7C
- active site: R112 (= R112), H149 (= H148), Q152 (= Q151), K238 (= K252), C276 (= C294), R304 (= R322)
- binding phosphoric acid mono(formamide)ester: S49 (= S49), L50 (≠ M50), R51 (= R51), T52 (= T52), R112 (= R112), L277 (= L295), R304 (= R322)
- binding n-(3-carboxypropanoyl)-l-norvaline: W77 (= W77), P92 (≠ E92), F114 (= F114), E144 (= E144), H178 (= H180), R180 (≠ K182), L182 (= L184), P183 (≠ N185), K238 (= K252), R280 (= R298)
1js1X Crystal structure of a new transcarbamylase from the anaerobic bacterium bacteroides fragilis at 2.0 a resolution (see paper)
35% identity, 95% coverage: 3:322/336 of query aligns to 1:302/324 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)
35% identity, 95% coverage: 3:322/336 of query aligns to 1:302/318 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 294:295) binding in other chain
- R302 (= R322) 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: 4:335/336 of query aligns to 8:311/315 of Q51742
- W22 (≠ D18) mutation to A: Decreased heat stability.
- E26 (≠ T22) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ L26) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (vs. gap) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y250) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ W263) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (≠ K302) 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)
34% identity, 99% coverage: 3:335/336 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)
34% identity, 99% coverage: 3:335/336 of query aligns to 1:296/297 of 8qevA
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
30% identity, 99% coverage: 1:333/336 of query aligns to 9:308/316 of Q81M99
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
30% identity, 99% coverage: 1:333/336 of query aligns to 5:304/307 of 4nf2A
- active site: R55 (= R51), T56 (= T52), R83 (≠ T91), R104 (= R112), H131 (= H148), Q134 (= Q151), D226 (≠ K252), C265 (= C294), R293 (= R322)
- binding phosphoric acid mono(formamide)ester: S53 (= S49), T54 (≠ M50), R55 (= R51), T56 (= T52), R104 (= R112), H131 (= H148), Q134 (= Q151), C265 (= C294), L266 (= L295), R293 (= R322)
- binding norvaline: L126 (≠ M143), N162 (≠ A187), D226 (≠ K252), S230 (≠ A256), M231 (≠ L257)
1duvG Crystal structure of e. Coli ornithine transcarbamoylase complexed with ndelta-l-ornithine-diaminophosphinyl-n-sulphonic acid (psorn) (see paper)
31% identity, 98% coverage: 4:332/336 of query aligns to 6:329/333 of 1duvG
- binding ndelta-(n'-sulphodiaminophosphinyl)-l-ornithine: S55 (= S49), T56 (≠ M50), R57 (= R51), T58 (= T52), R106 (= R112), L128 (≠ M143), H133 (= H148), N167 (≠ T186), D231 (≠ K252), S235 (≠ A256), M236 (≠ L257), C273 (= C294), L274 (= L295), R319 (= R322)
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
31% identity, 98% coverage: 4:332/336 of query aligns to 7:330/334 of P04391
- S56 (= S49) mutation to H: Much less active than the wild-type.
- STRT 56:59 (≠ SMRT 49:52) binding
- R58 (= R51) mutation to G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate.
- Q83 (≠ N82) binding
- K87 (≠ E92) mutation to Q: Much less active than the wild-type.
- R107 (= R112) binding
- HPTQ 134:137 (≠ HPCQ 148:151) binding
- N168 (≠ T186) binding
- D232 (≠ K252) binding
- SM 236:237 (≠ AL 256:257) binding
- C274 (= C294) binding ; mutation to A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization.
- CL 274:275 (= CL 294:295) binding
- R320 (= R322) binding ; mutation to A: Much less active than the wild-type.
- A326 (= A328) 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
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
31% identity, 98% coverage: 4:332/336 of query aligns to 6:329/333 of 2otcA
- active site: R57 (= R51), T58 (= T52), H85 (≠ T91), R106 (= R112), H133 (= H148), Q136 (= Q151), D231 (≠ K252), C273 (= C294), R319 (= R322)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S49), T56 (≠ M50), R57 (= R51), T58 (= T52), R106 (= R112), H133 (= H148), N167 (≠ T186), D231 (≠ K252), S235 (≠ A256), M236 (≠ L257), L274 (= L295), R319 (= R322)
Query Sequence
>WP_057687254.1 NCBI__GCF_001431535.1:WP_057687254.1
MSLKHFLNTQDWSRSELDALLTQAALFKRNKLGDQLKGKSIALVFFNPSMRTRTSFELGA
FQLGAHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVAKVLGRYCDMIAVRAFPKFVDW
SVDREDTVLKSFAKYSPVPVINMETITHPCQELAHAMALQEHFGTQDLRGKKYVLTWTYH
PKPLNTAVANSALTIATRMGMDVTLLCPTPDYILDERYMGWAEQNVAENGGSLQVSHDIE
SAYTGADVVYAKSWGALPFFGNWEPEKPIRDQYKHFIVDEQKMALTNNGVFSHCLPLRRN
VKATDAVMDSPQCIAINEAENRLHVQKAIMAALAGR
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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