SitesBLAST
Comparing 353243 FitnessBrowser__Btheta:353243 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)
93% identity, 100% coverage: 1:317/318 of query aligns to 1:317/324 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)
93% identity, 100% coverage: 1:317/318 of query aligns to 1:317/318 of E1WKT5
- SLRT 47:50 (= SLRT 47:50) binding in other chain
- W75 (= W75) binding
- P90 (= P90) 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 274:275) binding in other chain
- R302 (= R302) binding in other chain
2fg7C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with carbamoyl phosphate and n-succinyl-l-norvaline (see paper)
93% identity, 100% coverage: 1:317/318 of query aligns to 3:319/320 of 2fg7C
- active site: R112 (= R110), H149 (= H147), Q152 (= Q150), K238 (= K236), C276 (= C274), R304 (= R302)
- binding phosphoric acid mono(formamide)ester: S49 (= S47), L50 (= L48), R51 (= R49), T52 (= T50), R112 (= R110), L277 (= L275), R304 (= R302)
- binding n-(3-carboxypropanoyl)-l-norvaline: W77 (= W75), P92 (= P90), F114 (= F112), E144 (= E142), H178 (= H176), R180 (= R178), L182 (= L180), P183 (= P181), K238 (= K236), R280 (= R278)
2fg6C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with sulfate and n-succinyl-l-norvaline (see paper)
93% identity, 100% coverage: 1:317/318 of query aligns to 4:320/321 of 2fg6C
- active site: R113 (= R110), H150 (= H147), Q153 (= Q150), K239 (= K236), C277 (= C274), R305 (= R302)
- binding n-(3-carboxypropanoyl)-l-norvaline: F115 (= F112), E145 (= E142), H179 (= H176), R181 (= R178), L183 (= L180), P184 (= P181), K239 (= K236), R281 (= R278)
- binding sulfate ion: S50 (= S47), L51 (= L48), R52 (= R49), R113 (= R110)
2g7mC Crystal structure of b. Fragilis n-succinylornithine transcarbamylase p90e mutant complexed with carbamoyl phosphate and n-acetylnorvaline (see paper)
93% identity, 100% coverage: 1:317/318 of query aligns to 3:319/320 of 2g7mC
- active site: R112 (= R110), H149 (= H147), Q152 (= Q150), K238 (= K236), C276 (= C274), R304 (= R302)
- binding n-acetyl-l-norvaline: W77 (= W75), E92 (≠ P90), F114 (= F112), E144 (= E142), L182 (= L180), P183 (= P181), K238 (= K236)
- binding phosphoric acid mono(formamide)ester: S49 (= S47), L50 (= L48), R51 (= R49), T52 (= T50), R112 (= R110), L277 (= L275), R304 (= R302)
3l02A Crystal structure of n-acetyl-l-ornithine transcarbamylase e92a mutant complexed with carbamyl phosphate and n-succinyl-l-norvaline (see paper)
37% identity, 99% coverage: 1:314/318 of query aligns to 1:332/332 of 3l02A
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C274), R320 (= R302)
- binding phosphoric acid mono(formamide)ester: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), Q149 (= Q150), C292 (= C274), L293 (= L275), R320 (= R302)
- binding n-(3-carboxypropanoyl)-l-norvaline: F112 (= F112), E142 (= E142), H178 (= H176), K250 (= K236), C292 (= C274), R296 (= R278)
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)
37% identity, 99% coverage: 1:314/318 of query aligns to 3:334/339 of Q8P8J2
- SMRT 49:52 (≠ SLRT 47:50) binding in other chain
- W77 (= W75) binding
- E92 (≠ P90) 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
- HPCQ 148:151 (≠ HPLQ 147:150) binding in other chain
- K252 (= K236) binding
- CL 294:295 (= CL 274:275) binding in other chain
- L295 (= L275) binding
- K302 (≠ I282) modified: N6-carboxylysine; mutation K->A,E,R: Significant decrease in enzymatic activity.
- R322 (= R302) binding in other chain
3kzkA Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline (see paper)
37% identity, 99% coverage: 1:314/318 of query aligns to 1:332/334 of 3kzkA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C274), R320 (= R302)
- binding (s)-2-acetamido-5-ureidopentanoic acid: R110 (= R110), E142 (= E142), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C274), L293 (= L275), R320 (= R302)
3m4jA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with palao (see paper)
37% identity, 99% coverage: 1:314/318 of query aligns to 1:332/332 of 3m4jA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C274), R320 (= R302)
- binding N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), E142 (= E142), H146 (= H147), L182 (= L180), K250 (= K236), L293 (= L275)
3kzoA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate and n-acetyl-l-norvaline (see paper)
37% identity, 99% coverage: 1:314/318 of query aligns to 1:332/332 of 3kzoA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C274), R320 (= R302)
- binding n-acetyl-l-norvaline: E142 (= E142), L182 (= L180), K250 (= K236)
- binding phosphoric acid mono(formamide)ester: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), R320 (= R302)
3kznA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with n-acetyl-l-ornirthine (see paper)
37% identity, 99% coverage: 1:314/318 of query aligns to 1:332/332 of 3kznA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C274), R320 (= R302)
- binding n~2~-acetyl-l-ornithine: F112 (= F112), E142 (= E142), L182 (= L180), K250 (= K236), C292 (= C274), L293 (= L275)
3kzmA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate (see paper)
37% identity, 99% coverage: 1:314/318 of query aligns to 1:332/332 of 3kzmA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K236), C292 (= C274), R320 (= R302)
- binding phosphoric acid mono(formamide)ester: M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), C292 (= C274), L293 (= L275), R320 (= R302)
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
28% identity, 99% coverage: 1:314/318 of query aligns to 1:302/304 of 8qeuA
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
30% identity, 95% coverage: 18:318/318 of query aligns to 28:314/315 of Q51742
- M30 (≠ A20) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ Q24) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y234) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ G247) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (≠ I282) 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.
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
29% identity, 99% coverage: 1:314/318 of query aligns to 1:295/297 of 8qevA
1duvG Crystal structure of e. Coli ornithine transcarbamoylase complexed with ndelta-l-ornithine-diaminophosphinyl-n-sulphonic acid (psorn) (see paper)
27% identity, 92% coverage: 12:302/318 of query aligns to 18:319/333 of 1duvG
- binding ndelta-(n'-sulphodiaminophosphinyl)-l-ornithine: S55 (= S47), T56 (≠ L48), R57 (= R49), T58 (= T50), R106 (= R110), L128 (≠ E142), H133 (= H147), N167 (≠ A183), D231 (≠ K236), S235 (≠ A240), M236 (≠ Y241), C273 (= C274), L274 (= L275), R319 (= R302)
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
27% identity, 92% coverage: 12:302/318 of query aligns to 19:320/334 of P04391
- S56 (= S47) mutation to H: Much less active than the wild-type.
- STRT 56:59 (≠ SLRT 47:50) binding
- R58 (= R49) mutation to G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate.
- Q83 (≠ A74) binding
- K87 (= K89) mutation to Q: Much less active than the wild-type.
- R107 (= R110) binding
- HPTQ 134:137 (≠ HPLQ 147:150) binding
- N168 (≠ A183) binding
- D232 (≠ K236) binding
- SM 236:237 (≠ AY 240:241) binding
- C274 (= C274) binding ; mutation to A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization.
- CL 274:275 (= CL 274:275) binding
- R320 (= R302) binding ; mutation to A: Much less active than the wild-type.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 326 A→G: Activity greater than the wild-type and Km for ornithwinas increases about twofold.
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
27% identity, 92% coverage: 12:302/318 of query aligns to 18:319/333 of 2otcA
- active site: R57 (= R49), T58 (= T50), H85 (≠ D88), R106 (= R110), H133 (= H147), Q136 (= Q150), D231 (≠ K236), C273 (= C274), R319 (= R302)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S47), T56 (≠ L48), R57 (= R49), T58 (= T50), R106 (= R110), H133 (= H147), N167 (≠ A183), D231 (≠ K236), S235 (≠ A240), M236 (≠ Y241), L274 (= L275), R319 (= R302)
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
23% identity, 94% coverage: 21:318/318 of query aligns to 31:313/316 of Q81M99
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
23% identity, 89% coverage: 21:302/318 of query aligns to 27:293/307 of 4nf2A
- active site: R55 (= R49), T56 (= T50), R83 (= R81), R104 (= R110), H131 (= H147), Q134 (= Q150), D226 (≠ K236), C265 (= C274), R293 (= R302)
- binding phosphoric acid mono(formamide)ester: S53 (= S47), T54 (≠ L48), R55 (= R49), T56 (= T50), R104 (= R110), H131 (= H147), Q134 (= Q150), C265 (= C274), L266 (= L275), R293 (= R302)
- binding norvaline: L126 (≠ E142), N162 (≠ P179), D226 (≠ K236), S230 (≠ A240), M231 (≠ Y241)
Query Sequence
>353243 FitnessBrowser__Btheta:353243
MKKFTCVQDIGDLKSALAEAFEIQKDRFKYVELGRNKTLMMIFFNSSLRTRLSTQKAALN
LGMNVMVLDINQGAWKLETERGVIMDGDKPEHLLEAIPVMGCYCDIIGVRSFARFEDRDF
DYQETILNQFIQYSGRPVFSMEAATRHPLQSFADLITIEEYKKTARPKVVMTWAPHPRPL
PQAVPNSFAEWMNATDYDFVITHPEGYELAPQFVGNAKVEYDQMKAFEGADFIYAKNWAA
YTGDNYGQILSKDREWTVSDRQMAVTNNAFFMHCLPVRRNMIVTDDVIESPQSIVIPEAA
NREISATVVLKRLIEGLE
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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