SitesBLAST
Comparing CA265_RS18520 FitnessBrowser__Pedo557:CA265_RS18520 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)
2g7mC Crystal structure of b. Fragilis n-succinylornithine transcarbamylase p90e mutant complexed with carbamoyl phosphate and n-acetylnorvaline (see paper)
49% identity, 100% coverage: 1:323/324 of query aligns to 3:319/320 of 2g7mC
- active site: R112 (= R110), H149 (= H147), Q152 (= Q150), K238 (= K244), C276 (= C280), R304 (= R308)
- binding n-acetyl-l-norvaline: W77 (= W75), E92 (≠ V90), F114 (= F112), E144 (= E142), L182 (= L184), P183 (= P185), K238 (= K244)
- binding phosphoric acid mono(formamide)ester: S49 (= S47), L50 (= L48), R51 (= R49), T52 (= T50), R112 (= R110), L277 (= L281), R304 (= R308)
1js1X Crystal structure of a new transcarbamylase from the anaerobic bacterium bacteroides fragilis at 2.0 a resolution (see paper)
49% identity, 100% coverage: 1:323/324 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)
49% identity, 100% coverage: 1:323/324 of query aligns to 1:317/318 of E1WKT5
- SLRT 47:50 (= SLRT 47:50) binding in other chain
- W75 (= W75) binding
- P90 (≠ V90) 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 280:281) binding in other chain
- R302 (= R308) binding in other chain
2fg7C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with carbamoyl phosphate and n-succinyl-l-norvaline (see paper)
49% identity, 100% coverage: 1:323/324 of query aligns to 3:319/320 of 2fg7C
- active site: R112 (= R110), H149 (= H147), Q152 (= Q150), K238 (= K244), C276 (= C280), R304 (= R308)
- binding phosphoric acid mono(formamide)ester: S49 (= S47), L50 (= L48), R51 (= R49), T52 (= T50), R112 (= R110), L277 (= L281), R304 (= R308)
- binding n-(3-carboxypropanoyl)-l-norvaline: W77 (= W75), P92 (≠ V90), F114 (= F112), E144 (= E142), H178 (= H180), R180 (≠ K182), L182 (= L184), P183 (= P185), K238 (= K244), R280 (= R284)
2fg6C N-succinyl-l-ornithine transcarbamylase from b. Fragilis complexed with sulfate and n-succinyl-l-norvaline (see paper)
49% identity, 100% coverage: 1:323/324 of query aligns to 4:320/321 of 2fg6C
- active site: R113 (= R110), H150 (= H147), Q153 (= Q150), K239 (= K244), C277 (= C280), R305 (= R308)
- binding n-(3-carboxypropanoyl)-l-norvaline: F115 (= F112), E145 (= E142), H179 (= H180), R181 (≠ K182), L183 (= L184), P184 (= P185), K239 (= K244), R281 (= R284)
- binding sulfate ion: S50 (= S47), L51 (= L48), R52 (= R49), R113 (= R110)
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)
34% identity, 97% coverage: 12:324/324 of query aligns to 2:338/339 of Q8P8J2
- SMRT 49:52 (≠ SLRT 47:50) binding in other chain
- W77 (= W75) binding
- E92 (≠ V90) 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 (= K244) binding
- CL 294:295 (= CL 280:281) binding in other chain
- L295 (= L281) binding
- K302 (≠ E288) modified: N6-carboxylysine; mutation K->A,E,R: Significant decrease in enzymatic activity.
- R322 (= R308) binding in other chain
3l02A Crystal structure of n-acetyl-l-ornithine transcarbamylase e92a mutant complexed with carbamyl phosphate and n-succinyl-l-norvaline (see paper)
34% identity, 95% coverage: 13:320/324 of query aligns to 1:332/332 of 3l02A
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K244), C292 (= C280), R320 (= R308)
- binding phosphoric acid mono(formamide)ester: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), Q149 (= Q150), C292 (= C280), L293 (= L281), R320 (= R308)
- binding n-(3-carboxypropanoyl)-l-norvaline: F112 (= F112), E142 (= E142), H178 (= H180), K250 (= K244), C292 (= C280), R296 (= R284)
3m4jA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with palao (see paper)
34% identity, 95% coverage: 13:320/324 of query aligns to 1:332/332 of 3m4jA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K244), C292 (= C280), R320 (= R308)
- binding N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), E142 (= E142), H146 (= H147), L182 (= L184), K250 (= K244), L293 (= L281)
3kzoA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate and n-acetyl-l-norvaline (see paper)
34% identity, 95% coverage: 13:320/324 of query aligns to 1:332/332 of 3kzoA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K244), C292 (= C280), R320 (= R308)
- binding n-acetyl-l-norvaline: E142 (= E142), L182 (= L184), K250 (= K244)
- binding phosphoric acid mono(formamide)ester: S47 (= S47), M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), R320 (= R308)
3kznA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with n-acetyl-l-ornirthine (see paper)
34% identity, 95% coverage: 13:320/324 of query aligns to 1:332/332 of 3kznA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K244), C292 (= C280), R320 (= R308)
- binding n~2~-acetyl-l-ornithine: F112 (= F112), E142 (= E142), L182 (= L184), K250 (= K244), C292 (= C280), L293 (= L281)
3kzmA Crystal structure of n-acetyl-l-ornithine transcarbamylase complexed with carbamyl phosphate (see paper)
34% identity, 95% coverage: 13:320/324 of query aligns to 1:332/332 of 3kzmA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K244), C292 (= C280), R320 (= R308)
- binding phosphoric acid mono(formamide)ester: M48 (≠ L48), R49 (= R49), T50 (= T50), R110 (= R110), C292 (= C280), L293 (= L281), R320 (= R308)
3kzkA Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline (see paper)
34% identity, 96% coverage: 13:322/324 of query aligns to 1:334/334 of 3kzkA
- active site: R110 (= R110), H146 (= H147), Q149 (= Q150), K250 (= K244), C292 (= C280), R320 (= R308)
- binding (s)-2-acetamido-5-ureidopentanoic acid: R110 (= R110), E142 (= E142), H146 (= H147), Q149 (= Q150), K250 (= K244), C292 (= C280), L293 (= L281), R320 (= R308)
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
28% identity, 95% coverage: 13:321/324 of query aligns to 21:306/307 of 4nf2A
- active site: R55 (= R49), T56 (= T50), R83 (≠ D81), R104 (= R110), H131 (= H147), Q134 (= Q150), D226 (≠ K244), C265 (= C280), R293 (= R308)
- binding phosphoric acid mono(formamide)ester: S53 (= S47), T54 (≠ L48), R55 (= R49), T56 (= T50), R104 (= R110), H131 (= H147), Q134 (= Q150), C265 (= C280), L266 (= L281), R293 (= R308)
- binding norvaline: L126 (≠ E142), N162 (≠ S191), D226 (≠ K244), S230 (= S248), M231 (≠ Y249)
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
28% identity, 96% coverage: 13:324/324 of query aligns to 25:313/316 of Q81M99
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
28% identity, 90% coverage: 33:324/324 of query aligns to 43:314/315 of Q51742
- Y228 (= Y242) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ K250) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E288) 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.
P05150 Ornithine carbamoyltransferase; Ornithine transcarbamylase; OTCase; EC 2.1.3.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 95% coverage: 10:316/324 of query aligns to 29:324/338 of P05150
- T68 (≠ L48) mutation to G: Reduces activity by 95%. Reduces affinity for ornithine 2-fold.
- G181 (≠ P179) mutation to R: Loss of activity.
- D182 (≠ H180) mutation to N: Reduces activity by 33%. Reduces affinity for ornithine 30-fold.
- N184 (= N190) mutation to Q: Reduces activity by 50%. Reduces affinity for ornithine 20-fold.
- N185 (≠ S191) mutation to Q: No effect on activity. Reduces affinity for ornithine 200-fold.
- E256 (≠ K250) mutation to Q: Reduces activity by 50%.
- K263 (vs. gap) mutation to A: Reduces activity by 70%. Reduces affinity for ornithine 18-fold.
- C289 (= C280) mutation to S: Reduces activity by 90%. Reduces affinity for ornithine 6-fold.
- L290 (= L281) mutation to S: Reduces activity by 86%.
Q837U7 Putrescine carbamoyltransferase; PTC; PTCase; Agmatine catabolism protein B; Putrescine transcarbamoylase; Putrescine transcarbamylase; EC 2.1.3.6 from Enterococcus faecalis (strain ATCC 700802 / V583) (see paper)
29% identity, 88% coverage: 33:316/324 of query aligns to 38:305/339 of Q837U7
- R54 (= R49) mutation to G: Loss of activity with putrescine and ornithine.
- YGLY 230:233 (≠ S--- 247) mutation to VSMG: Loss of activity with putrescine; increased activity with ornithine.
4a8hA Crystal structure of putrescine transcarbamylase from enterococcus faecalis with n-(phosphonoacetyl)-putrescine (see paper)
29% identity, 88% coverage: 33:316/324 of query aligns to 38:305/340 of 4a8hA
- active site: R54 (= R49), T55 (= T50), G82 (≠ S88), R103 (= R110), H130 (= H147), Q133 (= Q150), D227 (≠ K244), C269 (= C280), R297 (= R308)
- binding n-(phosphonoacetyl)-putrescine: S52 (= S47), T53 (≠ L48), R54 (= R49), T55 (= T50), R103 (= R110), M125 (≠ E142), H130 (= H147), Q164 (≠ P189), D227 (≠ K244), C269 (= C280), L270 (= L281), R297 (= R308)
4am8D Crystal structure of the r54g mutant of putrescine transcarbamylase from enterococcus faecalis bound to a curing guanidinium ion
29% identity, 88% coverage: 33:316/324 of query aligns to 38:305/349 of 4am8D
- active site: G54 (≠ R49), T55 (= T50), R103 (= R110), H130 (= H147), Q133 (= Q150), D227 (≠ K244), C269 (= C280), R297 (= R308)
- binding n-(phosphonoacetyl)-l-ornithine: S52 (= S47), T53 (≠ L48), G54 (≠ R49), T55 (= T50), R103 (= R110), M125 (≠ E142), H130 (= H147), Q164 (≠ P189), D227 (≠ K244), L270 (= L281), R297 (= R308)
4am8A Crystal structure of the r54g mutant of putrescine transcarbamylase from enterococcus faecalis bound to a curing guanidinium ion
29% identity, 88% coverage: 33:316/324 of query aligns to 38:305/336 of 4am8A
- active site: G54 (≠ R49), T55 (= T50), R103 (= R110), H130 (= H147), Q133 (= Q150), D227 (≠ K244), C269 (= C280), R297 (= R308)
- binding n-(phosphonoacetyl)-l-ornithine: S52 (= S47), T53 (≠ L48), G54 (≠ R49), T55 (= T50), R103 (= R110), M125 (≠ E142), H130 (= H147), Q164 (≠ P189), D227 (≠ K244), L270 (= L281), R297 (= R308)
Sites not aligning to the query:
Query Sequence
>CA265_RS18520 FitnessBrowser__Pedo557:CA265_RS18520
MKLFTSVHDVPSIKQFVNDALALKANPYAHQDLGKNKTLGLVFMNPSLRTRLSTQKAALN
LGMNVMVMNLDKEGWALETQDGVVMNGSTVEHIREAAAVMGQYCDILGLRSFPKLNNREE
DYSEDFFNKFVKYCAVPVVSLESATRHPLQSFADIITIHETWTKKPDGRKPKVVLAWAPH
VKALPQAVPNSFAEWMCKAQAEGMIDFTIAQPEGYELSEDFTPDANIQYNLEEALAGADY
VYVKNWSSYKEYGKVLTYPDGWMMNNEKLKFTNDAKVMHCLPVRRDLELSSEILDGPNSL
VIHEAGNRLWAAQAVIKAMLEELK
Or try a new SitesBLAST search
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