SitesBLAST
Comparing WP_089137031.1 NCBI__GCF_002217945.1:WP_089137031.1 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)
Q8G998 Ornithine carbamoyltransferase, catabolic; OTCase; EC 2.1.3.3 from Lentilactobacillus hilgardii (Lactobacillus hilgardii) (see paper)
84% identity, 100% coverage: 2:342/342 of query aligns to 3:343/343 of Q8G998
- H79 (= H78) binding Ni(2+)
- 337:343 (vs. 336:342, 71% identical) mutation Missing: It generates a metastable mutant that behaves as a mixture of monomeric and trimeric species with only the latter exhibiting OTC activity.
4jqoA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with citrulline and inorganic phosphate
50% identity, 96% coverage: 9:335/342 of query aligns to 9:337/338 of 4jqoA
- active site: R63 (= R63), T64 (= T64), D91 (≠ K91), R112 (= R112), H139 (= H139), Q142 (= Q142), D237 (= D235), C279 (= C277), R324 (= R322)
- binding citrulline: H139 (= H139), Q142 (= Q142), N173 (= N171), D237 (= D235), S241 (= S239), M242 (= M240), C279 (= C277), L280 (= L278), R324 (= R322)
4jfrB Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate
50% identity, 96% coverage: 9:335/342 of query aligns to 11:339/340 of 4jfrB
- active site: R65 (= R63), T66 (= T64), D93 (≠ K91), R114 (= R112), H141 (= H139), Q144 (= Q142), D239 (= D235), C281 (= C277), R326 (= R322)
- binding phosphoric acid mono(formamide)ester: S63 (= S61), T64 (= T62), R65 (= R63), T66 (= T64), R114 (= R112), H141 (= H139), Q144 (= Q142), C281 (= C277), R326 (= R322)
4h31A Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoyl phosphate and l-norvaline
50% identity, 96% coverage: 9:335/342 of query aligns to 7:335/335 of 4h31A
- active site: R61 (= R63), T62 (= T64), D89 (≠ K91), R110 (= R112), H137 (= H139), Q140 (= Q142), D235 (= D235), C277 (= C277), R322 (= R322)
- binding phosphoric acid mono(formamide)ester: S59 (= S61), T60 (= T62), R61 (= R63), T62 (= T64), R110 (= R112), H137 (= H139), Q140 (= Q142), C277 (= C277), L278 (= L278), R322 (= R322)
- binding norvaline: L132 (= L134), N171 (= N171), D235 (= D235), S239 (= S239), M240 (= M240)
4jhxA Crystal structure of anabolic ornithine carbamoyltransferase from vibrio vulnificus in complex with carbamoylphosphate and arginine
50% identity, 96% coverage: 9:335/342 of query aligns to 7:335/336 of 4jhxA
- active site: R61 (= R63), T62 (= T64), D89 (≠ K91), R110 (= R112), H137 (= H139), Q140 (= Q142), D235 (= D235), C277 (= C277), R322 (= R322)
- binding arginine: L132 (= L134), N171 (= N171), D235 (= D235), S239 (= S239), M240 (= M240), P279 (= P279)
- binding phosphoric acid mono(formamide)ester: S59 (= S61), T60 (= T62), R61 (= R63), T62 (= T64), R110 (= R112), H137 (= H139), C277 (= C277), L278 (= L278), R322 (= R322)
Q8DCF5 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Vibrio vulnificus (strain CMCP6)
50% identity, 96% coverage: 9:335/342 of query aligns to 5:333/334 of Q8DCF5
- STRT 57:60 (= STRT 61:64) binding carbamoyl phosphate
- Q84 (= Q88) binding carbamoyl phosphate
- R108 (= R112) binding carbamoyl phosphate
- HPTQ 135:138 (= HPTQ 139:142) binding carbamoyl phosphate
- N169 (= N171) binding L-ornithine
- D233 (= D235) binding L-ornithine
- SM 237:238 (= SM 239:240) binding L-ornithine
- CL 275:276 (= CL 277:278) binding carbamoyl phosphate
- R320 (= R322) binding carbamoyl phosphate
P08308 Ornithine carbamoyltransferase, catabolic; OTCase; EC 2.1.3.3 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 4 papers)
51% identity, 96% coverage: 9:337/342 of query aligns to 5:336/336 of P08308
- E106 (= E110) mutation E->A,G: Loss of homotropic cooperativity; gain of anabolic activity. Conformational change which modifies the catalytic site. This mutant is blocked in the active R (relaxed) state.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P04391 Ornithine carbamoyltransferase subunit I; OTCase-1; EC 2.1.3.3 from Escherichia coli (strain K12) (see 7 papers)
49% identity, 96% coverage: 7:334/342 of query aligns to 2:332/334 of P04391
- S56 (= S61) mutation to H: Much less active than the wild-type.
- STRT 56:59 (= STRT 61:64) binding carbamoyl phosphate
- R58 (= R63) mutation to G: The mutant is drastically inefficient in catalysis, but affects only moderately the binding of carbamoyl phosphate.
- Q83 (= Q88) binding carbamoyl phosphate
- K87 (= K92) mutation to Q: Much less active than the wild-type.
- R107 (= R112) binding carbamoyl phosphate
- HPTQ 134:137 (= HPTQ 139:142) binding carbamoyl phosphate
- N168 (= N171) binding L-ornithine
- D232 (= D235) binding L-ornithine
- SM 236:237 (= SM 239:240) binding L-ornithine
- C274 (= C277) binding Zn(2+); mutation to A: Zinc ion is no longer a tight-binding inhibitor and does not promote isomerization.
- CL 274:275 (= CL 277:278) binding carbamoyl phosphate
- R320 (= R322) binding carbamoyl phosphate; 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
1duvG Crystal structure of e. Coli ornithine transcarbamoylase complexed with ndelta-l-ornithine-diaminophosphinyl-n-sulphonic acid (psorn) (see paper)
49% identity, 96% coverage: 7:334/342 of query aligns to 1:331/333 of 1duvG
- binding ndelta-(n'-sulphodiaminophosphinyl)-l-ornithine: S55 (= S61), T56 (= T62), R57 (= R63), T58 (= T64), R106 (= R112), L128 (= L134), H133 (= H139), N167 (= N171), D231 (= D235), S235 (= S239), M236 (= M240), C273 (= C277), L274 (= L278), R319 (= R322)
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
49% identity, 96% coverage: 7:334/342 of query aligns to 1:331/333 of 2otcA
- active site: R57 (= R63), T58 (= T64), H85 (≠ K91), R106 (= R112), H133 (= H139), Q136 (= Q142), D231 (= D235), C273 (= C277), R319 (= R322)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S61), T56 (= T62), R57 (= R63), T58 (= T64), R106 (= R112), H133 (= H139), N167 (= N171), D231 (= D235), S235 (= S239), M236 (= M240), L274 (= L278), R319 (= R322)
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
38% identity, 96% coverage: 11:337/342 of query aligns to 7:313/315 of Q51742
- W22 (≠ N26) mutation to A: Decreased heat stability.
- E26 (≠ D30) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ H34) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ L38) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y233) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ W245) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E302) 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
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
37% identity, 96% coverage: 9:336/342 of query aligns to 37:344/354 of P00481
- R92 (= R63) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C277) mutation to S: Increases KM for ornithine 5-fold and decreases kcat 20-fold.
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1othA Crystal structure of human ornithine transcarbamoylase complexed with n-phosphonacetyl-l-ornithine (see paper)
37% identity, 96% coverage: 9:336/342 of query aligns to 4:311/321 of 1othA
- active site: R59 (= R63), T60 (= T64), V87 (≠ K91), R108 (= R112), H135 (= H139), Q138 (= Q142), D230 (= D235), C270 (= C277), R297 (= R322)
- binding n-(phosphonoacetyl)-l-ornithine: S57 (= S61), T58 (= T62), R59 (= R63), T60 (= T64), R108 (= R112), L130 (= L134), H135 (= H139), N166 (= N171), D230 (= D235), S234 (= S239), M235 (= M240), C270 (= C277), L271 (= L278), R297 (= R322)
1c9yA Human ornithine transcarbamylase: crystallographic insights into substrate recognition and catalytic mechanism (see paper)
37% identity, 96% coverage: 9:336/342 of query aligns to 4:311/321 of 1c9yA