SitesBLAST
Comparing AZOBR_RS08170 FitnessBrowser__azobra:AZOBR_RS08170 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)
5h8iC Crystal structure of medicago truncatula n-carbamoylputrescine amidohydrolase (mtcpa) in complex with n-(dihydroxymethyl)putrescine (see paper)
65% identity, 99% coverage: 1:296/298 of query aligns to 1:300/301 of 5h8iC
- active site: E48 (= E48), N104 (= N104), K121 (= K121), E132 (= E132), C158 (= C158), A183 (= A183)
- binding (4-azanylbutylamino)methanediol: E48 (= E48), P125 (= P125), Y130 (= Y130), C158 (= C158), W159 (= W159), A183 (= A183), E187 (= E187)
5h8jB Crystal structure of medicago truncatula n-carbamoylputrescine amidohydrolase (mtcpa) in complex with cadaverine (see paper)
66% identity, 98% coverage: 6:296/298 of query aligns to 2:296/297 of 5h8jB
5h8lB Crystal structure of medicago truncatula n-carbamoylputrescine amidohydrolase (mtcpa) c158s mutant in complex with putrescine (see paper)
66% identity, 98% coverage: 6:296/298 of query aligns to 3:297/298 of 5h8lB
3klcB Crystal structure of hyperthermophilic nitrilase (see paper)
32% identity, 93% coverage: 9:284/298 of query aligns to 1:259/261 of 3klcB
- active site: E41 (= E48), N96 (= N104), K112 (= K121), E119 (= E132), C145 (= C158), N170 (≠ A183)
- binding bromide ion: F106 (≠ V115), K109 (≠ V118), E152 (= E165), L171 (≠ I184), M173 (≠ Q196)
- binding magnesium ion: R254 (= R279), E256 (≠ P281)
Sites not aligning to the query:
3klcA Crystal structure of hyperthermophilic nitrilase (see paper)
32% identity, 93% coverage: 9:284/298 of query aligns to 1:259/261 of 3klcA
- active site: E41 (= E48), N96 (= N104), K112 (= K121), E119 (= E132), C145 (= C158), N170 (≠ A183)
- binding bromide ion: E14 (≠ D21), D16 (= D23), K17 (≠ A24), G102 (≠ D110), P103 (≠ A111), R104 (≠ D112), F106 (≠ V115), I107 (≠ L116), G108 (= G117), K109 (≠ V118), L171 (≠ I184), M173 (≠ Q196)
6ypaB The c146a variant of an amidase from pyrococcus horikoshii with bound glutaramide
32% identity, 95% coverage: 3:284/298 of query aligns to 3:267/269 of 6ypaB
- binding pentanediamide: E49 (= E48), K120 (= K121), F124 (≠ G129), E127 (= E132), A153 (≠ C158), F154 (≠ W159), W156 (≠ Q161), N178 (≠ A183), L179 (≠ I184), V180 (≠ S195), M181 (≠ Q196)
Q9UYV8 Nitrilase; PaNit; EC 3.5.5.1 from Pyrococcus abyssi (strain GE5 / Orsay) (see paper)
32% identity, 93% coverage: 9:284/298 of query aligns to 2:260/262 of Q9UYV8
- C146 (= C158) active site, Nucleophile
7ovgA The c146a variant of an amidase from pyrococcus horikoshii with bound acetamide (see paper)
32% identity, 93% coverage: 9:284/298 of query aligns to 3:261/263 of 7ovgA
Q44185 N-carbamoyl-D-amino acid hydrolase; D-N-alpha-carbamilase; EC 3.5.1.77 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see paper)
33% identity, 89% coverage: 22:285/298 of query aligns to 21:299/304 of Q44185
- H129 (= H123) mutation H->A,N,R: No activity.
- H144 (vs. gap) mutation to A: 5% activity of wild-type.
- H215 (≠ A197) mutation to A: 17% activity of wild-type.
Q9NQR4 Omega-amidase NIT2; Nitrilase homolog 2; EC 3.5.1.3 from Homo sapiens (Human) (see 2 papers)
31% identity, 92% coverage: 11:285/298 of query aligns to 6:270/276 of Q9NQR4
- E43 (= E48) mutation to A: Loss of activity using succinamate as substrate.
- K112 (= K121) mutation to A: Loss of activity using succinamate as substrate.
- 116:128 (vs. 125:132, 38% identical) mutation Missing: Less than 3% of wild-type activity using succinamate as substrate.
- C153 (= C158) mutation to A: Loss of activity using succinamate as substrate.
- V231 (≠ L245) to A: in dbSNP:rs17851799
1uf8A Crystal structure of c171a/v236a mutant of n-carbamyl-d-amino acid amidohydrolase complexed with n-carbamyl-d-phenylalanine
33% identity, 87% coverage: 32:290/298 of query aligns to 30:303/303 of 1uf8A
- active site: E46 (= E48), N109 (= N104), K126 (= K121), E145 (= E132), A171 (≠ C158), N196 (vs. gap)
- binding d-[(amino)carbonyl]phenylalanine: E46 (= E48), K126 (= K121), H143 (vs. gap), E145 (= E132), A171 (≠ C158), N172 (≠ W159), R174 (≠ Q161), R175 (≠ W162), N196 (vs. gap)
1uf7A Crystal structure of c171a/v236a mutant of n-carbamyl-d-amino acid amidohydrolase complexed with n-carbamyl-d-valine
33% identity, 87% coverage: 32:290/298 of query aligns to 30:303/303 of 1uf7A
- active site: E46 (= E48), N109 (= N104), K126 (= K121), E145 (= E132), A171 (≠ C158), N196 (vs. gap)
- binding 3-methyl-2-ureido-butyric acid: E46 (= E48), K126 (= K121), P130 (= P125), E145 (= E132), A171 (≠ C158), N172 (≠ W159), R175 (≠ W162), N196 (vs. gap)
1uf5A Crystal structure of c171a/v236a mutant of n-carbamyl-d-amino acid amidohydrolase complexed with n-carbamyl-d-methionine
33% identity, 87% coverage: 32:290/298 of query aligns to 30:303/303 of 1uf5A
- active site: E46 (= E48), N109 (= N104), K126 (= K121), E145 (= E132), A171 (≠ C158), N196 (vs. gap)
- binding 4-methylsulfanyl-2-ureido-butyric acid: E46 (= E48), K126 (= K121), P130 (= P125), E145 (= E132), A171 (≠ C158), N172 (≠ W159), R175 (≠ W162), N196 (vs. gap), T197 (≠ Y180)
Q9UBR1 Beta-ureidopropionase; BUP-1; Beta-alanine synthase; N-carbamoyl-beta-alanine amidohydrolase; EC 3.5.1.6 from Homo sapiens (Human) (see 4 papers)
29% identity, 86% coverage: 29:285/298 of query aligns to 100:366/384 of Q9UBR1
- R130 (≠ D58) mutation to I: Loss of catalytic activity.
- K132 (= K60) mutation to L: Loss of catalytic activity. Forms dimers, but no higher oligomers.
- S208 (≠ K133) mutation to A: Loss of catalytic activity.; mutation to C: Loss of catalytic activity. Forms dimers, but no higher oligomers.; mutation to R: Loss of catalytic activity. Forms dimers, but no higher oligomers.
- C233 (= C158) active site, Nucleophile; mutation to A: Loss of catalytic activity.
- G235 (≠ D160) to R: in UPB1D; complete loss of activity; dbSNP:rs766196011
- R236 (≠ Q161) to W: in UPB1D; complete loss of activity; dbSNP:rs144135211
- S264 (= S195) to R: in UPB1D; complete loss of activity
- E271 (≠ V202) to K: in UPB1D; complete loss of activity; abolishes formation of higher oligomers; dbSNP:rs747454154
- I286 (≠ S217) to T: in UPB1D; unknown pathological significance; mildly reduced enzyme activity; no effect on formation of higher oligomers; dbSNP:rs200034079
- T299 (vs. gap) mutation to C: Loss of catalytic activity. Forms dimers, but no higher oligomers.
- R326 (≠ L245) to Q: in UPB1D; complete loss of activity; abolishes formation of higher oligomers; dbSNP:rs118163237
- T359 (≠ D278) to M: in UPB1D; complete loss of activity; dbSNP:rs369879221
Sites not aligning to the query:
- 13 L → S: in UPB1D; strongly reduced activity; reduced formation of higher oligomers; dbSNP:rs200688546
- 85 A → E: in UPB1D; complete loss of activity; dbSNP:rs34035085
Q964D8 Beta-ureidopropionase; Beta-alanine synthase; N-carbamoyl-beta-alanine amidohydrolase; EC 3.5.1.6 from Dictyostelium discoideum (Social amoeba)
26% identity, 88% coverage: 29:289/298 of query aligns to 103:373/391 of Q964D8
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
Q94JV5 Deaminated glutathione amidase, chloroplastic/cytosolic; dGSH amidase; Nitrilase-like protein 2; Protein nitrilase 1 homolog; AtNit1; Protein Nit1 homolog; EC 3.5.1.128 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 94% coverage: 1:279/298 of query aligns to 29:302/307 of Q94JV5