SitesBLAST
Comparing 3609401 FitnessBrowser__Dino:3609401 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
52% identity, 83% coverage: 70:482/495 of query aligns to 71:473/485 of 2f2aA
- active site: K79 (= K78), S154 (= S158), S155 (= S159), S173 (≠ T177), T175 (= T179), G176 (= G180), G177 (= G181), S178 (= S182), Q181 (= Q185)
- binding glutamine: G130 (= G129), S154 (= S158), D174 (= D178), T175 (= T179), G176 (= G180), S178 (= S182), F206 (= F210), Y309 (= Y313), Y310 (= Y314), R358 (= R364), D425 (= D433)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
52% identity, 83% coverage: 70:482/495 of query aligns to 71:473/485 of 2dqnA
- active site: K79 (= K78), S154 (= S158), S155 (= S159), S173 (≠ T177), T175 (= T179), G176 (= G180), G177 (= G181), S178 (= S182), Q181 (= Q185)
- binding asparagine: M129 (= M128), G130 (= G129), T175 (= T179), G176 (= G180), S178 (= S182), Y309 (= Y313), Y310 (= Y314), R358 (= R364), D425 (= D433)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
46% identity, 96% coverage: 8:483/495 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K78), S147 (= S158), S148 (= S159), S166 (≠ T177), T168 (= T179), G169 (= G180), G170 (= G181), S171 (= S182), Q174 (= Q185)
- binding glutamine: M122 (= M128), G123 (= G129), D167 (= D178), T168 (= T179), G169 (= G180), G170 (= G181), S171 (= S182), F199 (= F210), Y302 (= Y313), R351 (= R364), D418 (= D433)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
46% identity, 96% coverage: 8:483/495 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K78), S147 (= S158), S148 (= S159), S166 (≠ T177), T168 (= T179), G169 (= G180), G170 (= G181), S171 (= S182), Q174 (= Q185)
- binding asparagine: G123 (= G129), S147 (= S158), G169 (= G180), G170 (= G181), S171 (= S182), Y302 (= Y313), R351 (= R364), D418 (= D433)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 95% coverage: 15:484/495 of query aligns to 4:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 82% coverage: 69:476/495 of query aligns to 29:444/450 of 4n0iA
- active site: K38 (= K78), S116 (= S158), S117 (= S159), T135 (= T177), T137 (= T179), G138 (= G180), G139 (= G181), S140 (= S182), L143 (≠ Q185)
- binding glutamine: G89 (= G129), T137 (= T179), G138 (= G180), S140 (= S182), Y168 (≠ F210), Y271 (= Y313), Y272 (= Y314), R320 (= R364), D404 (= D433)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 96% coverage: 9:483/495 of query aligns to 8:477/487 of 1m21A
- active site: K81 (= K78), S160 (= S158), S161 (= S159), T179 (= T177), T181 (= T179), D182 (≠ G180), G183 (= G181), S184 (= S182), C187 (≠ Q185)
- binding : A129 (= A127), N130 (≠ M128), F131 (≠ G129), C158 (≠ G156), G159 (= G157), S160 (= S158), S184 (= S182), C187 (≠ Q185), I212 (≠ F210), R318 (≠ Y314), L321 (≠ A317), L365 (≠ M366), F426 (≠ D425)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
30% identity, 89% coverage: 54:495/495 of query aligns to 180:601/607 of Q7XJJ7
- K205 (= K78) mutation to A: Loss of activity.
- SS 281:282 (= SS 158:159) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 179:182) binding
- S305 (= S182) mutation to A: Loss of activity.
- R307 (= R184) mutation to A: Loss of activity.
- S360 (≠ H237) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 89% coverage: 54:495/495 of query aligns to 180:601/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ S130), S281 (= S158), G302 (≠ T179), G303 (= G180), S305 (= S182), S472 (≠ T369), I532 (≠ V427), M539 (≠ V434)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 93% coverage: 22:482/495 of query aligns to 16:448/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 99% coverage: 3:493/495 of query aligns to 24:498/507 of Q84DC4
- T31 (≠ A10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K78) mutation to A: Abolishes activity on mandelamide.
- S180 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S159) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G180) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S182) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q185) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ T302) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ D378) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ T438) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 85% coverage: 70:491/495 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K78), S170 (= S158), S171 (= S159), G189 (≠ T177), Q191 (≠ T179), G192 (= G180), G193 (= G181), A194 (≠ S182), I197 (≠ Q185)
- binding benzamide: F145 (≠ M128), S146 (≠ G129), G147 (≠ S130), Q191 (≠ T179), G192 (= G180), G193 (= G181), A194 (≠ S182), W327 (≠ Y313)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 85% coverage: 50:472/495 of query aligns to 61:451/605 of Q936X2
- K91 (= K78) mutation to A: Loss of activity.
- S165 (≠ L153) mutation to A: Loss of activity.
- S189 (= S182) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 95% coverage: 16:485/495 of query aligns to 15:476/490 of 4yjiA
- active site: K79 (= K78), S158 (= S158), S159 (= S159), G179 (≠ T179), G180 (= G180), G181 (= G181), A182 (≠ S182)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L80), G132 (≠ A127), S158 (= S158), G179 (≠ T179), G180 (= G180), A182 (≠ S182)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 84% coverage: 53:466/495 of query aligns to 49:422/461 of 4gysB
- active site: K72 (= K78), S146 (= S158), S147 (= S159), T165 (= T177), T167 (= T179), A168 (≠ G180), G169 (= G181), S170 (= S182), V173 (≠ Q185)
- binding malonate ion: A120 (= A127), G122 (= G129), S146 (= S158), T167 (= T179), A168 (≠ G180), S170 (= S182), S193 (≠ W205), G194 (= G206), V195 (≠ I207), R200 (≠ S212), Y297 (= Y328), R305 (= R336)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
25% identity, 98% coverage: 3:485/495 of query aligns to 1:447/457 of 5h6sC
- active site: K77 (= K78), S152 (= S158), S153 (= S159), L173 (≠ T179), G174 (= G180), G175 (= G181), S176 (= S182)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ G129), W129 (≠ S130), S152 (= S158), L173 (≠ T179), G174 (= G180), S176 (= S182), W306 (≠ Y313), F338 (≠ I367)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
26% identity, 99% coverage: 3:493/495 of query aligns to 1:560/564 of 6te4A
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 88% coverage: 47:484/495 of query aligns to 17:409/412 of 1o9oA
- active site: K62 (= K78), A131 (≠ S158), S132 (= S159), T150 (= T177), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182), R158 (≠ Q185)
- binding 3-amino-3-oxopropanoic acid: G130 (= G157), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182), R158 (≠ Q185), P359 (= P426)
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 31% coverage: 72:223/495 of query aligns to 30:178/425 of Q9FR37
- K36 (= K78) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S158) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S159) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D178) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S182) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ V190) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 88% coverage: 47:484/495 of query aligns to 17:409/412 of 1ocmA
- active site: K62 (= K78), S131 (= S158), S132 (= S159), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182)
- binding pyrophosphate 2-: R113 (≠ S131), S131 (= S158), Q151 (≠ D178), T152 (= T179), G153 (= G180), G154 (= G181), S155 (= S182), R158 (≠ Q185), P359 (= P426)
Query Sequence
>3609401 FitnessBrowser__Dino:3609401
MSELSSLTIAAARDKLRAREITATELTEACLAEVEGAGALGAFVHNTPDLARAQAEAADA
RLAAGDAPAMCGIPLGIKDLFCTKGVPSQAASAILGGFKPEYESTVTSQLFAAGAVMLGK
LNMDEFAMGSSNETSTYGNAVNPWRRGNEDTALTPGGSSGGSASAVAADLCLAATGTDTG
GSIRQPAAFVGITGLKPTYGRCSRWGIVAFASSLDQAGPMTKDVRDCAIMLGAMAGHDPK
DSTSADLPVPDFEAMLTGDIRGKVIGIPKEYRMDGMPEEIEALWSRGAEMLRDAGAELRD
ITLPHTKYALPAYYVIAPAEASSNLARYDGVRFGHRAKLAQGDGITEMYEKTRAEGFGHE
VQRRIMIGTYVLSAGFYDAYYNRARKVRALIKRDFDEVFAAGVDAILTPATPSAAFGLGE
MAEADPVQMYLNDVFTVTVNLAGLPGIAVPAGLDKQGLPLGLQLIGRPWEEGDLLNTAYA
LEQAAGFVAKPNRWW
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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